Full text data of C1R
C1R
[Confidence: low (only semi-automatic identification from reviews)]
Complement C1r subcomponent; 3.4.21.41 (Complement component 1 subcomponent r; Complement C1r subcomponent heavy chain; Complement C1r subcomponent light chain; Flags: Precursor)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Complement C1r subcomponent; 3.4.21.41 (Complement component 1 subcomponent r; Complement C1r subcomponent heavy chain; Complement C1r subcomponent light chain; Flags: Precursor)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P00736
ID C1R_HUMAN Reviewed; 705 AA.
AC P00736; A6NJQ8; Q68D77; Q8J012;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
read moreDT 16-DEC-2008, sequence version 2.
DT 22-JAN-2014, entry version 174.
DE RecName: Full=Complement C1r subcomponent;
DE EC=3.4.21.41;
DE AltName: Full=Complement component 1 subcomponent r;
DE Contains:
DE RecName: Full=Complement C1r subcomponent heavy chain;
DE Contains:
DE RecName: Full=Complement C1r subcomponent light chain;
DE Flags: Precursor;
GN Name=C1R;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ARG-186.
RX PubMed=3021205; DOI=10.1021/bi00365a020;
RA Leytus S.P., Kurachi K., Sakariassen K.S., Davie E.W.;
RT "Nucleotide sequence of the cDNA coding for human complement C1r.";
RL Biochemistry 25:4855-4863(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS LEU-152 AND ARG-186.
RX PubMed=3030286;
RA Journet A., Tosi M.;
RT "Cloning and sequencing of full-length cDNA encoding the precursor of
RT human complement component C1r.";
RL Biochem. J. 240:783-787(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS HIS-131; LEU-152;
RP TYR-163; LYS-184; ARG-186 AND ARG-261.
RX PubMed=12914573; DOI=10.1046/j.1469-1809.2003.00019.x;
RA Nakagawa M., Yuasa I., Irizawa Y., Umetsu K.;
RT "The human complement component C1R gene: the exon-intron structure
RT and the molecular basis of allelic diversity.";
RL Ann. Hum. Genet. 67:207-215(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon endothelium;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
RA Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
RA Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
RA Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
RA Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
RA Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
RA Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
RA Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
RA Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
RA Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
RA Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
RA Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
RA Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
RA Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
RA Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
RA Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
RA Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
RA Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
RA Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
RA Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
RA Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
RA Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
RA Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
RA Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
RA Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
RA Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
RA Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
RA Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
RA Kucherlapati R., Weinstock G., Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS LEU-152 AND
RP ARG-186.
RC TISSUE=Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP PROTEIN SEQUENCE OF 18-463.
RX PubMed=3036070;
RA Arlaud G.J., Willis A.C., Gagnon J.;
RT "Complete amino acid sequence of the A chain of human complement-
RT classical-pathway enzyme C1r.";
RL Biochem. J. 241:711-720(1987).
RN [8]
RP PROTEIN SEQUENCE OF 464-705.
RX PubMed=6303394; DOI=10.1021/bi00277a003;
RA Arlaud G.J., Gagnon J.;
RT "Complete amino acid sequence of the catalytic chain of human
RT complement subcomponent C1-r.";
RL Biochemistry 22:1758-1764(1983).
RN [9]
RP PROTEIN SEQUENCE OF 152-186, AND HYDROXYLATION.
RX PubMed=2820791; DOI=10.1016/0014-5793(87)80205-3;
RA Arlaud G.J., van Dorsselaer A., Bell A., Mancini M., Aude C.,
RA Gagnon J.;
RT "Identification of erythro-beta-hydroxyasparagine in the EGF-like
RT domain of human C1r.";
RL FEBS Lett. 222:129-134(1987).
RN [10]
RP PROTEIN SEQUENCE OF 133-137; 187-211 AND 609-613, AND PHOSPHORYLATION
RP AT SER-206 BY CK2.
RX PubMed=8635594; DOI=10.1016/0014-5793(96)00403-6;
RA Pelloux S., Thielens N.M., Hudry-Clergeon G., Petillot Y., Filhol O.,
RA Arlaud G.J.;
RT "Identification of a cryptic protein kinase CK2 phosphorylation site
RT in human complement protease Clr, and its use to probe intramolecular
RT interaction.";
RL FEBS Lett. 386:15-20(1996).
RN [11]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-125; ASN-221 AND ASN-514,
RP AND MASS SPECTROMETRY.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
RA Moore R.J., Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [12]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-514, AND MASS
RP SPECTROMETRY.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of
RT multiple enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [13]
RP STRUCTURE BY NMR OF 140-192.
RX PubMed=9477945; DOI=10.1021/bi971851v;
RA Bersch B., Hernandez J.-F., Marion D., Arlaud G.J.;
RT "Solution structure of the epidermal growth factor (EGF)-like module
RT of human complement protease C1r, an atypical member of the EGF
RT family.";
RL Biochemistry 37:1204-1214(1998).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 307-702.
RX PubMed=11823416; DOI=10.1093/emboj/21.3.231;
RA Budayova-Spano M., Lacroix M., Thielens N.M., Arlaud G.J.,
RA Fontecilla-Camps J.-C., Gaboriaud C.;
RT "The crystal structure of the zymogen catalytic domain of complement
RT protease C1r reveals that a disruptive mechanical stress is required
RT to trigger activation of the C1 complex.";
RL EMBO J. 21:231-239(2002).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 375-702.
RX PubMed=12429092; DOI=10.1016/S0969-2126(02)00881-X;
RA Budayova-Spano M., Grabarse W., Thielens N.M., Hillen H., Lacroix M.,
RA Schmidt M., Fontecilla-Camps J.-C., Arlaud G.J., Gaboriaud C.;
RT "Monomeric structures of the zymogen and active catalytic domain of
RT complement protease c1r: further insights into the c1 activation
RT mechanism.";
RL Structure 10:1509-1519(2002).
RN [16]
RP VARIANT LEU-152.
RX PubMed=8162045; DOI=10.1093/hmg/3.1.217-a;
RA Nothen M.M., Dewald G.;
RT "A common amino acid polymorphism in complement component C1R.";
RL Hum. Mol. Genet. 3:217-217(1994).
RN [17]
RP VARIANTS LYS-184 AND ARG-261, AND MASS SPECTROMETRY.
RX PubMed=22028381; DOI=10.1093/jmcb/mjr024;
RA Su Z.D., Sun L., Yu D.X., Li R.X., Li H.X., Yu Z.J., Sheng Q.H.,
RA Lin X., Zeng R., Wu J.R.;
RT "Quantitative detection of single amino acid polymorphisms by targeted
RT proteomics.";
RL J. Mol. Cell Biol. 3:309-315(2011).
CC -!- FUNCTION: C1r B chain is a serine protease that combines with C1q
CC and C1s to form C1, the first component of the classical pathway
CC of the complement system.
CC -!- CATALYTIC ACTIVITY: Selective cleavage of Lys(or Arg)-|-Ile bond
CC in complement subcomponent C1s to form the active form of C1s
CC (EC 3.4.21.42).
CC -!- SUBUNIT: C1 is a calcium-dependent trimolecular complex of C1q,
CC C1r and C1s in the molar ration of 1:2:2. C1r is a dimer of
CC identical chains, each of which is activated by cleavage into two
CC chains, A and B, connected by disulfide bonds.
CC -!- INTERACTION:
CC P09871:C1S; NbExp=3; IntAct=EBI-3926504, EBI-2810045;
CC -!- PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of
CC aspartate and asparagine is (R) stereospecific within EGF domains.
CC -!- POLYMORPHISM: Complement component C1r deficiency [MIM:216950]
CC leads to the failure of the classical complement system activation
CC pathway (C1 deficiency). Individuals with C1 deficiency are highly
CC susceptible to infections by microorganisms and have greater risk
CC in developing autoimmune diseases such as systemic lupus
CC erythematosus (SLE).
CC -!- SIMILARITY: Belongs to the peptidase S1 family.
CC -!- SIMILARITY: Contains 2 CUB domains.
CC -!- SIMILARITY: Contains 1 EGF-like domain.
CC -!- SIMILARITY: Contains 1 peptidase S1 domain.
CC -!- SIMILARITY: Contains 2 Sushi (CCP/SCR) domains.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; M14058; AAA51851.1; -; mRNA.
DR EMBL; X04701; CAA28407.1; -; mRNA.
DR EMBL; AB083037; BAC19850.2; -; Genomic_DNA.
DR EMBL; AC094008; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC140077; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR749540; CAH18343.1; -; mRNA.
DR EMBL; BC035220; AAH35220.1; -; mRNA.
DR PIR; A24170; C1HURB.
DR RefSeq; NP_001724.3; NM_001733.4.
DR UniGene; Hs.524224; -.
DR PDB; 1APQ; NMR; -; A=140-192.
DR PDB; 1GPZ; X-ray; 2.90 A; A/B=307-705.
DR PDB; 1MD7; X-ray; 3.20 A; A=375-702.
DR PDB; 1MD8; X-ray; 2.80 A; A=375-703.
DR PDB; 2QY0; X-ray; 2.60 A; A/C=309-463, B/D=464-705.
DR PDBsum; 1APQ; -.
DR PDBsum; 1GPZ; -.
DR PDBsum; 1MD7; -.
DR PDBsum; 1MD8; -.
DR PDBsum; 2QY0; -.
DR DisProt; DP00621; -.
DR ProteinModelPortal; P00736; -.
DR SMR; P00736; 25-302, 307-703.
DR IntAct; P00736; 3.
DR MINT; MINT-8045732; -.
DR STRING; 9606.ENSP00000290575; -.
DR BindingDB; P00736; -.
DR ChEMBL; CHEMBL4611; -.
DR DrugBank; DB00054; Abciximab.
DR DrugBank; DB00051; Adalimumab.
DR DrugBank; DB00092; Alefacept.
DR DrugBank; DB00087; Alemtuzumab.
DR DrugBank; DB00074; Basiliximab.
DR DrugBank; DB00112; Bevacizumab.
DR DrugBank; DB00002; Cetuximab.
DR DrugBank; DB00111; Daclizumab.
DR DrugBank; DB00095; Efalizumab.
DR DrugBank; DB00005; Etanercept.
DR DrugBank; DB00056; Gemtuzumab ozogamicin.
DR DrugBank; DB00078; Ibritumomab.
DR DrugBank; DB00028; Immune globulin.
DR DrugBank; DB00075; Muromonab.
DR DrugBank; DB00108; Natalizumab.
DR DrugBank; DB00110; Palivizumab.
DR DrugBank; DB00073; Rituximab.
DR DrugBank; DB00081; Tositumomab.
DR DrugBank; DB00072; Trastuzumab.
DR MEROPS; S01.192; -.
DR PhosphoSite; P00736; -.
DR DMDM; 218511956; -.
DR PaxDb; P00736; -.
DR PeptideAtlas; P00736; -.
DR PRIDE; P00736; -.
DR DNASU; 715; -.
DR Ensembl; ENST00000290575; ENSP00000290575; ENSG00000159403.
DR GeneID; 715; -.
DR KEGG; hsa:715; -.
DR CTD; 715; -.
DR GeneCards; GC12M007187; -.
DR HGNC; HGNC:1246; C1R.
DR HPA; HPA001551; -.
DR MIM; 216950; phenotype.
DR MIM; 613785; gene.
DR neXtProt; NX_P00736; -.
DR Orphanet; 169147; Immunodeficiency due to an early component of complement deficiency.
DR PharmGKB; PA25635; -.
DR eggNOG; COG5640; -.
DR HOVERGEN; HBG000559; -.
DR KO; K01330; -.
DR OrthoDB; EOG7W6WK4; -.
DR Reactome; REACT_6900; Immune System.
DR ChiTaRS; C1R; human.
DR EvolutionaryTrace; P00736; -.
DR GeneWiki; C1R_(gene); -.
DR GenomeRNAi; 715; -.
DR NextBio; 2906; -.
DR PRO; PR:P00736; -.
DR Bgee; P00736; -.
DR CleanEx; HS_C1R; -.
DR Genevestigator; P00736; -.
DR GO; GO:0005576; C:extracellular region; NAS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; EXP:Reactome.
DR GO; GO:0006958; P:complement activation, classical pathway; TAS:Reactome.
DR GO; GO:0045087; P:innate immune response; TAS:Reactome.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.60.120.290; -; 2.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR013032; EGF-like_CS.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR024175; Pept_S1A_C1r/C1S/mannan-bd.
DR InterPro; IPR001254; Peptidase_S1.
DR InterPro; IPR018114; Peptidase_S1_AS.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR000436; Sushi_SCR_CCP.
DR InterPro; IPR009003; Trypsin-like_Pept_dom.
DR Pfam; PF00431; CUB; 2.
DR Pfam; PF00084; Sushi; 2.
DR Pfam; PF00089; Trypsin; 1.
DR PIRSF; PIRSF001155; C1r_C1s_MASP; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00032; CCP; 2.
DR SMART; SM00042; CUB; 2.
DR SMART; SM00179; EGF_CA; 1.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF49854; SSF49854; 2.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF57535; SSF57535; 2.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS01180; CUB; 2.
DR PROSITE; PS00022; EGF_1; FALSE_NEG.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; FALSE_NEG.
DR PROSITE; PS01187; EGF_CA; 1.
DR PROSITE; PS50923; SUSHI; 2.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; FALSE_NEG.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Complement pathway; Complete proteome;
KW Direct protein sequencing; Disulfide bond; EGF-like domain;
KW Glycoprotein; Hydrolase; Hydroxylation; Immunity; Innate immunity;
KW Phosphoprotein; Polymorphism; Protease; Reference proteome; Repeat;
KW Serine protease; Signal; Sushi.
FT SIGNAL 1 17
FT CHAIN 18 705 Complement C1r subcomponent.
FT /FTId=PRO_0000027577.
FT CHAIN 18 463 Complement C1r subcomponent heavy chain.
FT /FTId=PRO_0000027578.
FT CHAIN 464 705 Complement C1r subcomponent light chain.
FT /FTId=PRO_0000027579.
FT DOMAIN 18 141 CUB 1.
FT DOMAIN 142 190 EGF-like; calcium-binding (Potential).
FT DOMAIN 193 305 CUB 2.
FT DOMAIN 307 373 Sushi 1.
FT DOMAIN 374 449 Sushi 2.
FT DOMAIN 464 702 Peptidase S1.
FT ACT_SITE 502 502 Charge relay system.
FT ACT_SITE 557 557 Charge relay system.
FT ACT_SITE 654 654 Charge relay system.
FT MOD_RES 167 167 (3R)-3-hydroxyasparagine.
FT MOD_RES 206 206 Phosphoserine; by CK2.
FT CARBOHYD 125 125 N-linked (GlcNAc...).
FT CARBOHYD 221 221 N-linked (GlcNAc...).
FT CARBOHYD 514 514 N-linked (GlcNAc...).
FT CARBOHYD 581 581 N-linked (GlcNAc...).
FT DISULFID 71 89 Probable.
FT DISULFID 146 165
FT DISULFID 161 174
FT DISULFID 176 189
FT DISULFID 193 220 Probable.
FT DISULFID 250 268 Probable.
FT DISULFID 309 358
FT DISULFID 338 371
FT DISULFID 376 429
FT DISULFID 406 447
FT DISULFID 451 577 Interchain (between heavy and light
FT chains).
FT DISULFID 620 639
FT DISULFID 650 680
FT VARIANT 131 131 Y -> H.
FT /FTId=VAR_018667.
FT VARIANT 152 152 S -> L (common polymorphism;
FT dbSNP:rs1801046).
FT /FTId=VAR_016103.
FT VARIANT 163 163 H -> Y.
FT /FTId=VAR_018668.
FT VARIANT 184 184 E -> K (polymorphism confirmed at protein
FT level; dbSNP:rs1126605).
FT /FTId=VAR_018669.
FT VARIANT 186 186 T -> R (in dbSNP:rs4519167).
FT /FTId=VAR_047933.
FT VARIANT 261 261 G -> R (polymorphism confirmed at protein
FT level; dbSNP:rs3813728).
FT /FTId=VAR_018670.
FT TURN 145 147
FT TURN 150 152
FT STRAND 156 158
FT STRAND 162 168
FT STRAND 171 175
FT STRAND 319 322
FT STRAND 326 328
FT STRAND 333 338
FT STRAND 342 346
FT STRAND 349 352
FT STRAND 355 358
FT STRAND 364 366
FT STRAND 370 373
FT STRAND 385 392
FT STRAND 401 406
FT TURN 408 410
FT STRAND 411 413
FT STRAND 426 429
FT STRAND 433 437
FT TURN 438 440
FT STRAND 447 449
FT STRAND 478 492
FT TURN 493 495
FT STRAND 496 499
FT HELIX 501 504
FT STRAND 518 522
FT HELIX 526 532
FT STRAND 537 542
FT STRAND 548 552
FT STRAND 559 565
FT STRAND 571 573
FT HELIX 582 585
FT STRAND 590 595
FT STRAND 600 602
FT STRAND 608 614
FT HELIX 617 626
FT STRAND 637 641
FT HELIX 643 650
FT TURN 651 655
FT STRAND 657 661
FT TURN 663 665
FT STRAND 668 676
FT STRAND 678 683
FT STRAND 685 689
FT HELIX 690 693
FT HELIX 694 700
SQ SEQUENCE 705 AA; 80119 MW; B45D120201061462 CRC64;
MWLLYLLVPA LFCRAGGSIP IPQKLFGEVT SPLFPKPYPN NFETTTVITV PTGYRVKLVF
QQFDLEPSEG CFYDYVKISA DKKSLGRFCG QLGSPLGNPP GKKEFMSQGN KMLLTFHTDF
SNEENGTIMF YKGFLAYYQA VDLDECASRS KSGEEDPQPQ CQHLCHNYVG GYFCSCRPGY
ELQEDTHSCQ AECSSELYTE ASGYISSLEY PRSYPPDLRC NYSIRVERGL TLHLKFLEPF
DIDDHQQVHC PYDQLQIYAN GKNIGEFCGK QRPPDLDTSS NAVDLLFFTD ESGDSRGWKL
RYTTEIIKCP QPKTLDEFTI IQNLQPQYQF RDYFIATCKQ GYQLIEGNQV LHSFTAVCQD
DGTWHRAMPR CKIKDCGQPR NLPNGDFRYT TTMGVNTYKA RIQYYCHEPY YKMQTRAGSR
ESEQGVYTCT AQGIWKNEQK GEKIPRCLPV CGKPVNPVEQ RQRIIGGQKA KMGNFPWQVF
TNIHGRGGGA LLGDRWILTA AHTLYPKEHE AQSNASLDVF LGHTNVEELM KLGNHPIRRV
SVHPDYRQDE SYNFEGDIAL LELENSVTLG PNLLPICLPD NDTFYDLGLM GYVSGFGVME
EKIAHDLRFV RLPVANPQAC ENWLRGKNRM DVFSQNMFCA GHPSLKQDAC QGDSGGVFAV
RDPNTDRWVA TGIVSWGIGC SRGYGFYTKV LNYVDWIKKE MEEED
//
ID C1R_HUMAN Reviewed; 705 AA.
AC P00736; A6NJQ8; Q68D77; Q8J012;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
read moreDT 16-DEC-2008, sequence version 2.
DT 22-JAN-2014, entry version 174.
DE RecName: Full=Complement C1r subcomponent;
DE EC=3.4.21.41;
DE AltName: Full=Complement component 1 subcomponent r;
DE Contains:
DE RecName: Full=Complement C1r subcomponent heavy chain;
DE Contains:
DE RecName: Full=Complement C1r subcomponent light chain;
DE Flags: Precursor;
GN Name=C1R;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ARG-186.
RX PubMed=3021205; DOI=10.1021/bi00365a020;
RA Leytus S.P., Kurachi K., Sakariassen K.S., Davie E.W.;
RT "Nucleotide sequence of the cDNA coding for human complement C1r.";
RL Biochemistry 25:4855-4863(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS LEU-152 AND ARG-186.
RX PubMed=3030286;
RA Journet A., Tosi M.;
RT "Cloning and sequencing of full-length cDNA encoding the precursor of
RT human complement component C1r.";
RL Biochem. J. 240:783-787(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS HIS-131; LEU-152;
RP TYR-163; LYS-184; ARG-186 AND ARG-261.
RX PubMed=12914573; DOI=10.1046/j.1469-1809.2003.00019.x;
RA Nakagawa M., Yuasa I., Irizawa Y., Umetsu K.;
RT "The human complement component C1R gene: the exon-intron structure
RT and the molecular basis of allelic diversity.";
RL Ann. Hum. Genet. 67:207-215(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon endothelium;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
RA Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
RA Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
RA Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
RA Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
RA Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
RA Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
RA Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
RA Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
RA Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
RA Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
RA Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
RA Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
RA Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
RA Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
RA Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
RA Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
RA Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
RA Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
RA Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
RA Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
RA Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
RA Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
RA Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
RA Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
RA Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
RA Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
RA Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
RA Kucherlapati R., Weinstock G., Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS LEU-152 AND
RP ARG-186.
RC TISSUE=Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP PROTEIN SEQUENCE OF 18-463.
RX PubMed=3036070;
RA Arlaud G.J., Willis A.C., Gagnon J.;
RT "Complete amino acid sequence of the A chain of human complement-
RT classical-pathway enzyme C1r.";
RL Biochem. J. 241:711-720(1987).
RN [8]
RP PROTEIN SEQUENCE OF 464-705.
RX PubMed=6303394; DOI=10.1021/bi00277a003;
RA Arlaud G.J., Gagnon J.;
RT "Complete amino acid sequence of the catalytic chain of human
RT complement subcomponent C1-r.";
RL Biochemistry 22:1758-1764(1983).
RN [9]
RP PROTEIN SEQUENCE OF 152-186, AND HYDROXYLATION.
RX PubMed=2820791; DOI=10.1016/0014-5793(87)80205-3;
RA Arlaud G.J., van Dorsselaer A., Bell A., Mancini M., Aude C.,
RA Gagnon J.;
RT "Identification of erythro-beta-hydroxyasparagine in the EGF-like
RT domain of human C1r.";
RL FEBS Lett. 222:129-134(1987).
RN [10]
RP PROTEIN SEQUENCE OF 133-137; 187-211 AND 609-613, AND PHOSPHORYLATION
RP AT SER-206 BY CK2.
RX PubMed=8635594; DOI=10.1016/0014-5793(96)00403-6;
RA Pelloux S., Thielens N.M., Hudry-Clergeon G., Petillot Y., Filhol O.,
RA Arlaud G.J.;
RT "Identification of a cryptic protein kinase CK2 phosphorylation site
RT in human complement protease Clr, and its use to probe intramolecular
RT interaction.";
RL FEBS Lett. 386:15-20(1996).
RN [11]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-125; ASN-221 AND ASN-514,
RP AND MASS SPECTROMETRY.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
RA Moore R.J., Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [12]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-514, AND MASS
RP SPECTROMETRY.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of
RT multiple enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [13]
RP STRUCTURE BY NMR OF 140-192.
RX PubMed=9477945; DOI=10.1021/bi971851v;
RA Bersch B., Hernandez J.-F., Marion D., Arlaud G.J.;
RT "Solution structure of the epidermal growth factor (EGF)-like module
RT of human complement protease C1r, an atypical member of the EGF
RT family.";
RL Biochemistry 37:1204-1214(1998).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 307-702.
RX PubMed=11823416; DOI=10.1093/emboj/21.3.231;
RA Budayova-Spano M., Lacroix M., Thielens N.M., Arlaud G.J.,
RA Fontecilla-Camps J.-C., Gaboriaud C.;
RT "The crystal structure of the zymogen catalytic domain of complement
RT protease C1r reveals that a disruptive mechanical stress is required
RT to trigger activation of the C1 complex.";
RL EMBO J. 21:231-239(2002).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 375-702.
RX PubMed=12429092; DOI=10.1016/S0969-2126(02)00881-X;
RA Budayova-Spano M., Grabarse W., Thielens N.M., Hillen H., Lacroix M.,
RA Schmidt M., Fontecilla-Camps J.-C., Arlaud G.J., Gaboriaud C.;
RT "Monomeric structures of the zymogen and active catalytic domain of
RT complement protease c1r: further insights into the c1 activation
RT mechanism.";
RL Structure 10:1509-1519(2002).
RN [16]
RP VARIANT LEU-152.
RX PubMed=8162045; DOI=10.1093/hmg/3.1.217-a;
RA Nothen M.M., Dewald G.;
RT "A common amino acid polymorphism in complement component C1R.";
RL Hum. Mol. Genet. 3:217-217(1994).
RN [17]
RP VARIANTS LYS-184 AND ARG-261, AND MASS SPECTROMETRY.
RX PubMed=22028381; DOI=10.1093/jmcb/mjr024;
RA Su Z.D., Sun L., Yu D.X., Li R.X., Li H.X., Yu Z.J., Sheng Q.H.,
RA Lin X., Zeng R., Wu J.R.;
RT "Quantitative detection of single amino acid polymorphisms by targeted
RT proteomics.";
RL J. Mol. Cell Biol. 3:309-315(2011).
CC -!- FUNCTION: C1r B chain is a serine protease that combines with C1q
CC and C1s to form C1, the first component of the classical pathway
CC of the complement system.
CC -!- CATALYTIC ACTIVITY: Selective cleavage of Lys(or Arg)-|-Ile bond
CC in complement subcomponent C1s to form the active form of C1s
CC (EC 3.4.21.42).
CC -!- SUBUNIT: C1 is a calcium-dependent trimolecular complex of C1q,
CC C1r and C1s in the molar ration of 1:2:2. C1r is a dimer of
CC identical chains, each of which is activated by cleavage into two
CC chains, A and B, connected by disulfide bonds.
CC -!- INTERACTION:
CC P09871:C1S; NbExp=3; IntAct=EBI-3926504, EBI-2810045;
CC -!- PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of
CC aspartate and asparagine is (R) stereospecific within EGF domains.
CC -!- POLYMORPHISM: Complement component C1r deficiency [MIM:216950]
CC leads to the failure of the classical complement system activation
CC pathway (C1 deficiency). Individuals with C1 deficiency are highly
CC susceptible to infections by microorganisms and have greater risk
CC in developing autoimmune diseases such as systemic lupus
CC erythematosus (SLE).
CC -!- SIMILARITY: Belongs to the peptidase S1 family.
CC -!- SIMILARITY: Contains 2 CUB domains.
CC -!- SIMILARITY: Contains 1 EGF-like domain.
CC -!- SIMILARITY: Contains 1 peptidase S1 domain.
CC -!- SIMILARITY: Contains 2 Sushi (CCP/SCR) domains.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; M14058; AAA51851.1; -; mRNA.
DR EMBL; X04701; CAA28407.1; -; mRNA.
DR EMBL; AB083037; BAC19850.2; -; Genomic_DNA.
DR EMBL; AC094008; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC140077; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR749540; CAH18343.1; -; mRNA.
DR EMBL; BC035220; AAH35220.1; -; mRNA.
DR PIR; A24170; C1HURB.
DR RefSeq; NP_001724.3; NM_001733.4.
DR UniGene; Hs.524224; -.
DR PDB; 1APQ; NMR; -; A=140-192.
DR PDB; 1GPZ; X-ray; 2.90 A; A/B=307-705.
DR PDB; 1MD7; X-ray; 3.20 A; A=375-702.
DR PDB; 1MD8; X-ray; 2.80 A; A=375-703.
DR PDB; 2QY0; X-ray; 2.60 A; A/C=309-463, B/D=464-705.
DR PDBsum; 1APQ; -.
DR PDBsum; 1GPZ; -.
DR PDBsum; 1MD7; -.
DR PDBsum; 1MD8; -.
DR PDBsum; 2QY0; -.
DR DisProt; DP00621; -.
DR ProteinModelPortal; P00736; -.
DR SMR; P00736; 25-302, 307-703.
DR IntAct; P00736; 3.
DR MINT; MINT-8045732; -.
DR STRING; 9606.ENSP00000290575; -.
DR BindingDB; P00736; -.
DR ChEMBL; CHEMBL4611; -.
DR DrugBank; DB00054; Abciximab.
DR DrugBank; DB00051; Adalimumab.
DR DrugBank; DB00092; Alefacept.
DR DrugBank; DB00087; Alemtuzumab.
DR DrugBank; DB00074; Basiliximab.
DR DrugBank; DB00112; Bevacizumab.
DR DrugBank; DB00002; Cetuximab.
DR DrugBank; DB00111; Daclizumab.
DR DrugBank; DB00095; Efalizumab.
DR DrugBank; DB00005; Etanercept.
DR DrugBank; DB00056; Gemtuzumab ozogamicin.
DR DrugBank; DB00078; Ibritumomab.
DR DrugBank; DB00028; Immune globulin.
DR DrugBank; DB00075; Muromonab.
DR DrugBank; DB00108; Natalizumab.
DR DrugBank; DB00110; Palivizumab.
DR DrugBank; DB00073; Rituximab.
DR DrugBank; DB00081; Tositumomab.
DR DrugBank; DB00072; Trastuzumab.
DR MEROPS; S01.192; -.
DR PhosphoSite; P00736; -.
DR DMDM; 218511956; -.
DR PaxDb; P00736; -.
DR PeptideAtlas; P00736; -.
DR PRIDE; P00736; -.
DR DNASU; 715; -.
DR Ensembl; ENST00000290575; ENSP00000290575; ENSG00000159403.
DR GeneID; 715; -.
DR KEGG; hsa:715; -.
DR CTD; 715; -.
DR GeneCards; GC12M007187; -.
DR HGNC; HGNC:1246; C1R.
DR HPA; HPA001551; -.
DR MIM; 216950; phenotype.
DR MIM; 613785; gene.
DR neXtProt; NX_P00736; -.
DR Orphanet; 169147; Immunodeficiency due to an early component of complement deficiency.
DR PharmGKB; PA25635; -.
DR eggNOG; COG5640; -.
DR HOVERGEN; HBG000559; -.
DR KO; K01330; -.
DR OrthoDB; EOG7W6WK4; -.
DR Reactome; REACT_6900; Immune System.
DR ChiTaRS; C1R; human.
DR EvolutionaryTrace; P00736; -.
DR GeneWiki; C1R_(gene); -.
DR GenomeRNAi; 715; -.
DR NextBio; 2906; -.
DR PRO; PR:P00736; -.
DR Bgee; P00736; -.
DR CleanEx; HS_C1R; -.
DR Genevestigator; P00736; -.
DR GO; GO:0005576; C:extracellular region; NAS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; EXP:Reactome.
DR GO; GO:0006958; P:complement activation, classical pathway; TAS:Reactome.
DR GO; GO:0045087; P:innate immune response; TAS:Reactome.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.60.120.290; -; 2.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR013032; EGF-like_CS.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR024175; Pept_S1A_C1r/C1S/mannan-bd.
DR InterPro; IPR001254; Peptidase_S1.
DR InterPro; IPR018114; Peptidase_S1_AS.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR000436; Sushi_SCR_CCP.
DR InterPro; IPR009003; Trypsin-like_Pept_dom.
DR Pfam; PF00431; CUB; 2.
DR Pfam; PF00084; Sushi; 2.
DR Pfam; PF00089; Trypsin; 1.
DR PIRSF; PIRSF001155; C1r_C1s_MASP; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00032; CCP; 2.
DR SMART; SM00042; CUB; 2.
DR SMART; SM00179; EGF_CA; 1.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF49854; SSF49854; 2.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF57535; SSF57535; 2.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS01180; CUB; 2.
DR PROSITE; PS00022; EGF_1; FALSE_NEG.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; FALSE_NEG.
DR PROSITE; PS01187; EGF_CA; 1.
DR PROSITE; PS50923; SUSHI; 2.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; FALSE_NEG.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Complement pathway; Complete proteome;
KW Direct protein sequencing; Disulfide bond; EGF-like domain;
KW Glycoprotein; Hydrolase; Hydroxylation; Immunity; Innate immunity;
KW Phosphoprotein; Polymorphism; Protease; Reference proteome; Repeat;
KW Serine protease; Signal; Sushi.
FT SIGNAL 1 17
FT CHAIN 18 705 Complement C1r subcomponent.
FT /FTId=PRO_0000027577.
FT CHAIN 18 463 Complement C1r subcomponent heavy chain.
FT /FTId=PRO_0000027578.
FT CHAIN 464 705 Complement C1r subcomponent light chain.
FT /FTId=PRO_0000027579.
FT DOMAIN 18 141 CUB 1.
FT DOMAIN 142 190 EGF-like; calcium-binding (Potential).
FT DOMAIN 193 305 CUB 2.
FT DOMAIN 307 373 Sushi 1.
FT DOMAIN 374 449 Sushi 2.
FT DOMAIN 464 702 Peptidase S1.
FT ACT_SITE 502 502 Charge relay system.
FT ACT_SITE 557 557 Charge relay system.
FT ACT_SITE 654 654 Charge relay system.
FT MOD_RES 167 167 (3R)-3-hydroxyasparagine.
FT MOD_RES 206 206 Phosphoserine; by CK2.
FT CARBOHYD 125 125 N-linked (GlcNAc...).
FT CARBOHYD 221 221 N-linked (GlcNAc...).
FT CARBOHYD 514 514 N-linked (GlcNAc...).
FT CARBOHYD 581 581 N-linked (GlcNAc...).
FT DISULFID 71 89 Probable.
FT DISULFID 146 165
FT DISULFID 161 174
FT DISULFID 176 189
FT DISULFID 193 220 Probable.
FT DISULFID 250 268 Probable.
FT DISULFID 309 358
FT DISULFID 338 371
FT DISULFID 376 429
FT DISULFID 406 447
FT DISULFID 451 577 Interchain (between heavy and light
FT chains).
FT DISULFID 620 639
FT DISULFID 650 680
FT VARIANT 131 131 Y -> H.
FT /FTId=VAR_018667.
FT VARIANT 152 152 S -> L (common polymorphism;
FT dbSNP:rs1801046).
FT /FTId=VAR_016103.
FT VARIANT 163 163 H -> Y.
FT /FTId=VAR_018668.
FT VARIANT 184 184 E -> K (polymorphism confirmed at protein
FT level; dbSNP:rs1126605).
FT /FTId=VAR_018669.
FT VARIANT 186 186 T -> R (in dbSNP:rs4519167).
FT /FTId=VAR_047933.
FT VARIANT 261 261 G -> R (polymorphism confirmed at protein
FT level; dbSNP:rs3813728).
FT /FTId=VAR_018670.
FT TURN 145 147
FT TURN 150 152
FT STRAND 156 158
FT STRAND 162 168
FT STRAND 171 175
FT STRAND 319 322
FT STRAND 326 328
FT STRAND 333 338
FT STRAND 342 346
FT STRAND 349 352
FT STRAND 355 358
FT STRAND 364 366
FT STRAND 370 373
FT STRAND 385 392
FT STRAND 401 406
FT TURN 408 410
FT STRAND 411 413
FT STRAND 426 429
FT STRAND 433 437
FT TURN 438 440
FT STRAND 447 449
FT STRAND 478 492
FT TURN 493 495
FT STRAND 496 499
FT HELIX 501 504
FT STRAND 518 522
FT HELIX 526 532
FT STRAND 537 542
FT STRAND 548 552
FT STRAND 559 565
FT STRAND 571 573
FT HELIX 582 585
FT STRAND 590 595
FT STRAND 600 602
FT STRAND 608 614
FT HELIX 617 626
FT STRAND 637 641
FT HELIX 643 650
FT TURN 651 655
FT STRAND 657 661
FT TURN 663 665
FT STRAND 668 676
FT STRAND 678 683
FT STRAND 685 689
FT HELIX 690 693
FT HELIX 694 700
SQ SEQUENCE 705 AA; 80119 MW; B45D120201061462 CRC64;
MWLLYLLVPA LFCRAGGSIP IPQKLFGEVT SPLFPKPYPN NFETTTVITV PTGYRVKLVF
QQFDLEPSEG CFYDYVKISA DKKSLGRFCG QLGSPLGNPP GKKEFMSQGN KMLLTFHTDF
SNEENGTIMF YKGFLAYYQA VDLDECASRS KSGEEDPQPQ CQHLCHNYVG GYFCSCRPGY
ELQEDTHSCQ AECSSELYTE ASGYISSLEY PRSYPPDLRC NYSIRVERGL TLHLKFLEPF
DIDDHQQVHC PYDQLQIYAN GKNIGEFCGK QRPPDLDTSS NAVDLLFFTD ESGDSRGWKL
RYTTEIIKCP QPKTLDEFTI IQNLQPQYQF RDYFIATCKQ GYQLIEGNQV LHSFTAVCQD
DGTWHRAMPR CKIKDCGQPR NLPNGDFRYT TTMGVNTYKA RIQYYCHEPY YKMQTRAGSR
ESEQGVYTCT AQGIWKNEQK GEKIPRCLPV CGKPVNPVEQ RQRIIGGQKA KMGNFPWQVF
TNIHGRGGGA LLGDRWILTA AHTLYPKEHE AQSNASLDVF LGHTNVEELM KLGNHPIRRV
SVHPDYRQDE SYNFEGDIAL LELENSVTLG PNLLPICLPD NDTFYDLGLM GYVSGFGVME
EKIAHDLRFV RLPVANPQAC ENWLRGKNRM DVFSQNMFCA GHPSLKQDAC QGDSGGVFAV
RDPNTDRWVA TGIVSWGIGC SRGYGFYTKV LNYVDWIKKE MEEED
//
MIM
216950
*RECORD*
*FIELD* NO
216950
*FIELD* TI
%216950 COMPLEMENT COMPONENT C1r/C1s DEFICIENCY
;;C1r/C1s DEFICIENCY
*FIELD* TX
CLINICAL FEATURES
read more
Day et al. (1972) observed 2 sibs with deficiency of C1r (613785). The
brother (18 years old) had shown lupus-like features for 5 years. The
sister (24 years old) had had arthralgia and recurrent rhinobronchitis
from early childhood. Three sibs had died, 1 at age 12 with symptoms
like those in the male and 2 in infancy, probably from infection.
Laboratory findings suggested the existence of an alternative pathway
for activation of the terminal portion of the complement cascade which
does not use the usual early components.
Lee et al. (1978) described a family in which 4 of 11 children had
absence of C1r and marked deficiency of C1s (120580). Two of the 4 had a
syndrome combining discoid lupus erythematosus and nondeforming
rheumatoid-like arthritis; 1 had mild nephritis. C1 and C4 deficiencies
are more often associated with lupus-like illness than is deficiency of
C2. Linkage of HLA and C1 was excluded by the fact that all 4 parental
haplotypes were represented in the 4 deficient sibs. Deficiency of C1s
has been observed in other cases of C1r absence and may be a secondary
effect; however, close linkage of C1s and C1r means that both may be
deleted or otherwise deranged.
Loos and Heinz (1986) stated that all reported cases of C1r deficiency
also had deficiency of C1s.
A selective deficiency of C1s has been reported; see 613783.
MAPPING
Day et al. (1975) found that C1r deficiency is not linked to the HLA
region.
Using a panel of human-rodent cell hybrids, Van Cong et al. (1988)
assigned the C1r and C1s genes to chromosome 12. In situ hybridization
confirmed these assignments and localized the genes to 12p13.
*FIELD* SA
Moncada et al. (1972); Rich et al. (1979)
*FIELD* RF
1. Day, N. K.; Geiger, H.; Stroud, R.; deBracco, M.; Mancado, B.;
Windhorst, D. B.; Good, R. A.: C-prime-1r deficiency: an inborn error
associated with cutaneous and renal disease. J. Clin. Invest. 51:
1102-1108, 1972.
2. Day, N. K.; Rubinstein, P.; deBracco, M.; Moncada, B.; Hansen,
J. A.; Dupont, B.; Thomsen, M.; Svejgaard, A.; Jersild, C.: Hereditary
C1r deficiency: lack of linkage to the HL-A region in two families.In:
Kissmeyer-Nielsen, F.: Histocompatibility Testing 1975. Copenhagen:
Munksgaard (pub.) (1st ed.): 1975. Pp. 961-962.
3. Lee, S. L.; Wallace, S. L.; Barone, R.; Blum, L.; Chase, P. H.
: Familial deficiency of two subunits of the first component of complement:
C1r and C1s associated with a lupus erythematosus-like disease. Arthritis
Rheum. 21: 958-967, 1978.
4. Loos, M.; Heinz, H. P.: Component deficiencies. I. The first component:
C1q, C1r, C1s. Prog. Allergy 39: 212-231, 1986.
5. Moncada, B.; Day, N. K. B.; Good, R. A.; Windhorst, D. B.: Lupus-erythematosus-like
syndrome with a familial defect of complement. New Eng. J. Med. 286:
689-693, 1972.
6. Rich, K. C., Jr.; Hurley, J.; Gewurz, H.: Inborn C1r deficiency
with a mild lupus-like syndrome. Clin. Immun. Immunopath. 13: 77-84,
1979.
7. Van Cong, N.; Tosi, M.; Gross, M. S.; Cohen-Haguenauer, O.; Jegou-Foubert,
C.; de Tand, M. F.; Meo, T.; Frezal, J.: Assignment of the complement
serine protease genes C1r and C1s to chromosome 12 region 12p13. Hum.
Genet. 78: 363-368, 1988.
*FIELD* CS
Immune:
Autoimmune disease
Lab:
C1r deficiency
Joints:
Arthralgia;
Nondeforming rheumatoid-like arthritis
Pulmonary:
Recurrent rhinobronchitis
Skin:
Discoid lupus erythematosus
GU:
Mild nephritis
Inheritance:
Autosomal recessive
*FIELD* CD
Victor A. McKusick: 6/3/1986
*FIELD* ED
carol: 03/02/2011
carol: 3/1/2011
alopez: 3/17/2004
carol: 4/21/1999
carol: 8/4/1998
dkim: 6/30/1998
alopez: 6/10/1997
mark: 6/7/1996
pfoster: 9/7/1994
davew: 8/3/1994
warfield: 3/8/1994
mimadm: 2/19/1994
supermim: 3/16/1992
carol: 2/26/1991
*RECORD*
*FIELD* NO
216950
*FIELD* TI
%216950 COMPLEMENT COMPONENT C1r/C1s DEFICIENCY
;;C1r/C1s DEFICIENCY
*FIELD* TX
CLINICAL FEATURES
read more
Day et al. (1972) observed 2 sibs with deficiency of C1r (613785). The
brother (18 years old) had shown lupus-like features for 5 years. The
sister (24 years old) had had arthralgia and recurrent rhinobronchitis
from early childhood. Three sibs had died, 1 at age 12 with symptoms
like those in the male and 2 in infancy, probably from infection.
Laboratory findings suggested the existence of an alternative pathway
for activation of the terminal portion of the complement cascade which
does not use the usual early components.
Lee et al. (1978) described a family in which 4 of 11 children had
absence of C1r and marked deficiency of C1s (120580). Two of the 4 had a
syndrome combining discoid lupus erythematosus and nondeforming
rheumatoid-like arthritis; 1 had mild nephritis. C1 and C4 deficiencies
are more often associated with lupus-like illness than is deficiency of
C2. Linkage of HLA and C1 was excluded by the fact that all 4 parental
haplotypes were represented in the 4 deficient sibs. Deficiency of C1s
has been observed in other cases of C1r absence and may be a secondary
effect; however, close linkage of C1s and C1r means that both may be
deleted or otherwise deranged.
Loos and Heinz (1986) stated that all reported cases of C1r deficiency
also had deficiency of C1s.
A selective deficiency of C1s has been reported; see 613783.
MAPPING
Day et al. (1975) found that C1r deficiency is not linked to the HLA
region.
Using a panel of human-rodent cell hybrids, Van Cong et al. (1988)
assigned the C1r and C1s genes to chromosome 12. In situ hybridization
confirmed these assignments and localized the genes to 12p13.
*FIELD* SA
Moncada et al. (1972); Rich et al. (1979)
*FIELD* RF
1. Day, N. K.; Geiger, H.; Stroud, R.; deBracco, M.; Mancado, B.;
Windhorst, D. B.; Good, R. A.: C-prime-1r deficiency: an inborn error
associated with cutaneous and renal disease. J. Clin. Invest. 51:
1102-1108, 1972.
2. Day, N. K.; Rubinstein, P.; deBracco, M.; Moncada, B.; Hansen,
J. A.; Dupont, B.; Thomsen, M.; Svejgaard, A.; Jersild, C.: Hereditary
C1r deficiency: lack of linkage to the HL-A region in two families.In:
Kissmeyer-Nielsen, F.: Histocompatibility Testing 1975. Copenhagen:
Munksgaard (pub.) (1st ed.): 1975. Pp. 961-962.
3. Lee, S. L.; Wallace, S. L.; Barone, R.; Blum, L.; Chase, P. H.
: Familial deficiency of two subunits of the first component of complement:
C1r and C1s associated with a lupus erythematosus-like disease. Arthritis
Rheum. 21: 958-967, 1978.
4. Loos, M.; Heinz, H. P.: Component deficiencies. I. The first component:
C1q, C1r, C1s. Prog. Allergy 39: 212-231, 1986.
5. Moncada, B.; Day, N. K. B.; Good, R. A.; Windhorst, D. B.: Lupus-erythematosus-like
syndrome with a familial defect of complement. New Eng. J. Med. 286:
689-693, 1972.
6. Rich, K. C., Jr.; Hurley, J.; Gewurz, H.: Inborn C1r deficiency
with a mild lupus-like syndrome. Clin. Immun. Immunopath. 13: 77-84,
1979.
7. Van Cong, N.; Tosi, M.; Gross, M. S.; Cohen-Haguenauer, O.; Jegou-Foubert,
C.; de Tand, M. F.; Meo, T.; Frezal, J.: Assignment of the complement
serine protease genes C1r and C1s to chromosome 12 region 12p13. Hum.
Genet. 78: 363-368, 1988.
*FIELD* CS
Immune:
Autoimmune disease
Lab:
C1r deficiency
Joints:
Arthralgia;
Nondeforming rheumatoid-like arthritis
Pulmonary:
Recurrent rhinobronchitis
Skin:
Discoid lupus erythematosus
GU:
Mild nephritis
Inheritance:
Autosomal recessive
*FIELD* CD
Victor A. McKusick: 6/3/1986
*FIELD* ED
carol: 03/02/2011
carol: 3/1/2011
alopez: 3/17/2004
carol: 4/21/1999
carol: 8/4/1998
dkim: 6/30/1998
alopez: 6/10/1997
mark: 6/7/1996
pfoster: 9/7/1994
davew: 8/3/1994
warfield: 3/8/1994
mimadm: 2/19/1994
supermim: 3/16/1992
carol: 2/26/1991
MIM
613785
*RECORD*
*FIELD* NO
613785
*FIELD* TI
*613785 COMPLEMENT COMPONENT 1, r SUBCOMPONENT; C1R
;;COMPLEMENT COMPONENT C1r
*FIELD* TX
read more
DESCRIPTION
The complement system is a major mediator of innate immunity. The first
enzymatic event in the cascade of the classical pathway of complement is
the activation of its first component, C1. C1 is a multimolecular
complex consisting of 2 loosely interacting entities: C1q (see 120550),
the recognition subunit, and C1r(2)/C1s(2), the catalytic one.
C1r(2)/C1s(2) is a tetrameric Ca(2+)-dependent complex of C1r and C1s
(120580), 2 serine-proteinase zymogens. C1r acts by transforming the
activation signal (the fixation of C1q on activating reagents, e.g.,
immune complexes) into an enzymic activity (summary by Journet and Tosi,
1986).
CLONING
Leytus et al. (1986) reported the nucleotide sequence for cDNA coding
for C1r. Journet and Tosi (1986) cloned and sequenced a full-length cDNA
for the C1r precursor, which contains a 17-amino acid leader peptide,
followed by a mature 688-amino acid protein.
MAPPING
By means of a cDNA in somatic cell hybrids, Cohen-Haguenauer et al.
(1986) assigned the C1R and C1S genes to chromosome 12. Leppert et al.
(1987) found a maximum lod score of 5.99 at theta = 0.038 for linkage
between C1S and one of the PRP loci (see 168710); the maximum lod score
between C1R and another PRP locus was 4.21 at theta = 0.001. Although
C1r and C1s are structurally and functionally similar, with a
significant degree of sequence homology suggesting origin by gene
duplication, cDNA probes for human C1r and C1s do not cross-hybridize
even at mild stringency conditions and are therefore gene-specific.
Using a panel of human-rodent cell hybrids, Van Cong et al. (1988)
independently assigned the C1r and C1s genes to chromosome 12. In situ
hybridization confirmed these assignments and localized the genes to
12p13.
In a study of 5 families heterozygous at both the C1R and the C1S locus,
Lyons et al. (1989) found evidence consistent with, but not proving,
linkage of the loci; maximum lod score = 1.505 at theta = 0.00.
By hybridization of C1r and C1s probes to restriction endonuclease
fragments of genomic DNA, Tosi et al. (1987) demonstrated close physical
linkage of the genes. This finding was consistent with their evolution
through tandem gene duplication and was also consistent with the
previously observed combined hereditary deficiencies of C1r and C1s (see
216950). Their coordinate expression may depend on the close linkage.
The 2 genes lie in a DNA stretch not longer than 50 kb.
By DNA blotting and sequencing analyses of genomic DNA and of an
isolated genomic DNA clone, Kusumoto et al. (1988) showed that the C1r
and C1s genes are closely located in a 'tail-to-tail' arrangement at a
distance of about 9.5 kb.
MOLECULAR GENETICS
Kamboh and Ferrell (1986) demonstrated genetic polymorphism of C1R using
the high-resolving power of isoelectric focusing in 6M urea followed by
immunoblotting. Kamboh et al. (1988) described a new allele by
isoelectric focusing and immunoblotting. Using the same methods, Kamboh
et al. (1989) described 5 new alleles.
Data on gene frequencies of allelic variants were tabulated by
Roychoudhury and Nei (1988).
*FIELD* RF
1. Cohen-Haguenauer, O.; Serero, S.; Tosi, M.; Van Cong, N.; Stubnicer,
A.-C.; de Tand, M.-F.; Meo, T.; Frezal, J.: Chromosomal assignment
of human C1R, C1S genes on chromosome 12 and C1 inhibitor gene on
chromosome 11. (Abstract) 7th Int. Cong. Hum. Genet., Berlin 617
only, 1986.
2. Journet, A.; Tosi, M.: Cloning and sequencing of full-length cDNA
encoding the precursor of human complement component C1r. Biochem.
J. 240: 783-787, 1986.
3. Kamboh, M. I.; Ferrell, R. E.: Genetic studies of low abundance
human plasma proteins. III. Polymorphism of the C1R subcomponent of
the first complement component. Am. J. Hum. Genet. 39: 826-831,
1986.
4. Kamboh, M. I.; Lyons, L.; Ferrell, R. E.: Genetic studies of low-abundance
human plasma proteins. IX. A new allele at the complement subcomponent
C1R structural locus. Hum. Genet. 81: 93-94, 1988.
5. Kamboh, M. I.; Lyons, L. A.; Ferrell, R. E.: Genetic studies of
low-abundance human plasma proteins. XIII. Population genetics of
C1R complement subcomponent and description of new variants. Am.
J. Hum. Genet. 44: 148-153, 1989.
6. Kusumoto, H.; Hirosawa, S.; Salier, J. P.; Hagen, F. S.; Kurachi,
K.: Human genes for complement components C1r and C1s in a close
tail-to-tail arrangement. Proc. Nat. Acad. Sci. 85: 7307-7311, 1988.
7. Leppert, M.; Ferrell, R.; Kamboh, M. I.; Beasley, J.; O'Connell,
P.; Lathrop, M.; Lalouel, J. M.; White, R.: Linkage of the polymorphic
protein markers F13B, C1S, C1R, and blood group antigen Kidd in CEPH
reference families. (Abstract) Cytogenet. Cell Genet. 46: 647 only,
1987.
8. Leytus, S. P.; Kurachi, K.; Sakariassen, K. S.; Davie, E. W.:
Nucleotide sequence of the cDNA coding for human complement C1r. Biochemistry 25:
4855-4863, 1986.
9. Lyons, L. A.; Kamboh, M. I.; Ferrell, R. E.: Genetic studies of
low-abundance human plasma proteins. XI. Linkage analysis and population
genetics of the C1S subcomponent of the first complement component. Complement
Inflamm. 6: 81-87, 1989.
10. Roychoudhury, A. K.; Nei, M.: Human Polymorphic Genes: World
Distribution. New York: Oxford Univ. Press (pub.) 1988.
11. Tosi, M.; Duponchel, C.; Meo, T.; Julier, C.: Complete cDNA sequence
of human complement C1s and close physical linkage of the homologous
genes C1s and C1r. Biochemistry 26: 8516-8524, 1987.
12. Van Cong, N.; Tosi, M.; Gross, M. S.; Cohen-Haguenauer, O.; Jegou-Foubert,
C.; de Tand, M. F.; Meo, T.; Frezal, J.: Assignment of the complement
serine protease genes C1r and C1s to chromosome 12 region 12p13. Hum.
Genet. 78: 363-368, 1988.
*FIELD* CD
Carol A. Bocchini: 3/1/2011
*FIELD* ED
carol: 03/02/2011
carol: 3/1/2011
*RECORD*
*FIELD* NO
613785
*FIELD* TI
*613785 COMPLEMENT COMPONENT 1, r SUBCOMPONENT; C1R
;;COMPLEMENT COMPONENT C1r
*FIELD* TX
read more
DESCRIPTION
The complement system is a major mediator of innate immunity. The first
enzymatic event in the cascade of the classical pathway of complement is
the activation of its first component, C1. C1 is a multimolecular
complex consisting of 2 loosely interacting entities: C1q (see 120550),
the recognition subunit, and C1r(2)/C1s(2), the catalytic one.
C1r(2)/C1s(2) is a tetrameric Ca(2+)-dependent complex of C1r and C1s
(120580), 2 serine-proteinase zymogens. C1r acts by transforming the
activation signal (the fixation of C1q on activating reagents, e.g.,
immune complexes) into an enzymic activity (summary by Journet and Tosi,
1986).
CLONING
Leytus et al. (1986) reported the nucleotide sequence for cDNA coding
for C1r. Journet and Tosi (1986) cloned and sequenced a full-length cDNA
for the C1r precursor, which contains a 17-amino acid leader peptide,
followed by a mature 688-amino acid protein.
MAPPING
By means of a cDNA in somatic cell hybrids, Cohen-Haguenauer et al.
(1986) assigned the C1R and C1S genes to chromosome 12. Leppert et al.
(1987) found a maximum lod score of 5.99 at theta = 0.038 for linkage
between C1S and one of the PRP loci (see 168710); the maximum lod score
between C1R and another PRP locus was 4.21 at theta = 0.001. Although
C1r and C1s are structurally and functionally similar, with a
significant degree of sequence homology suggesting origin by gene
duplication, cDNA probes for human C1r and C1s do not cross-hybridize
even at mild stringency conditions and are therefore gene-specific.
Using a panel of human-rodent cell hybrids, Van Cong et al. (1988)
independently assigned the C1r and C1s genes to chromosome 12. In situ
hybridization confirmed these assignments and localized the genes to
12p13.
In a study of 5 families heterozygous at both the C1R and the C1S locus,
Lyons et al. (1989) found evidence consistent with, but not proving,
linkage of the loci; maximum lod score = 1.505 at theta = 0.00.
By hybridization of C1r and C1s probes to restriction endonuclease
fragments of genomic DNA, Tosi et al. (1987) demonstrated close physical
linkage of the genes. This finding was consistent with their evolution
through tandem gene duplication and was also consistent with the
previously observed combined hereditary deficiencies of C1r and C1s (see
216950). Their coordinate expression may depend on the close linkage.
The 2 genes lie in a DNA stretch not longer than 50 kb.
By DNA blotting and sequencing analyses of genomic DNA and of an
isolated genomic DNA clone, Kusumoto et al. (1988) showed that the C1r
and C1s genes are closely located in a 'tail-to-tail' arrangement at a
distance of about 9.5 kb.
MOLECULAR GENETICS
Kamboh and Ferrell (1986) demonstrated genetic polymorphism of C1R using
the high-resolving power of isoelectric focusing in 6M urea followed by
immunoblotting. Kamboh et al. (1988) described a new allele by
isoelectric focusing and immunoblotting. Using the same methods, Kamboh
et al. (1989) described 5 new alleles.
Data on gene frequencies of allelic variants were tabulated by
Roychoudhury and Nei (1988).
*FIELD* RF
1. Cohen-Haguenauer, O.; Serero, S.; Tosi, M.; Van Cong, N.; Stubnicer,
A.-C.; de Tand, M.-F.; Meo, T.; Frezal, J.: Chromosomal assignment
of human C1R, C1S genes on chromosome 12 and C1 inhibitor gene on
chromosome 11. (Abstract) 7th Int. Cong. Hum. Genet., Berlin 617
only, 1986.
2. Journet, A.; Tosi, M.: Cloning and sequencing of full-length cDNA
encoding the precursor of human complement component C1r. Biochem.
J. 240: 783-787, 1986.
3. Kamboh, M. I.; Ferrell, R. E.: Genetic studies of low abundance
human plasma proteins. III. Polymorphism of the C1R subcomponent of
the first complement component. Am. J. Hum. Genet. 39: 826-831,
1986.
4. Kamboh, M. I.; Lyons, L.; Ferrell, R. E.: Genetic studies of low-abundance
human plasma proteins. IX. A new allele at the complement subcomponent
C1R structural locus. Hum. Genet. 81: 93-94, 1988.
5. Kamboh, M. I.; Lyons, L. A.; Ferrell, R. E.: Genetic studies of
low-abundance human plasma proteins. XIII. Population genetics of
C1R complement subcomponent and description of new variants. Am.
J. Hum. Genet. 44: 148-153, 1989.
6. Kusumoto, H.; Hirosawa, S.; Salier, J. P.; Hagen, F. S.; Kurachi,
K.: Human genes for complement components C1r and C1s in a close
tail-to-tail arrangement. Proc. Nat. Acad. Sci. 85: 7307-7311, 1988.
7. Leppert, M.; Ferrell, R.; Kamboh, M. I.; Beasley, J.; O'Connell,
P.; Lathrop, M.; Lalouel, J. M.; White, R.: Linkage of the polymorphic
protein markers F13B, C1S, C1R, and blood group antigen Kidd in CEPH
reference families. (Abstract) Cytogenet. Cell Genet. 46: 647 only,
1987.
8. Leytus, S. P.; Kurachi, K.; Sakariassen, K. S.; Davie, E. W.:
Nucleotide sequence of the cDNA coding for human complement C1r. Biochemistry 25:
4855-4863, 1986.
9. Lyons, L. A.; Kamboh, M. I.; Ferrell, R. E.: Genetic studies of
low-abundance human plasma proteins. XI. Linkage analysis and population
genetics of the C1S subcomponent of the first complement component. Complement
Inflamm. 6: 81-87, 1989.
10. Roychoudhury, A. K.; Nei, M.: Human Polymorphic Genes: World
Distribution. New York: Oxford Univ. Press (pub.) 1988.
11. Tosi, M.; Duponchel, C.; Meo, T.; Julier, C.: Complete cDNA sequence
of human complement C1s and close physical linkage of the homologous
genes C1s and C1r. Biochemistry 26: 8516-8524, 1987.
12. Van Cong, N.; Tosi, M.; Gross, M. S.; Cohen-Haguenauer, O.; Jegou-Foubert,
C.; de Tand, M. F.; Meo, T.; Frezal, J.: Assignment of the complement
serine protease genes C1r and C1s to chromosome 12 region 12p13. Hum.
Genet. 78: 363-368, 1988.
*FIELD* CD
Carol A. Bocchini: 3/1/2011
*FIELD* ED
carol: 03/02/2011
carol: 3/1/2011