Full text data of FCN2
FCN2
(FCNL)
[Confidence: low (only semi-automatic identification from reviews)]
Ficolin-2 (37 kDa elastin-binding protein; Collagen/fibrinogen domain-containing protein 2; EBP-37; Ficolin-B; Ficolin-beta; Hucolin; L-ficolin; Serum lectin p35; Flags: Precursor)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Ficolin-2 (37 kDa elastin-binding protein; Collagen/fibrinogen domain-containing protein 2; EBP-37; Ficolin-B; Ficolin-beta; Hucolin; L-ficolin; Serum lectin p35; Flags: Precursor)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q15485
ID FCN2_HUMAN Reviewed; 313 AA.
AC Q15485; A6NFG7; A8K478; Q6IS69; Q7M4P4; Q9UC57;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 15-JAN-2008, sequence version 2.
DT 22-JAN-2014, entry version 124.
DE RecName: Full=Ficolin-2;
DE AltName: Full=37 kDa elastin-binding protein;
DE AltName: Full=Collagen/fibrinogen domain-containing protein 2;
DE AltName: Full=EBP-37;
DE AltName: Full=Ficolin-B;
DE AltName: Full=Ficolin-beta;
DE AltName: Full=Hucolin;
DE AltName: Full=L-ficolin;
DE AltName: Full=Serum lectin p35;
DE Flags: Precursor;
GN Name=FCN2; Synonyms=FCNL;
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 [GENOMIC DNA].
RX PubMed=8884275; DOI=10.1006/geno.1996.0497;
RA Endo Y., Sato Y., Matsushita M., Fujita T.;
RT "Cloning and characterization of the human lectin P35 gene and its
RT related gene.";
RL Genomics 36:515-521(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Liver;
RX PubMed=8576206; DOI=10.1074/jbc.271.5.2448;
RA Matsushita M., Endo Y., Taira S., Sato Y., Fujita T., Ichikawa N.,
RA Nakata M., Mizuochi T.;
RT "A novel human serum lectin with collagen- and fibrinogen-like domains
RT that functions as an opsonin.";
RL J. Biol. Chem. 271:2448-2454(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Tan J., Ong R., Hibberd M.L., Seielstad M.;
RT "Genetic variation in immune response genes.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
RP TYR-113.
RC TISSUE=Liver;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
RA Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
RA Rogers J., Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [8]
RP PROTEIN SEQUENCE OF 26-50 (ISOFORM 1).
RC TISSUE=Plasma;
RX PubMed=7498469; DOI=10.1016/0014-5793(95)01205-S;
RA Edgar P.F.;
RT "Hucolin, a new corticosteroid-binding protein from human plasma with
RT structural similarities to ficolins, transforming growth factor-beta
RT 1-binding proteins.";
RL FEBS Lett. 375:159-161(1995).
RN [9]
RP PROTEIN SEQUENCE OF 65-99; 191-198 AND 218-228 (ISOFORM 1), SUBUNIT,
RP AND HYDROXYLATION AT PRO-77; PRO-80 AND PRO-86.
RC TISSUE=Plasma;
RX PubMed=8586615;
RA Harumiya S., Omori A., Sugiura T., Fukumoto Y., Tachikawa H.,
RA Fujimoto D.;
RT "EBP-37, a new elastin-binding protein in human plasma: structural
RT similarity to ficolins, transforming growth factor-beta 1-binding
RT proteins.";
RL J. Biochem. 117:1029-1035(1995).
RN [10]
RP FUNCTION, AND INTERACTION WITH MASP1 AND MASP2.
RX PubMed=10679061;
RA Matsushita M., Endo Y., Fujita T.;
RT "Complement-activating complex of ficolin and mannose-binding lectin-
RT associated serine protease.";
RL J. Immunol. 164:2281-2284(2000).
RN [11]
RP VARIANT [LARGE SCALE ANALYSIS] LEU-80.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal
RT cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: May function in innate immunity through activation of
CC the lectin complement pathway. Calcium-dependent and GlcNAc-
CC binding lectin. Enhances phagocytosis of S.typhimurium by
CC neutrophils, suggesting an opsonic effect via the collagen region.
CC -!- SUBUNIT: Homopolymer; disulfide-linked. Interacts with elastin.
CC Interacts with MASP1 and MASP2.
CC -!- INTERACTION:
CC Q07954:LRP1; NbExp=2; IntAct=EBI-7468784, EBI-1046087;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q15485-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q15485-2; Sequence=VSP_030027;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma.
CC -!- DOMAIN: The fibrinogen-like domain (FBG) contains potential
CC calcium-binding sites that may be involved in carbohydrate
CC binding.
CC -!- SIMILARITY: Belongs to the ficolin lectin family.
CC -!- SIMILARITY: Contains 1 collagen-like domain.
CC -!- SIMILARITY: Contains 1 fibrinogen C-terminal domain.
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DR EMBL; D63160; BAA09636.1; -; Genomic_DNA.
DR EMBL; D49353; BAA08352.1; -; mRNA.
DR EMBL; DQ217935; ABB01005.1; -; Genomic_DNA.
DR EMBL; AK290843; BAF83532.1; -; mRNA.
DR EMBL; AL603650; CAI39861.1; -; Genomic_DNA.
DR EMBL; CH471090; EAW88133.1; -; Genomic_DNA.
DR EMBL; CH471090; EAW88135.1; -; Genomic_DNA.
DR EMBL; BC069572; AAH69572.1; -; mRNA.
DR EMBL; BC069825; AAH69825.1; -; mRNA.
DR PIR; PH0263; PH0263.
DR PIR; S68005; S68005.
DR RefSeq; NP_004099.2; NM_004108.2.
DR RefSeq; NP_056652.1; NM_015837.2.
DR UniGene; Hs.54517; -.
DR PDB; 2J0G; X-ray; 2.85 A; A/B/C/D/E/F=97-313.
DR PDB; 2J0H; X-ray; 2.85 A; A/B/C/D/E/F=97-313.
DR PDB; 2J0Y; X-ray; 2.35 A; A/B/C/D/E/F=97-313.
DR PDB; 2J1G; X-ray; 1.95 A; A/B/C/D/E/F=97-313.
DR PDB; 2J2P; X-ray; 2.80 A; A/B/C/D/E/F=97-313.
DR PDB; 2J3F; X-ray; 2.80 A; A/B/C/D/E/F=95-313.
DR PDB; 2J3G; X-ray; 2.50 A; A/B/C/D/E/F=97-313.
DR PDB; 2J3O; X-ray; 2.65 A; A/B/C/D/E/F=95-313.
DR PDB; 2J3U; X-ray; 2.15 A; A/B/C/D/E/F=97-313.
DR PDB; 2J61; X-ray; 2.70 A; A/B=97-313.
DR PDBsum; 2J0G; -.
DR PDBsum; 2J0H; -.
DR PDBsum; 2J0Y; -.
DR PDBsum; 2J1G; -.
DR PDBsum; 2J2P; -.
DR PDBsum; 2J3F; -.
DR PDBsum; 2J3G; -.
DR PDBsum; 2J3O; -.
DR PDBsum; 2J3U; -.
DR PDBsum; 2J61; -.
DR ProteinModelPortal; Q15485; -.
DR SMR; Q15485; 62-92, 97-313.
DR IntAct; Q15485; 2.
DR MINT; MINT-5223224; -.
DR STRING; 9606.ENSP00000291744; -.
DR DMDM; 166214934; -.
DR PaxDb; Q15485; -.
DR PRIDE; Q15485; -.
DR Ensembl; ENST00000291744; ENSP00000291744; ENSG00000160339.
DR Ensembl; ENST00000350339; ENSP00000291741; ENSG00000160339.
DR GeneID; 2220; -.
DR KEGG; hsa:2220; -.
DR UCSC; uc004cfg.1; human.
DR CTD; 2220; -.
DR GeneCards; GC09P137772; -.
DR HGNC; HGNC:3624; FCN2.
DR MIM; 601624; gene.
DR neXtProt; NX_Q15485; -.
DR PharmGKB; PA28070; -.
DR eggNOG; NOG249945; -.
DR HOGENOM; HOG000037127; -.
DR HOVERGEN; HBG001644; -.
DR KO; K10104; -.
DR OMA; NTGNCAV; -.
DR OrthoDB; EOG7X9G60; -.
DR PhylomeDB; Q15485; -.
DR Reactome; REACT_6900; Immune System.
DR EvolutionaryTrace; Q15485; -.
DR GeneWiki; FCN2; -.
DR GenomeRNAi; 2220; -.
DR NextBio; 9005; -.
DR PRO; PR:Q15485; -.
DR Bgee; Q15485; -.
DR CleanEx; HS_FCN2; -.
DR Genevestigator; Q15485; -.
DR GO; GO:0005581; C:collagen; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0003823; F:antigen binding; TAS:ProtInc.
DR GO; GO:0005509; F:calcium ion binding; TAS:ProtInc.
DR GO; GO:0030246; F:carbohydrate binding; TAS:ProtInc.
DR GO; GO:0001867; P:complement activation, lectin pathway; TAS:Reactome.
DR GO; GO:0008228; P:opsonization; TAS:ProtInc.
DR Gene3D; 3.90.215.10; -; 1.
DR Gene3D; 4.10.530.10; -; 1.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR014716; Fibrinogen_a/b/g_C_1.
DR InterPro; IPR014715; Fibrinogen_a/b/g_C_2.
DR InterPro; IPR002181; Fibrinogen_a/b/g_C_dom.
DR InterPro; IPR020837; Fibrinogen_CS.
DR Pfam; PF01391; Collagen; 1.
DR Pfam; PF00147; Fibrinogen_C; 1.
DR SMART; SM00186; FBG; 1.
DR SUPFAM; SSF56496; SSF56496; 1.
DR PROSITE; PS00514; FIBRINOGEN_C_1; 1.
DR PROSITE; PS51406; FIBRINOGEN_C_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Collagen;
KW Complement activation lectin pathway; Complete proteome;
KW Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Hydroxylation; Immunity; Innate immunity; Lectin; Polymorphism;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1 25 Potential.
FT CHAIN 26 313 Ficolin-2.
FT /FTId=PRO_0000009139.
FT DOMAIN 51 92 Collagen-like.
FT DOMAIN 96 313 Fibrinogen C-terminal.
FT MOD_RES 77 77 Hydroxyproline.
FT MOD_RES 80 80 Hydroxyproline.
FT MOD_RES 86 86 Hydroxyproline.
FT CARBOHYD 240 240 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 300 300 N-linked (GlcNAc...) (Potential).
FT VAR_SEQ 34 71 Missing (in isoform 2).
FT /FTId=VSP_030027.
FT VARIANT 80 80 P -> L (in a colorectal cancer sample;
FT somatic mutation).
FT /FTId=VAR_036342.
FT VARIANT 113 113 H -> Y (in dbSNP:rs17549179).
FT /FTId=VAR_049072.
FT VARIANT 117 117 G -> S (in dbSNP:rs12684476).
FT /FTId=VAR_049073.
FT VARIANT 236 236 T -> M (in dbSNP:rs17549193).
FT /FTId=VAR_049074.
FT VARIANT 258 258 A -> S (in dbSNP:rs7851696).
FT /FTId=VAR_049075.
FT CONFLICT 61 61 P -> D (in Ref. 1; BAA08352 and 2;
FT ABB01005).
FT CONFLICT 98 98 C -> A (in Ref. 9; AA sequence).
FT STRAND 99 101
FT HELIX 105 110
FT STRAND 115 122
FT STRAND 124 126
FT STRAND 128 134
FT HELIX 137 139
FT STRAND 142 151
FT HELIX 159 164
FT STRAND 166 168
FT HELIX 177 182
FT STRAND 185 187
FT STRAND 191 196
FT STRAND 198 200
FT STRAND 202 208
FT STRAND 210 212
FT TURN 215 219
FT STRAND 221 223
FT STRAND 226 228
FT HELIX 236 238
FT STRAND 246 248
FT STRAND 251 255
FT HELIX 258 261
FT STRAND 263 265
FT STRAND 268 270
FT STRAND 272 274
FT STRAND 285 288
FT STRAND 290 293
FT TURN 294 297
FT STRAND 299 302
FT STRAND 304 310
SQ SEQUENCE 313 AA; 34001 MW; D363029846CCB3C9 CRC64;
MELDRAVGVL GAATLLLSFL GMAWALQAAD TCPEVKMVGL EGSDKLTILR GCPGLPGAPG
PKGEAGTNGK RGERGPPGPP GKAGPPGPNG APGEPQPCLT GPRTCKDLLD RGHFLSGWHT
IYLPDCRPLT VLCDMDTDGG GWTVFQRRVD GSVDFYRDWA TYKQGFGSRL GEFWLGNDNI
HALTAQGTSE LRVDLVDFED NYQFAKYRSF KVADEAEKYN LVLGAFVEGS AGDSLTFHNN
QSFSTKDQDN DLNTGNCAVM FQGAWWYKNC HVSNLNGRYL RGTHGSFANG INWKSGKGYN
YSYKVSEMKV RPA
//
ID FCN2_HUMAN Reviewed; 313 AA.
AC Q15485; A6NFG7; A8K478; Q6IS69; Q7M4P4; Q9UC57;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 15-JAN-2008, sequence version 2.
DT 22-JAN-2014, entry version 124.
DE RecName: Full=Ficolin-2;
DE AltName: Full=37 kDa elastin-binding protein;
DE AltName: Full=Collagen/fibrinogen domain-containing protein 2;
DE AltName: Full=EBP-37;
DE AltName: Full=Ficolin-B;
DE AltName: Full=Ficolin-beta;
DE AltName: Full=Hucolin;
DE AltName: Full=L-ficolin;
DE AltName: Full=Serum lectin p35;
DE Flags: Precursor;
GN Name=FCN2; Synonyms=FCNL;
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 [GENOMIC DNA].
RX PubMed=8884275; DOI=10.1006/geno.1996.0497;
RA Endo Y., Sato Y., Matsushita M., Fujita T.;
RT "Cloning and characterization of the human lectin P35 gene and its
RT related gene.";
RL Genomics 36:515-521(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Liver;
RX PubMed=8576206; DOI=10.1074/jbc.271.5.2448;
RA Matsushita M., Endo Y., Taira S., Sato Y., Fujita T., Ichikawa N.,
RA Nakata M., Mizuochi T.;
RT "A novel human serum lectin with collagen- and fibrinogen-like domains
RT that functions as an opsonin.";
RL J. Biol. Chem. 271:2448-2454(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Tan J., Ong R., Hibberd M.L., Seielstad M.;
RT "Genetic variation in immune response genes.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
RP TYR-113.
RC TISSUE=Liver;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
RA Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
RA Rogers J., Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [8]
RP PROTEIN SEQUENCE OF 26-50 (ISOFORM 1).
RC TISSUE=Plasma;
RX PubMed=7498469; DOI=10.1016/0014-5793(95)01205-S;
RA Edgar P.F.;
RT "Hucolin, a new corticosteroid-binding protein from human plasma with
RT structural similarities to ficolins, transforming growth factor-beta
RT 1-binding proteins.";
RL FEBS Lett. 375:159-161(1995).
RN [9]
RP PROTEIN SEQUENCE OF 65-99; 191-198 AND 218-228 (ISOFORM 1), SUBUNIT,
RP AND HYDROXYLATION AT PRO-77; PRO-80 AND PRO-86.
RC TISSUE=Plasma;
RX PubMed=8586615;
RA Harumiya S., Omori A., Sugiura T., Fukumoto Y., Tachikawa H.,
RA Fujimoto D.;
RT "EBP-37, a new elastin-binding protein in human plasma: structural
RT similarity to ficolins, transforming growth factor-beta 1-binding
RT proteins.";
RL J. Biochem. 117:1029-1035(1995).
RN [10]
RP FUNCTION, AND INTERACTION WITH MASP1 AND MASP2.
RX PubMed=10679061;
RA Matsushita M., Endo Y., Fujita T.;
RT "Complement-activating complex of ficolin and mannose-binding lectin-
RT associated serine protease.";
RL J. Immunol. 164:2281-2284(2000).
RN [11]
RP VARIANT [LARGE SCALE ANALYSIS] LEU-80.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal
RT cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: May function in innate immunity through activation of
CC the lectin complement pathway. Calcium-dependent and GlcNAc-
CC binding lectin. Enhances phagocytosis of S.typhimurium by
CC neutrophils, suggesting an opsonic effect via the collagen region.
CC -!- SUBUNIT: Homopolymer; disulfide-linked. Interacts with elastin.
CC Interacts with MASP1 and MASP2.
CC -!- INTERACTION:
CC Q07954:LRP1; NbExp=2; IntAct=EBI-7468784, EBI-1046087;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q15485-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q15485-2; Sequence=VSP_030027;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma.
CC -!- DOMAIN: The fibrinogen-like domain (FBG) contains potential
CC calcium-binding sites that may be involved in carbohydrate
CC binding.
CC -!- SIMILARITY: Belongs to the ficolin lectin family.
CC -!- SIMILARITY: Contains 1 collagen-like domain.
CC -!- SIMILARITY: Contains 1 fibrinogen C-terminal domain.
CC -----------------------------------------------------------------------
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CC Distributed under the Creative Commons Attribution-NoDerivs License
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DR EMBL; D63160; BAA09636.1; -; Genomic_DNA.
DR EMBL; D49353; BAA08352.1; -; mRNA.
DR EMBL; DQ217935; ABB01005.1; -; Genomic_DNA.
DR EMBL; AK290843; BAF83532.1; -; mRNA.
DR EMBL; AL603650; CAI39861.1; -; Genomic_DNA.
DR EMBL; CH471090; EAW88133.1; -; Genomic_DNA.
DR EMBL; CH471090; EAW88135.1; -; Genomic_DNA.
DR EMBL; BC069572; AAH69572.1; -; mRNA.
DR EMBL; BC069825; AAH69825.1; -; mRNA.
DR PIR; PH0263; PH0263.
DR PIR; S68005; S68005.
DR RefSeq; NP_004099.2; NM_004108.2.
DR RefSeq; NP_056652.1; NM_015837.2.
DR UniGene; Hs.54517; -.
DR PDB; 2J0G; X-ray; 2.85 A; A/B/C/D/E/F=97-313.
DR PDB; 2J0H; X-ray; 2.85 A; A/B/C/D/E/F=97-313.
DR PDB; 2J0Y; X-ray; 2.35 A; A/B/C/D/E/F=97-313.
DR PDB; 2J1G; X-ray; 1.95 A; A/B/C/D/E/F=97-313.
DR PDB; 2J2P; X-ray; 2.80 A; A/B/C/D/E/F=97-313.
DR PDB; 2J3F; X-ray; 2.80 A; A/B/C/D/E/F=95-313.
DR PDB; 2J3G; X-ray; 2.50 A; A/B/C/D/E/F=97-313.
DR PDB; 2J3O; X-ray; 2.65 A; A/B/C/D/E/F=95-313.
DR PDB; 2J3U; X-ray; 2.15 A; A/B/C/D/E/F=97-313.
DR PDB; 2J61; X-ray; 2.70 A; A/B=97-313.
DR PDBsum; 2J0G; -.
DR PDBsum; 2J0H; -.
DR PDBsum; 2J0Y; -.
DR PDBsum; 2J1G; -.
DR PDBsum; 2J2P; -.
DR PDBsum; 2J3F; -.
DR PDBsum; 2J3G; -.
DR PDBsum; 2J3O; -.
DR PDBsum; 2J3U; -.
DR PDBsum; 2J61; -.
DR ProteinModelPortal; Q15485; -.
DR SMR; Q15485; 62-92, 97-313.
DR IntAct; Q15485; 2.
DR MINT; MINT-5223224; -.
DR STRING; 9606.ENSP00000291744; -.
DR DMDM; 166214934; -.
DR PaxDb; Q15485; -.
DR PRIDE; Q15485; -.
DR Ensembl; ENST00000291744; ENSP00000291744; ENSG00000160339.
DR Ensembl; ENST00000350339; ENSP00000291741; ENSG00000160339.
DR GeneID; 2220; -.
DR KEGG; hsa:2220; -.
DR UCSC; uc004cfg.1; human.
DR CTD; 2220; -.
DR GeneCards; GC09P137772; -.
DR HGNC; HGNC:3624; FCN2.
DR MIM; 601624; gene.
DR neXtProt; NX_Q15485; -.
DR PharmGKB; PA28070; -.
DR eggNOG; NOG249945; -.
DR HOGENOM; HOG000037127; -.
DR HOVERGEN; HBG001644; -.
DR KO; K10104; -.
DR OMA; NTGNCAV; -.
DR OrthoDB; EOG7X9G60; -.
DR PhylomeDB; Q15485; -.
DR Reactome; REACT_6900; Immune System.
DR EvolutionaryTrace; Q15485; -.
DR GeneWiki; FCN2; -.
DR GenomeRNAi; 2220; -.
DR NextBio; 9005; -.
DR PRO; PR:Q15485; -.
DR Bgee; Q15485; -.
DR CleanEx; HS_FCN2; -.
DR Genevestigator; Q15485; -.
DR GO; GO:0005581; C:collagen; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0003823; F:antigen binding; TAS:ProtInc.
DR GO; GO:0005509; F:calcium ion binding; TAS:ProtInc.
DR GO; GO:0030246; F:carbohydrate binding; TAS:ProtInc.
DR GO; GO:0001867; P:complement activation, lectin pathway; TAS:Reactome.
DR GO; GO:0008228; P:opsonization; TAS:ProtInc.
DR Gene3D; 3.90.215.10; -; 1.
DR Gene3D; 4.10.530.10; -; 1.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR014716; Fibrinogen_a/b/g_C_1.
DR InterPro; IPR014715; Fibrinogen_a/b/g_C_2.
DR InterPro; IPR002181; Fibrinogen_a/b/g_C_dom.
DR InterPro; IPR020837; Fibrinogen_CS.
DR Pfam; PF01391; Collagen; 1.
DR Pfam; PF00147; Fibrinogen_C; 1.
DR SMART; SM00186; FBG; 1.
DR SUPFAM; SSF56496; SSF56496; 1.
DR PROSITE; PS00514; FIBRINOGEN_C_1; 1.
DR PROSITE; PS51406; FIBRINOGEN_C_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Collagen;
KW Complement activation lectin pathway; Complete proteome;
KW Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Hydroxylation; Immunity; Innate immunity; Lectin; Polymorphism;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1 25 Potential.
FT CHAIN 26 313 Ficolin-2.
FT /FTId=PRO_0000009139.
FT DOMAIN 51 92 Collagen-like.
FT DOMAIN 96 313 Fibrinogen C-terminal.
FT MOD_RES 77 77 Hydroxyproline.
FT MOD_RES 80 80 Hydroxyproline.
FT MOD_RES 86 86 Hydroxyproline.
FT CARBOHYD 240 240 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 300 300 N-linked (GlcNAc...) (Potential).
FT VAR_SEQ 34 71 Missing (in isoform 2).
FT /FTId=VSP_030027.
FT VARIANT 80 80 P -> L (in a colorectal cancer sample;
FT somatic mutation).
FT /FTId=VAR_036342.
FT VARIANT 113 113 H -> Y (in dbSNP:rs17549179).
FT /FTId=VAR_049072.
FT VARIANT 117 117 G -> S (in dbSNP:rs12684476).
FT /FTId=VAR_049073.
FT VARIANT 236 236 T -> M (in dbSNP:rs17549193).
FT /FTId=VAR_049074.
FT VARIANT 258 258 A -> S (in dbSNP:rs7851696).
FT /FTId=VAR_049075.
FT CONFLICT 61 61 P -> D (in Ref. 1; BAA08352 and 2;
FT ABB01005).
FT CONFLICT 98 98 C -> A (in Ref. 9; AA sequence).
FT STRAND 99 101
FT HELIX 105 110
FT STRAND 115 122
FT STRAND 124 126
FT STRAND 128 134
FT HELIX 137 139
FT STRAND 142 151
FT HELIX 159 164
FT STRAND 166 168
FT HELIX 177 182
FT STRAND 185 187
FT STRAND 191 196
FT STRAND 198 200
FT STRAND 202 208
FT STRAND 210 212
FT TURN 215 219
FT STRAND 221 223
FT STRAND 226 228
FT HELIX 236 238
FT STRAND 246 248
FT STRAND 251 255
FT HELIX 258 261
FT STRAND 263 265
FT STRAND 268 270
FT STRAND 272 274
FT STRAND 285 288
FT STRAND 290 293
FT TURN 294 297
FT STRAND 299 302
FT STRAND 304 310
SQ SEQUENCE 313 AA; 34001 MW; D363029846CCB3C9 CRC64;
MELDRAVGVL GAATLLLSFL GMAWALQAAD TCPEVKMVGL EGSDKLTILR GCPGLPGAPG
PKGEAGTNGK RGERGPPGPP GKAGPPGPNG APGEPQPCLT GPRTCKDLLD RGHFLSGWHT
IYLPDCRPLT VLCDMDTDGG GWTVFQRRVD GSVDFYRDWA TYKQGFGSRL GEFWLGNDNI
HALTAQGTSE LRVDLVDFED NYQFAKYRSF KVADEAEKYN LVLGAFVEGS AGDSLTFHNN
QSFSTKDQDN DLNTGNCAVM FQGAWWYKNC HVSNLNGRYL RGTHGSFANG INWKSGKGYN
YSYKVSEMKV RPA
//
MIM
601624
*RECORD*
*FIELD* NO
601624
*FIELD* TI
*601624 FICOLIN 2; FCN2
;;COLLAGEN/FIBRINOGEN DOMAIN-CONTAINING LECTIN 2 P35;;
OPSONIN P35
read more*FIELD* TX
CLONING
Matsushita et al. (1996) reported the cloning and characterization of
P35, a human lectin with collagen and fibrinogen domains. The P35 gene
encodes ficolin-2 (FCN2). Endo et al. (1996) isolated genomic clones for
P35 and a related gene shown to be identical to ficolin-1 (FCN1;
601252).
GENE STRUCTURE
Hummelshoj et al. (2005) noted that the FCN2 gene contains 8 exons.
MAPPING
Endo et al. (1996) mapped the FCN2 gene to chromosome 9q34 by
fluorescence in situ hybridization.
MOLECULAR GENETICS
Serum concentration of ficolin-2 varies considerably in healthy
individuals. Hummelshoj et al. (2005) sequenced the promoter region,
exons, and intron-exon boundaries of FCN2 in 157 Danish Caucasians, and
measured ficolin-2 concentrations in serum and N-acetylglucosamine
(GlcNAc) binding. FCN2 promoter polymorphisms were associated with
marked changes in the ficolin-2 serum concentration, whereas 2
nonsynonymous SNPs (dbSNP rs17549193 and dbSNP rs7851696) clustered in
exon 8 encoding the fibrinogen-like domain were associated with
decreased and increased GlcNAc binding, respectively. Hummelshoj et al.
(2005) suggested that functional polymorphic sites may regulate both the
expression and function of ficolin-2.
EVOLUTION
Endo et al. (2012) noted that human FCN1 is the ortholog of mouse Fcnb.
Human FCN2 is closely related to mouse Fcna, but the genes appear to
have evolved independently in each murine and primate lineage. The human
FCN3 gene (604973) is a pseudogene in mouse.
ANIMAL MODEL
Endo et al. (2012) noted that ficolins and mannose-binding lectin (MBL,
or MBL2; 154545) are complexed with MBL-associated serine proteases
(MASPs; see 600521). MBL is important in both autoimmune and infectious
diseases. Endo et al. (2012) found that Fcna -/- mice and Fcna -/- Fcnb
-/- mice lacked complement activation in sera due to the absence of
complexes of Fcna and MASPs. Transnasal challenge of mice with a
Streptococcus pneumoniae strain recognized by ficolins, but not by Mbl,
resulted in reduced mouse survival and higher bacterial loads in Fcna
-/-, Fcnb -/-, and Fcna -/- Fcnb -/- mice. Reconstitution of the
Fcna-mediated lectin pathway with an Fcna-encoding plasmid prior to
infection improved survival of Fcna -/- mice, but not Fcna -/- Fcnb -/-
mice, indicating that both Fcna and Fcnb are essential in defense
against S. pneumoniae. Endo et al. (2012) proposed that FCNA and FCNB
have a crucial role in defense against pneumococcal infection through
the lectin complement pathway.
*FIELD* RF
1. Endo, Y.; Sato, Y.; Matsushita, M.; Fujita, T.: Cloning and characterization
of the human lectin P35 gene and its related gene. Genomics 36:
515-521, 1996.
2. Endo, Y.; Takahashi, M.; Iwaki, D.; Ishida, Y.; Nakazawa, N.; Kodama,
T.; Matsuzaka, T.; Kanno, K.; Liu, Y.; Tsuchiya, K.; Kawamura, I.;
Ikawa, M.; Waguri, S.; Wada, I.; Matsushita, M.; Schwaeble, W. J.;
Fujita, T.: Mice deficient in ficolin, a lectin component pathway
recognition molecule, are susceptible to Streptococcus pneumoniae
infection. J. Immun. 189: 5860-5866, 2012.
3. Hummelshoj, T.; Munthe-Fog, L.; Madsen, H. O.; Fujita, T.; Matsushita,
M.; Garred, P.: Polymorphisms in the FCN2 gene determine serum variation
and function of ficolin-2. Hum. Molec. Genet. 14: 1651-1658, 2005.
Note: Erratum: Hum. Molec. Genet. 15: 163-165, 2006.
4. Matsushita, M.; Endo, Y.; Taira, S.; Sato, Y.; Fujita, T.; Ichikawa,
N.; Nakata, M.; Misuochi, T.: A novel human lectin with collagen-
and fibrinogen-like domains which functions as an opsonin. J. Biol.
Chem. 271: 2448-2454, 1996.
*FIELD* CN
Matthew B. Gross - updated: 06/20/2013
Paul J. Converse - updated: 6/20/2013
George E. Tiller - updated: 6/16/2008
*FIELD* CD
Mark H. Paalman: 1/11/1997
*FIELD* ED
mgross: 06/20/2013
mgross: 6/20/2013
wwang: 11/4/2009
ckniffin: 10/29/2009
carol: 7/9/2009
wwang: 6/19/2008
terry: 6/16/2008
mgross: 12/13/1999
mark: 1/11/1997
*RECORD*
*FIELD* NO
601624
*FIELD* TI
*601624 FICOLIN 2; FCN2
;;COLLAGEN/FIBRINOGEN DOMAIN-CONTAINING LECTIN 2 P35;;
OPSONIN P35
read more*FIELD* TX
CLONING
Matsushita et al. (1996) reported the cloning and characterization of
P35, a human lectin with collagen and fibrinogen domains. The P35 gene
encodes ficolin-2 (FCN2). Endo et al. (1996) isolated genomic clones for
P35 and a related gene shown to be identical to ficolin-1 (FCN1;
601252).
GENE STRUCTURE
Hummelshoj et al. (2005) noted that the FCN2 gene contains 8 exons.
MAPPING
Endo et al. (1996) mapped the FCN2 gene to chromosome 9q34 by
fluorescence in situ hybridization.
MOLECULAR GENETICS
Serum concentration of ficolin-2 varies considerably in healthy
individuals. Hummelshoj et al. (2005) sequenced the promoter region,
exons, and intron-exon boundaries of FCN2 in 157 Danish Caucasians, and
measured ficolin-2 concentrations in serum and N-acetylglucosamine
(GlcNAc) binding. FCN2 promoter polymorphisms were associated with
marked changes in the ficolin-2 serum concentration, whereas 2
nonsynonymous SNPs (dbSNP rs17549193 and dbSNP rs7851696) clustered in
exon 8 encoding the fibrinogen-like domain were associated with
decreased and increased GlcNAc binding, respectively. Hummelshoj et al.
(2005) suggested that functional polymorphic sites may regulate both the
expression and function of ficolin-2.
EVOLUTION
Endo et al. (2012) noted that human FCN1 is the ortholog of mouse Fcnb.
Human FCN2 is closely related to mouse Fcna, but the genes appear to
have evolved independently in each murine and primate lineage. The human
FCN3 gene (604973) is a pseudogene in mouse.
ANIMAL MODEL
Endo et al. (2012) noted that ficolins and mannose-binding lectin (MBL,
or MBL2; 154545) are complexed with MBL-associated serine proteases
(MASPs; see 600521). MBL is important in both autoimmune and infectious
diseases. Endo et al. (2012) found that Fcna -/- mice and Fcna -/- Fcnb
-/- mice lacked complement activation in sera due to the absence of
complexes of Fcna and MASPs. Transnasal challenge of mice with a
Streptococcus pneumoniae strain recognized by ficolins, but not by Mbl,
resulted in reduced mouse survival and higher bacterial loads in Fcna
-/-, Fcnb -/-, and Fcna -/- Fcnb -/- mice. Reconstitution of the
Fcna-mediated lectin pathway with an Fcna-encoding plasmid prior to
infection improved survival of Fcna -/- mice, but not Fcna -/- Fcnb -/-
mice, indicating that both Fcna and Fcnb are essential in defense
against S. pneumoniae. Endo et al. (2012) proposed that FCNA and FCNB
have a crucial role in defense against pneumococcal infection through
the lectin complement pathway.
*FIELD* RF
1. Endo, Y.; Sato, Y.; Matsushita, M.; Fujita, T.: Cloning and characterization
of the human lectin P35 gene and its related gene. Genomics 36:
515-521, 1996.
2. Endo, Y.; Takahashi, M.; Iwaki, D.; Ishida, Y.; Nakazawa, N.; Kodama,
T.; Matsuzaka, T.; Kanno, K.; Liu, Y.; Tsuchiya, K.; Kawamura, I.;
Ikawa, M.; Waguri, S.; Wada, I.; Matsushita, M.; Schwaeble, W. J.;
Fujita, T.: Mice deficient in ficolin, a lectin component pathway
recognition molecule, are susceptible to Streptococcus pneumoniae
infection. J. Immun. 189: 5860-5866, 2012.
3. Hummelshoj, T.; Munthe-Fog, L.; Madsen, H. O.; Fujita, T.; Matsushita,
M.; Garred, P.: Polymorphisms in the FCN2 gene determine serum variation
and function of ficolin-2. Hum. Molec. Genet. 14: 1651-1658, 2005.
Note: Erratum: Hum. Molec. Genet. 15: 163-165, 2006.
4. Matsushita, M.; Endo, Y.; Taira, S.; Sato, Y.; Fujita, T.; Ichikawa,
N.; Nakata, M.; Misuochi, T.: A novel human lectin with collagen-
and fibrinogen-like domains which functions as an opsonin. J. Biol.
Chem. 271: 2448-2454, 1996.
*FIELD* CN
Matthew B. Gross - updated: 06/20/2013
Paul J. Converse - updated: 6/20/2013
George E. Tiller - updated: 6/16/2008
*FIELD* CD
Mark H. Paalman: 1/11/1997
*FIELD* ED
mgross: 06/20/2013
mgross: 6/20/2013
wwang: 11/4/2009
ckniffin: 10/29/2009
carol: 7/9/2009
wwang: 6/19/2008
terry: 6/16/2008
mgross: 12/13/1999
mark: 1/11/1997