Full text data of ORM2
ORM2
(AGP2)
[Confidence: low (only semi-automatic identification from reviews)]
Alpha-1-acid glycoprotein 2; AGP 2 (Orosomucoid-2; OMD 2; Flags: Precursor)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Alpha-1-acid glycoprotein 2; AGP 2 (Orosomucoid-2; OMD 2; Flags: Precursor)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P19652
ID A1AG2_HUMAN Reviewed; 201 AA.
AC P19652; B2R5L2; Q16571; Q5T538; Q6IB74;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-APR-1993, sequence version 2.
DT 22-JAN-2014, entry version 146.
DE RecName: Full=Alpha-1-acid glycoprotein 2;
DE Short=AGP 2;
DE AltName: Full=Orosomucoid-2;
DE Short=OMD 2;
DE Flags: Precursor;
GN Name=ORM2; Synonyms=AGP2;
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=2822385;
RA Dente L., Pizza M.G., Metspalu A., Cortese R.;
RT "Structure and expression of the genes coding for human alpha 1-acid
RT glycoprotein.";
RL EMBO J. 6:2289-2296(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2970990; DOI=10.1016/0378-1119(88)90228-4;
RA Merritt C.M., Board P.G.;
RT "Structure and characterisation of a duplicated human alpha 1 acid
RT glycoprotein gene.";
RL Gene 66:97-106(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
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].
RC TISSUE=Skeletal muscle;
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 DISULFIDE BONDS.
RX PubMed=4603214; DOI=10.1021/bi00710a006;
RA Schmid K., Buergi W., Collins J.H., Nanno S.;
RT "The disulfide bonds of alpha1-acid glycoprotein.";
RL Biochemistry 13:2694-2697(1974).
RN [9]
RP GLYCOSYLATION AT ASN-33; ASN-56; ASN-72; ASN-93 AND ASN-103.
RX PubMed=1567356;
RA Treuheit M.J., Costello C.E., Halsall H.B.;
RT "Analysis of the five glycosylation sites of human alpha 1-acid
RT glycoprotein.";
RL Biochem. J. 283:105-112(1992).
RN [10]
RP PYROGLUTAMATE FORMATION AT GLN-19, GLYCOSYLATION AT ASN-33 AND ASN-93,
RP AND MASS SPECTROMETRY.
RX PubMed=15253437; DOI=10.1021/pr034112b;
RA Hagglund P., Bunkenborg J., Elortza F., Jensen O.N., Roepstorff P.;
RT "A new strategy for identification of N-glycosylated proteins and
RT unambiguous assignment of their glycosylation sites using HILIC
RT enrichment and partial deglycosylation.";
RL J. Proteome Res. 3:556-566(2004).
RN [11]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-33, AND MASS SPECTROMETRY.
RC TISSUE=Bile;
RX PubMed=15084671; DOI=10.1074/mcp.M400015-MCP200;
RA Kristiansen T.Z., Bunkenborg J., Gronborg M., Molina H.,
RA Thuluvath P.J., Argani P., Goggins M.G., Maitra A., Pandey A.;
RT "A proteomic analysis of human bile.";
RL Mol. Cell. Proteomics 3:715-728(2004).
RN [12]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-33; ASN-56; ASN-72 AND
RP ASN-93, AND MASS SPECTROMETRY.
RC TISSUE=Plasma;
RX PubMed=14760718; DOI=10.1002/pmic.200300556;
RA Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.;
RT "Screening for N-glycosylated proteins by liquid chromatography mass
RT spectrometry.";
RL Proteomics 4:454-465(2004).
RN [13]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-33; ASN-56; ASN-72; ASN-93
RP AND ASN-103, 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 [14]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-33; ASN-56; ASN-93 AND
RP ASN-103, AND MASS 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 [15]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-33, STRUCTURE OF
RP CARBOHYDRATES, AND MASS SPECTROMETRY.
RC TISSUE=Cerebrospinal fluid;
RX PubMed=19838169; DOI=10.1038/nmeth.1392;
RA Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E.,
RA Brinkmalm G., Larson G.;
RT "Enrichment of glycopeptides for glycan structure and attachment site
RT identification.";
RL Nat. Methods 6:809-811(2009).
RN [16]
RP GLYCOSYLATION AT ASN-33, STRUCTURE OF CARBOHYDRATES, AND MASS
RP SPECTROMETRY.
RX PubMed=22171320; DOI=10.1074/mcp.M111.013649;
RA Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.;
RT "Human urinary glycoproteomics; attachment site specific analysis of
RT N-and O-linked glycosylations by CID and ECD.";
RL Mol. Cell. Proteomics 0:0-0(2011).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 19-201 OF VARIANT ARG-167 IN
RP COMPLEXES WITH DISOPYRAMIDE; AMITRIPTYLINE AND CHLORPROMAZINE,
RP FUNCTION, DISULFIDE BONDS, AND DOMAIN.
RX PubMed=21349832; DOI=10.1074/jbc.M110.208926;
RA Nishi K., Ono T., Nakamura T., Fukunaga N., Izumi M., Watanabe H.,
RA Suenaga A., Maruyama T., Yamagata Y., Curry S., Otagiri M.;
RT "Structural insights into differences in drug-binding selectivity
RT between two forms of human {alpha}1-acid glycoprotein genetic
RT variants, the A and F1*S forms.";
RL J. Biol. Chem. 286:14427-14434(2011).
CC -!- FUNCTION: Functions as transport protein in the blood stream.
CC Binds various hydrophobic ligands in the interior of its beta-
CC barrel domain. Also binds synthetic drugs and influences their
CC distribution and availability. Appears to function in modulating
CC the activity of the immune system during the acute-phase reaction.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma.
CC -!- INDUCTION: Synthesis is controlled by glucocorticoids,
CC interleukin-1 and interleukin-6, It increases 5- to 50-fold upon
CC inflammation.
CC -!- DOMAIN: Contains a beta-barrel that binds various ligands in its
CC interior.
CC -!- PTM: N-glycosylated. N-glycan heterogeneity at Asn-33: Hex5HexNAc4
CC (minor), Hex6HexNAc5 (major) and dHex1Hex6HexNAc5 (minor).
CC -!- POLYMORPHISM: Many different variants of ORM2 are known.
CC -!- SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA29873.2; Type=Erroneous gene model prediction;
CC Sequence=CAA29874.1; Type=Erroneous gene model prediction;
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DR EMBL; X06675; CAA29874.1; ALT_SEQ; Genomic_DNA.
DR EMBL; X05780; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; X06674; CAA29873.2; ALT_SEQ; Genomic_DNA.
DR EMBL; X06676; CAA29873.2; JOINED; Genomic_DNA.
DR EMBL; X06677; CAA29873.2; JOINED; Genomic_DNA.
DR EMBL; X06678; CAA29873.2; JOINED; Genomic_DNA.
DR EMBL; X06679; CAA29873.2; JOINED; Genomic_DNA.
DR EMBL; X06680; CAA29873.2; JOINED; Genomic_DNA.
DR EMBL; X05784; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; M21540; AAA51549.1; -; Genomic_DNA.
DR EMBL; AK312226; BAG35159.1; -; mRNA.
DR EMBL; CR456930; CAG33211.1; -; mRNA.
DR EMBL; AL356796; CAI16860.1; -; Genomic_DNA.
DR EMBL; CH471090; EAW87417.1; -; Genomic_DNA.
DR EMBL; BC015964; AAH15964.1; -; mRNA.
DR EMBL; BC056239; AAH56239.1; -; mRNA.
DR PIR; JT0326; OMHU2.
DR RefSeq; NP_000599.1; NM_000608.2.
DR UniGene; Hs.719954; -.
DR PDB; 3APU; X-ray; 2.10 A; A/B=19-201.
DR PDB; 3APV; X-ray; 2.15 A; A/B=19-201.
DR PDB; 3APW; X-ray; 2.20 A; A/B=19-201.
DR PDB; 3APX; X-ray; 2.20 A; A=19-201.
DR PDBsum; 3APU; -.
DR PDBsum; 3APV; -.
DR PDBsum; 3APW; -.
DR PDBsum; 3APX; -.
DR ProteinModelPortal; P19652; -.
DR SMR; P19652; 19-196.
DR IntAct; P19652; 3.
DR STRING; 9606.ENSP00000394936; -.
DR ChEMBL; CHEMBL5958; -.
DR PhosphoSite; P19652; -.
DR UniCarbKB; P19652; -.
DR DMDM; 231458; -.
DR DOSAC-COBS-2DPAGE; P19652; -.
DR SWISS-2DPAGE; P19652; -.
DR PeptideAtlas; P19652; -.
DR PRIDE; P19652; -.
DR DNASU; 5005; -.
DR Ensembl; ENST00000431067; ENSP00000394936; ENSG00000228278.
DR GeneID; 5005; -.
DR KEGG; hsa:5005; -.
DR UCSC; uc004bil.3; human.
DR CTD; 5005; -.
DR GeneCards; GC09P117092; -.
DR HGNC; HGNC:8499; ORM2.
DR HPA; HPA046438; -.
DR MIM; 138610; gene.
DR neXtProt; NX_P19652; -.
DR PharmGKB; PA32818; -.
DR HOGENOM; HOG000125170; -.
DR HOVERGEN; HBG000035; -.
DR InParanoid; P19652; -.
DR KO; K17308; -.
DR OMA; FHEALKC; -.
DR OrthoDB; EOG7B5WXT; -.
DR EvolutionaryTrace; P19652; -.
DR GenomeRNAi; 5005; -.
DR NextBio; 19276; -.
DR PRO; PR:P19652; -.
DR ArrayExpress; P19652; -.
DR Bgee; P19652; -.
DR Genevestigator; P19652; -.
DR GO; GO:0005615; C:extracellular space; TAS:ProtInc.
DR GO; GO:0006953; P:acute-phase response; TAS:ProtInc.
DR GO; GO:0002682; P:regulation of immune system process; IEA:InterPro.
DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR Gene3D; 2.40.128.20; -; 1.
DR InterPro; IPR001500; A1A_glycop.
DR InterPro; IPR012674; Calycin.
DR InterPro; IPR011038; Calycin-like.
DR InterPro; IPR000566; Lipocln_cytosolic_FA-bd_dom.
DR PANTHER; PTHR11967; PTHR11967; 1.
DR Pfam; PF00061; Lipocalin; 1.
DR PIRSF; PIRSF036899; AGP; 1.
DR PRINTS; PR00708; A1AGLPROTEIN.
DR SUPFAM; SSF50814; SSF50814; 1.
DR PROSITE; PS00213; LIPOCALIN; FALSE_NEG.
PE 1: Evidence at protein level;
KW 3D-structure; Acute phase; Complete proteome; Disulfide bond;
KW Glycoprotein; Polymorphism; Pyrrolidone carboxylic acid;
KW Reference proteome; Secreted; Signal; Transport.
FT SIGNAL 1 18
FT CHAIN 19 201 Alpha-1-acid glycoprotein 2.
FT /FTId=PRO_0000017861.
FT MOD_RES 19 19 Pyrrolidone carboxylic acid.
FT CARBOHYD 33 33 N-linked (GlcNAc...) (complex).
FT CARBOHYD 56 56 N-linked (GlcNAc...).
FT CARBOHYD 72 72 N-linked (GlcNAc...).
FT CARBOHYD 93 93 N-linked (GlcNAc...).
FT CARBOHYD 103 103 N-linked (GlcNAc...).
FT /FTId=CAR_000171.
FT DISULFID 23 165
FT DISULFID 90 183
FT VARIANT 38 38 R -> Q (in dbSNP:rs17650).
FT /FTId=VAR_014667.
FT VARIANT 99 99 V -> A (in dbSNP:rs2636889).
FT /FTId=VAR_050172.
FT VARIANT 141 141 G -> R (in dbSNP:rs12685968).
FT /FTId=VAR_050173.
FT VARIANT 167 167 C -> R (in dbSNP:rs1126777).
FT /FTId=VAR_050174.
FT VARIANT 174 174 M -> V (in dbSNP:rs2636890).
FT /FTId=VAR_050175.
FT CONFLICT 32 32 T -> I (in Ref. 4; CAG33211).
FT CONFLICT 102 102 E -> D (in Ref. 3; BAG35159).
FT CONFLICT 125 125 T -> I (in Ref. 3; BAG35159).
FT CONFLICT 162 162 A -> V (in Ref. 3; BAG35159).
FT CONFLICT 189 189 Q -> H (in Ref. 3; BAG35159).
FT TURN 20 23
FT HELIX 24 26
FT HELIX 33 39
FT STRAND 41 51
FT HELIX 53 60
FT STRAND 62 72
FT TURN 73 76
FT STRAND 77 86
FT STRAND 89 100
FT TURN 101 104
FT STRAND 105 110
FT STRAND 113 120
FT STRAND 127 133
FT TURN 137 139
FT STRAND 141 150
FT HELIX 153 165
FT HELIX 170 172
FT HELIX 178 180
FT HELIX 184 191
SQ SEQUENCE 201 AA; 23603 MW; 49167ABCC22933B9 CRC64;
MALSWVLTVL SLLPLLEAQI PLCANLVPVP ITNATLDRIT GKWFYIASAF RNEEYNKSVQ
EIQATFFYFT PNKTEDTIFL REYQTRQNQC FYNSSYLNVQ RENGTVSRYE GGREHVAHLL
FLRDTKTLMF GSYLDDEKNW GLSFYADKPE TTKEQLGEFY EALDCLCIPR SDVMYTDWKK
DKCEPLEKQH EKERKQEEGE S
//
ID A1AG2_HUMAN Reviewed; 201 AA.
AC P19652; B2R5L2; Q16571; Q5T538; Q6IB74;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-APR-1993, sequence version 2.
DT 22-JAN-2014, entry version 146.
DE RecName: Full=Alpha-1-acid glycoprotein 2;
DE Short=AGP 2;
DE AltName: Full=Orosomucoid-2;
DE Short=OMD 2;
DE Flags: Precursor;
GN Name=ORM2; Synonyms=AGP2;
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=2822385;
RA Dente L., Pizza M.G., Metspalu A., Cortese R.;
RT "Structure and expression of the genes coding for human alpha 1-acid
RT glycoprotein.";
RL EMBO J. 6:2289-2296(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2970990; DOI=10.1016/0378-1119(88)90228-4;
RA Merritt C.M., Board P.G.;
RT "Structure and characterisation of a duplicated human alpha 1 acid
RT glycoprotein gene.";
RL Gene 66:97-106(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
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].
RC TISSUE=Skeletal muscle;
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 DISULFIDE BONDS.
RX PubMed=4603214; DOI=10.1021/bi00710a006;
RA Schmid K., Buergi W., Collins J.H., Nanno S.;
RT "The disulfide bonds of alpha1-acid glycoprotein.";
RL Biochemistry 13:2694-2697(1974).
RN [9]
RP GLYCOSYLATION AT ASN-33; ASN-56; ASN-72; ASN-93 AND ASN-103.
RX PubMed=1567356;
RA Treuheit M.J., Costello C.E., Halsall H.B.;
RT "Analysis of the five glycosylation sites of human alpha 1-acid
RT glycoprotein.";
RL Biochem. J. 283:105-112(1992).
RN [10]
RP PYROGLUTAMATE FORMATION AT GLN-19, GLYCOSYLATION AT ASN-33 AND ASN-93,
RP AND MASS SPECTROMETRY.
RX PubMed=15253437; DOI=10.1021/pr034112b;
RA Hagglund P., Bunkenborg J., Elortza F., Jensen O.N., Roepstorff P.;
RT "A new strategy for identification of N-glycosylated proteins and
RT unambiguous assignment of their glycosylation sites using HILIC
RT enrichment and partial deglycosylation.";
RL J. Proteome Res. 3:556-566(2004).
RN [11]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-33, AND MASS SPECTROMETRY.
RC TISSUE=Bile;
RX PubMed=15084671; DOI=10.1074/mcp.M400015-MCP200;
RA Kristiansen T.Z., Bunkenborg J., Gronborg M., Molina H.,
RA Thuluvath P.J., Argani P., Goggins M.G., Maitra A., Pandey A.;
RT "A proteomic analysis of human bile.";
RL Mol. Cell. Proteomics 3:715-728(2004).
RN [12]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-33; ASN-56; ASN-72 AND
RP ASN-93, AND MASS SPECTROMETRY.
RC TISSUE=Plasma;
RX PubMed=14760718; DOI=10.1002/pmic.200300556;
RA Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.;
RT "Screening for N-glycosylated proteins by liquid chromatography mass
RT spectrometry.";
RL Proteomics 4:454-465(2004).
RN [13]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-33; ASN-56; ASN-72; ASN-93
RP AND ASN-103, 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 [14]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-33; ASN-56; ASN-93 AND
RP ASN-103, AND MASS 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 [15]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-33, STRUCTURE OF
RP CARBOHYDRATES, AND MASS SPECTROMETRY.
RC TISSUE=Cerebrospinal fluid;
RX PubMed=19838169; DOI=10.1038/nmeth.1392;
RA Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E.,
RA Brinkmalm G., Larson G.;
RT "Enrichment of glycopeptides for glycan structure and attachment site
RT identification.";
RL Nat. Methods 6:809-811(2009).
RN [16]
RP GLYCOSYLATION AT ASN-33, STRUCTURE OF CARBOHYDRATES, AND MASS
RP SPECTROMETRY.
RX PubMed=22171320; DOI=10.1074/mcp.M111.013649;
RA Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.;
RT "Human urinary glycoproteomics; attachment site specific analysis of
RT N-and O-linked glycosylations by CID and ECD.";
RL Mol. Cell. Proteomics 0:0-0(2011).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 19-201 OF VARIANT ARG-167 IN
RP COMPLEXES WITH DISOPYRAMIDE; AMITRIPTYLINE AND CHLORPROMAZINE,
RP FUNCTION, DISULFIDE BONDS, AND DOMAIN.
RX PubMed=21349832; DOI=10.1074/jbc.M110.208926;
RA Nishi K., Ono T., Nakamura T., Fukunaga N., Izumi M., Watanabe H.,
RA Suenaga A., Maruyama T., Yamagata Y., Curry S., Otagiri M.;
RT "Structural insights into differences in drug-binding selectivity
RT between two forms of human {alpha}1-acid glycoprotein genetic
RT variants, the A and F1*S forms.";
RL J. Biol. Chem. 286:14427-14434(2011).
CC -!- FUNCTION: Functions as transport protein in the blood stream.
CC Binds various hydrophobic ligands in the interior of its beta-
CC barrel domain. Also binds synthetic drugs and influences their
CC distribution and availability. Appears to function in modulating
CC the activity of the immune system during the acute-phase reaction.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma.
CC -!- INDUCTION: Synthesis is controlled by glucocorticoids,
CC interleukin-1 and interleukin-6, It increases 5- to 50-fold upon
CC inflammation.
CC -!- DOMAIN: Contains a beta-barrel that binds various ligands in its
CC interior.
CC -!- PTM: N-glycosylated. N-glycan heterogeneity at Asn-33: Hex5HexNAc4
CC (minor), Hex6HexNAc5 (major) and dHex1Hex6HexNAc5 (minor).
CC -!- POLYMORPHISM: Many different variants of ORM2 are known.
CC -!- SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA29873.2; Type=Erroneous gene model prediction;
CC Sequence=CAA29874.1; Type=Erroneous gene model prediction;
CC -----------------------------------------------------------------------
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DR EMBL; X06675; CAA29874.1; ALT_SEQ; Genomic_DNA.
DR EMBL; X05780; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; X06674; CAA29873.2; ALT_SEQ; Genomic_DNA.
DR EMBL; X06676; CAA29873.2; JOINED; Genomic_DNA.
DR EMBL; X06677; CAA29873.2; JOINED; Genomic_DNA.
DR EMBL; X06678; CAA29873.2; JOINED; Genomic_DNA.
DR EMBL; X06679; CAA29873.2; JOINED; Genomic_DNA.
DR EMBL; X06680; CAA29873.2; JOINED; Genomic_DNA.
DR EMBL; X05784; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; M21540; AAA51549.1; -; Genomic_DNA.
DR EMBL; AK312226; BAG35159.1; -; mRNA.
DR EMBL; CR456930; CAG33211.1; -; mRNA.
DR EMBL; AL356796; CAI16860.1; -; Genomic_DNA.
DR EMBL; CH471090; EAW87417.1; -; Genomic_DNA.
DR EMBL; BC015964; AAH15964.1; -; mRNA.
DR EMBL; BC056239; AAH56239.1; -; mRNA.
DR PIR; JT0326; OMHU2.
DR RefSeq; NP_000599.1; NM_000608.2.
DR UniGene; Hs.719954; -.
DR PDB; 3APU; X-ray; 2.10 A; A/B=19-201.
DR PDB; 3APV; X-ray; 2.15 A; A/B=19-201.
DR PDB; 3APW; X-ray; 2.20 A; A/B=19-201.
DR PDB; 3APX; X-ray; 2.20 A; A=19-201.
DR PDBsum; 3APU; -.
DR PDBsum; 3APV; -.
DR PDBsum; 3APW; -.
DR PDBsum; 3APX; -.
DR ProteinModelPortal; P19652; -.
DR SMR; P19652; 19-196.
DR IntAct; P19652; 3.
DR STRING; 9606.ENSP00000394936; -.
DR ChEMBL; CHEMBL5958; -.
DR PhosphoSite; P19652; -.
DR UniCarbKB; P19652; -.
DR DMDM; 231458; -.
DR DOSAC-COBS-2DPAGE; P19652; -.
DR SWISS-2DPAGE; P19652; -.
DR PeptideAtlas; P19652; -.
DR PRIDE; P19652; -.
DR DNASU; 5005; -.
DR Ensembl; ENST00000431067; ENSP00000394936; ENSG00000228278.
DR GeneID; 5005; -.
DR KEGG; hsa:5005; -.
DR UCSC; uc004bil.3; human.
DR CTD; 5005; -.
DR GeneCards; GC09P117092; -.
DR HGNC; HGNC:8499; ORM2.
DR HPA; HPA046438; -.
DR MIM; 138610; gene.
DR neXtProt; NX_P19652; -.
DR PharmGKB; PA32818; -.
DR HOGENOM; HOG000125170; -.
DR HOVERGEN; HBG000035; -.
DR InParanoid; P19652; -.
DR KO; K17308; -.
DR OMA; FHEALKC; -.
DR OrthoDB; EOG7B5WXT; -.
DR EvolutionaryTrace; P19652; -.
DR GenomeRNAi; 5005; -.
DR NextBio; 19276; -.
DR PRO; PR:P19652; -.
DR ArrayExpress; P19652; -.
DR Bgee; P19652; -.
DR Genevestigator; P19652; -.
DR GO; GO:0005615; C:extracellular space; TAS:ProtInc.
DR GO; GO:0006953; P:acute-phase response; TAS:ProtInc.
DR GO; GO:0002682; P:regulation of immune system process; IEA:InterPro.
DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR Gene3D; 2.40.128.20; -; 1.
DR InterPro; IPR001500; A1A_glycop.
DR InterPro; IPR012674; Calycin.
DR InterPro; IPR011038; Calycin-like.
DR InterPro; IPR000566; Lipocln_cytosolic_FA-bd_dom.
DR PANTHER; PTHR11967; PTHR11967; 1.
DR Pfam; PF00061; Lipocalin; 1.
DR PIRSF; PIRSF036899; AGP; 1.
DR PRINTS; PR00708; A1AGLPROTEIN.
DR SUPFAM; SSF50814; SSF50814; 1.
DR PROSITE; PS00213; LIPOCALIN; FALSE_NEG.
PE 1: Evidence at protein level;
KW 3D-structure; Acute phase; Complete proteome; Disulfide bond;
KW Glycoprotein; Polymorphism; Pyrrolidone carboxylic acid;
KW Reference proteome; Secreted; Signal; Transport.
FT SIGNAL 1 18
FT CHAIN 19 201 Alpha-1-acid glycoprotein 2.
FT /FTId=PRO_0000017861.
FT MOD_RES 19 19 Pyrrolidone carboxylic acid.
FT CARBOHYD 33 33 N-linked (GlcNAc...) (complex).
FT CARBOHYD 56 56 N-linked (GlcNAc...).
FT CARBOHYD 72 72 N-linked (GlcNAc...).
FT CARBOHYD 93 93 N-linked (GlcNAc...).
FT CARBOHYD 103 103 N-linked (GlcNAc...).
FT /FTId=CAR_000171.
FT DISULFID 23 165
FT DISULFID 90 183
FT VARIANT 38 38 R -> Q (in dbSNP:rs17650).
FT /FTId=VAR_014667.
FT VARIANT 99 99 V -> A (in dbSNP:rs2636889).
FT /FTId=VAR_050172.
FT VARIANT 141 141 G -> R (in dbSNP:rs12685968).
FT /FTId=VAR_050173.
FT VARIANT 167 167 C -> R (in dbSNP:rs1126777).
FT /FTId=VAR_050174.
FT VARIANT 174 174 M -> V (in dbSNP:rs2636890).
FT /FTId=VAR_050175.
FT CONFLICT 32 32 T -> I (in Ref. 4; CAG33211).
FT CONFLICT 102 102 E -> D (in Ref. 3; BAG35159).
FT CONFLICT 125 125 T -> I (in Ref. 3; BAG35159).
FT CONFLICT 162 162 A -> V (in Ref. 3; BAG35159).
FT CONFLICT 189 189 Q -> H (in Ref. 3; BAG35159).
FT TURN 20 23
FT HELIX 24 26
FT HELIX 33 39
FT STRAND 41 51
FT HELIX 53 60
FT STRAND 62 72
FT TURN 73 76
FT STRAND 77 86
FT STRAND 89 100
FT TURN 101 104
FT STRAND 105 110
FT STRAND 113 120
FT STRAND 127 133
FT TURN 137 139
FT STRAND 141 150
FT HELIX 153 165
FT HELIX 170 172
FT HELIX 178 180
FT HELIX 184 191
SQ SEQUENCE 201 AA; 23603 MW; 49167ABCC22933B9 CRC64;
MALSWVLTVL SLLPLLEAQI PLCANLVPVP ITNATLDRIT GKWFYIASAF RNEEYNKSVQ
EIQATFFYFT PNKTEDTIFL REYQTRQNQC FYNSSYLNVQ RENGTVSRYE GGREHVAHLL
FLRDTKTLMF GSYLDDEKNW GLSFYADKPE TTKEQLGEFY EALDCLCIPR SDVMYTDWKK
DKCEPLEKQH EKERKQEEGE S
//
MIM
138610
*RECORD*
*FIELD* NO
138610
*FIELD* TI
*138610 OROSOMUCOID 2; ORM2
;;GLYCOPROTEIN, ALPHA-1-ACID, OF SERUM, TYPE 2;;
ALPHA-1-ACID GLYCOPROTEIN, TYPE 2; AGP2
read more*FIELD* TX
Yuasa et al. (1986) performed orosomucoid phenotyping by isoelectric
focusing and immunoprinting. The band pattern of desialyzed ORM
indicated to these workers that the ORM system is controlled by 2
structural loci, ORM1 (138600) and ORM2. Whereas the ORM1 locus was
polymorphic, the ORM2 locus appeared to be monomorphic. Later, however,
Yuasa et al. (1987) demonstrated polymorphism of the ORM2 locus, with 6
alleles in the Japanese population. By studies of orosomucoid cDNA
clones isolated from mouse liver, Cooper and Papaconstantinou (1986)
showed that 2 species of ORM mRNA are transcribed from 2 distinct genes.
Escallon et al. (1987) presented evidence for the expression of a second
structural locus (ORM2) in human plasma as well as for the detection of
genetically determined variation at the ORM2 locus in American blacks by
the use of a sensitive enzyme-linked immunoblotting technique. After
thin-layer polyacrylamide isoelectric focusing (IEF) in gels containing
6 M urea, the isoprotein species coded by the second locus did not
segregate with the predominant alleles at the ORM1 locus. Variation in
ORM2 was not observed in U.S. whites or in several other populations
studied. Because of the low frequency and unlimited distribution of ORM2
variation, Escallon et al. (1987) were unable to test for linkage
between the 2 ORM loci.
By in situ hybridization using a cDNA clone for AGP2, Webb et al. (1988)
mapped both alpha-1-acid glycoprotein genes in the 9q34 band. Yuasa et
al. (1988) used a modified isoelectric focusing, in which glycerine was
omitted from gels, to differentiate ORM1 and ORM2 variants. They
demonstrated linkage disequilibrium between alleles at the 2 loci, thus
corroborating the close linkage demonstrated physically by Dente et al.
(1987). Merritt and Board (1988) presented the complete nucleotide
sequence of the ORM2 gene, which is located approximately 3.3 kb
downstream from ORM1. The derived amino acid sequence indicated at least
21 amino acid differences between the products of the 2 genes.
Data on gene frequencies of allelic variants were tabulated by
Roychoudhury and Nei (1988).
*FIELD* RF
1. Cooper, R.; Papaconstantinou, J.: Evidence of multiple alpha-1
acid glycoprotein genes in the mouse. J. Biol. Chem. 261: 1849-1853,
1986.
2. Dente, L.; Pizza, M. G.; Metspalu, A.; Cortese, R.: Structure
and expression of the genes coding for human alpha-1-acid glycoprotein.
EMBO J. 6: 2289-2296, 1987.
3. Escallon, M. H.; Ferrell, R. E.; Kamboh, M. I.: Genetic studies
of low-abundance human plasma proteins. V. Evidence for a second orosomucoid
structural locus (ORM2) expressed in plasma. Am. J. Hum. Genet. 41:
418-427, 1987.
4. Merritt, C. M.; Board, P. G.: Structure and characterisation of
a duplicated human alpha-1 acid glycoprotein gene. Gene 66: 97-106,
1988.
5. Roychoudhury, A. K.; Nei, M.: Human Polymorphic Genes: World Distribution.
New York: Oxford Univ. Press (pub.) 1988.
6. Webb, G. C.; Earle, M. E.; Merritt, C.; Board, P. G.: Localization
of human alpha-1 acid glycoprotein genes to 9q31-q34.1. Cytogenet.
Cell Genet. 47: 18-21, 1988.
7. Yuasa, I.; Suenaga, K.; Umetsu, K.; Ito, K.; Robinet-Levy, M.:
Orosomucoid (ORM) typing by isoelectric focusing: evidence for gene
duplication of ORM1 and genetic polymorphism of ORM2. Hum. Genet. 77:
255-258, 1987.
8. Yuasa, I.; Umetsu, K.; Suenaga, K.: Orosomucoid (ORM) typing by
isoelectric focusing: evidence for an additional duplicated ORM1 locus
haplotype and close linkage of two ORM loci. Am. J. Hum. Genet. 43:
165-169, 1988.
9. Yuasa, I.; Umetsu, K.; Suenaga, K.; Robinet-Levy, M.: Orosomucoid
(ORM) typing by isoelectric focusing: evidence for two structural
loci ORM1 and ORM2. Hum. Genet. 74: 160-161, 1986.
*FIELD* CD
Victor A. McKusick: 12/15/1986
*FIELD* ED
mark: 06/07/1996
pfoster: 2/18/1994
supermim: 3/16/1992
carol: 2/26/1991
carol: 2/8/1991
supermim: 3/20/1990
ddp: 10/27/1989
*RECORD*
*FIELD* NO
138610
*FIELD* TI
*138610 OROSOMUCOID 2; ORM2
;;GLYCOPROTEIN, ALPHA-1-ACID, OF SERUM, TYPE 2;;
ALPHA-1-ACID GLYCOPROTEIN, TYPE 2; AGP2
read more*FIELD* TX
Yuasa et al. (1986) performed orosomucoid phenotyping by isoelectric
focusing and immunoprinting. The band pattern of desialyzed ORM
indicated to these workers that the ORM system is controlled by 2
structural loci, ORM1 (138600) and ORM2. Whereas the ORM1 locus was
polymorphic, the ORM2 locus appeared to be monomorphic. Later, however,
Yuasa et al. (1987) demonstrated polymorphism of the ORM2 locus, with 6
alleles in the Japanese population. By studies of orosomucoid cDNA
clones isolated from mouse liver, Cooper and Papaconstantinou (1986)
showed that 2 species of ORM mRNA are transcribed from 2 distinct genes.
Escallon et al. (1987) presented evidence for the expression of a second
structural locus (ORM2) in human plasma as well as for the detection of
genetically determined variation at the ORM2 locus in American blacks by
the use of a sensitive enzyme-linked immunoblotting technique. After
thin-layer polyacrylamide isoelectric focusing (IEF) in gels containing
6 M urea, the isoprotein species coded by the second locus did not
segregate with the predominant alleles at the ORM1 locus. Variation in
ORM2 was not observed in U.S. whites or in several other populations
studied. Because of the low frequency and unlimited distribution of ORM2
variation, Escallon et al. (1987) were unable to test for linkage
between the 2 ORM loci.
By in situ hybridization using a cDNA clone for AGP2, Webb et al. (1988)
mapped both alpha-1-acid glycoprotein genes in the 9q34 band. Yuasa et
al. (1988) used a modified isoelectric focusing, in which glycerine was
omitted from gels, to differentiate ORM1 and ORM2 variants. They
demonstrated linkage disequilibrium between alleles at the 2 loci, thus
corroborating the close linkage demonstrated physically by Dente et al.
(1987). Merritt and Board (1988) presented the complete nucleotide
sequence of the ORM2 gene, which is located approximately 3.3 kb
downstream from ORM1. The derived amino acid sequence indicated at least
21 amino acid differences between the products of the 2 genes.
Data on gene frequencies of allelic variants were tabulated by
Roychoudhury and Nei (1988).
*FIELD* RF
1. Cooper, R.; Papaconstantinou, J.: Evidence of multiple alpha-1
acid glycoprotein genes in the mouse. J. Biol. Chem. 261: 1849-1853,
1986.
2. Dente, L.; Pizza, M. G.; Metspalu, A.; Cortese, R.: Structure
and expression of the genes coding for human alpha-1-acid glycoprotein.
EMBO J. 6: 2289-2296, 1987.
3. Escallon, M. H.; Ferrell, R. E.; Kamboh, M. I.: Genetic studies
of low-abundance human plasma proteins. V. Evidence for a second orosomucoid
structural locus (ORM2) expressed in plasma. Am. J. Hum. Genet. 41:
418-427, 1987.
4. Merritt, C. M.; Board, P. G.: Structure and characterisation of
a duplicated human alpha-1 acid glycoprotein gene. Gene 66: 97-106,
1988.
5. Roychoudhury, A. K.; Nei, M.: Human Polymorphic Genes: World Distribution.
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7. Yuasa, I.; Suenaga, K.; Umetsu, K.; Ito, K.; Robinet-Levy, M.:
Orosomucoid (ORM) typing by isoelectric focusing: evidence for gene
duplication of ORM1 and genetic polymorphism of ORM2. Hum. Genet. 77:
255-258, 1987.
8. Yuasa, I.; Umetsu, K.; Suenaga, K.: Orosomucoid (ORM) typing by
isoelectric focusing: evidence for an additional duplicated ORM1 locus
haplotype and close linkage of two ORM loci. Am. J. Hum. Genet. 43:
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*FIELD* CD
Victor A. McKusick: 12/15/1986
*FIELD* ED
mark: 06/07/1996
pfoster: 2/18/1994
supermim: 3/16/1992
carol: 2/26/1991
carol: 2/8/1991
supermim: 3/20/1990
ddp: 10/27/1989