ZA2G_HUMAN
ID ZA2G_HUMAN Reviewed; 298 AA.
AC P25311; D6W5T8; O60386; Q5XKQ4; Q8N4N0;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 2.
DT 03-AUG-2022, entry version 217.
DE RecName: Full=Zinc-alpha-2-glycoprotein;
DE Short=Zn-alpha-2-GP;
DE Short=Zn-alpha-2-glycoprotein;
DE Flags: Precursor;
GN Name=AZGP1; Synonyms=ZAG, ZNGP1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Mammary gland;
RX PubMed=1915885; DOI=10.1016/0014-5793(91)81271-9;
RA Freije J.P., Fueyo A., Uria J., Lopez-Otin C.;
RT "Human Zn-alpha 2-glycoprotein cDNA cloning and expression analysis in
RT benign and malignant breast tissues.";
RL FEBS Lett. 290:247-249(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8241150; DOI=10.1021/bi00211a004;
RA Ueyama H., Deng H.X., Ohkubo I.;
RT "Molecular cloning and chromosomal assignment of the gene for human Zn-
RT alpha 2-glycoprotein.";
RL Biochemistry 32:12968-12976(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Leukocyte;
RX PubMed=8307568; DOI=10.1016/s0888-7543(05)80359-3;
RA Freije J.P., Fueyo A., Uria J.A., Velasco G., Sanchez L.M.,
RA Lopez-Boado Y.S., Lopez-Otin C.;
RT "Human Zn-alpha 2-glycoprotein: complete genomic sequence, identification
RT of a related pseudogene and relationship to class I major
RT histocompatibility complex genes.";
RL Genomics 18:575-587(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon, and Prostate;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2-298.
RC TISSUE=Liver, and Prostate;
RX PubMed=2049092; DOI=10.1016/0006-291x(91)91844-3;
RA Ueyama H., Niwa M., Tada T., Sasaki M., Ohkubo I.;
RT "Cloning and nucleotide sequence of a human Zn-alpha 2-glycoprotein cDNA
RT and chromosomal assignment of its gene.";
RL Biochem. Biophys. Res. Commun. 177:696-703(1991).
RN [9]
RP PROTEIN SEQUENCE OF 21-298, AND PYROGLUTAMATE FORMATION AT GLN-21.
RC TISSUE=Plasma;
RX PubMed=3422450; DOI=10.1073/pnas.85.3.679;
RA Araki T., Gejyo F., Takagaki K., Haupt H., Schwick H.G., Buergi W.,
RA Marti T., Schaller J., Rickli E., Brossmer R., Atkinson P.H., Putnam F.W.,
RA Schmid K.;
RT "Complete amino acid sequence of human plasma Zn-alpha 2-glycoprotein and
RT its homology to histocompatibility antigens.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:679-683(1988).
RN [10]
RP PROTEIN SEQUENCE OF 21-35.
RX PubMed=15340161; DOI=10.1110/ps.04682504;
RA Zhang Z., Henzel W.J.;
RT "Signal peptide prediction based on analysis of experimentally verified
RT cleavage sites.";
RL Protein Sci. 13:2819-2824(2004).
RN [11]
RP CHARACTERIZATION, AND CRYSTALLIZATION.
RX PubMed=9114041; DOI=10.1073/pnas.94.9.4626;
RA Sanchez L.M., Lopez-Otin C., Bjorkman P.J.;
RT "Biochemical characterization and crystallization of human Zn-alpha2-
RT glycoprotein, a soluble class I major histocompatibility complex homolog.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:4626-4630(1997).
RN [12]
RP IN VITRO BINDING OF FATTY ACID.
RX PubMed=11425849; DOI=10.1074/jbc.c100301200;
RA Kennedy M.W., Heikema A.P., Cooper A., Bjorkman P.J., Sanchez L.M.;
RT "Hydrophobic ligand binding by Zn-alpha 2-glycoprotein, a soluble fat-
RT depleting factor related to major histocompatibility complex proteins.";
RL J. Biol. Chem. 276:35008-35013(2001).
RN [13]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-128.
RC TISSUE=Bile;
RX PubMed=15084671; DOI=10.1074/mcp.m400015-mcp200;
RA Kristiansen T.Z., Bunkenborg J., Gronborg M., Molina H., Thuluvath P.J.,
RA 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 [14]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-112 AND ASN-128.
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 [15]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-112.
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., Moore R.J.,
RA 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 [16]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-109; ASN-112 AND ASN-128.
RC TISSUE=Saliva;
RX PubMed=16740002; DOI=10.1021/pr050492k;
RA Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T., Loo J.A.;
RT "Identification of N-linked glycoproteins in human saliva by glycoprotein
RT capture and mass spectrometry.";
RL J. Proteome Res. 5:1493-1503(2006).
RN [17]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-109; ASN-112 AND ASN-128.
RC TISSUE=Milk;
RX PubMed=18780401; DOI=10.1002/pmic.200701057;
RA Picariello G., Ferranti P., Mamone G., Roepstorff P., Addeo F.;
RT "Identification of N-linked glycoproteins in human milk by hydrophilic
RT interaction liquid chromatography and mass spectrometry.";
RL Proteomics 8:3833-3847(2008).
RN [18]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-109; ASN-112 AND ASN-128.
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 multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [19]
RP GLYCOSYLATION AT ASN-109 AND ASN-128.
RX PubMed=19139490; DOI=10.1074/mcp.m800504-mcp200;
RA Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., Zheng Z.B.,
RA Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L.,
RA Ying W.T., He S.M., Qian X.H.;
RT "A strategy for precise and large scale identification of core fucosylated
RT glycoproteins.";
RL Mol. Cell. Proteomics 8:913-923(2009).
RN [20]
RP GLYCOSYLATION AT ASN-128, STRUCTURE OF CARBOHYDRATES, AND IDENTIFICATION BY
RP MASS 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 N- and
RT O-linked glycosylations by CID and ECD.";
RL Mol. Cell. Proteomics 11:1-17(2012).
RN [21]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), DISULFIDE BONDS, AND GLYCOSYLATION
RP AT ASN-109; ASN-128 AND ASN-259.
RX PubMed=10206894; DOI=10.1126/science.283.5409.1914;
RA Sanchez L.M., Chirino A.J., Bjorkman P.J.;
RT "Crystal structure of human ZAG, a fat-depleting factor related to MHC
RT molecules.";
RL Science 283:1914-1919(1999).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 21-298, DISULFIDE BONDS, AND
RP GLYCOSYLATION AT ASN-128 AND ASN-259.
RX PubMed=15477100; DOI=10.1016/j.jsb.2004.04.009;
RA Delker S.L., West A.P. Jr., McDermott L., Kennedy M.W., Bjorkman P.J.;
RT "Crystallographic studies of ligand binding by Zn-alpha2-glycoprotein.";
RL J. Struct. Biol. 148:205-213(2004).
RN [24]
RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 32-149 IN COMPLEX WITH PIP,
RP DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-259.
RX PubMed=18930737; DOI=10.1016/j.jmb.2008.09.072;
RA Hassan M.I., Bilgrami S., Kumar V., Singh N., Yadav S., Kaur P.,
RA Singh T.P.;
RT "Crystal structure of the novel complex formed between zinc alpha2-
RT glycoprotein (ZAG) and prolactin-inducible protein (PIP) from human seminal
RT plasma.";
RL J. Mol. Biol. 384:663-672(2008).
CC -!- FUNCTION: Stimulates lipid degradation in adipocytes and causes the
CC extensive fat losses associated with some advanced cancers. May bind
CC polyunsaturated fatty acids.
CC -!- SUBUNIT: Interacts with PIP. {ECO:0000269|PubMed:18930737}.
CC -!- INTERACTION:
CC P25311; P04156: PRNP; NbExp=4; IntAct=EBI-2513837, EBI-977302;
CC P25311; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-2513837, EBI-947187;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Blood plasma, seminal plasma, urine, saliva, sweat,
CC epithelial cells of various human glands, liver.
CC -!- PTM: N-glycosylated. N-glycan at Asn-128: Hex5HexNAc4.
CC {ECO:0000269|PubMed:10206894, ECO:0000269|PubMed:14760718,
CC ECO:0000269|PubMed:15084671, ECO:0000269|PubMed:15477100,
CC ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:16740002,
CC ECO:0000269|PubMed:18780401, ECO:0000269|PubMed:18930737,
CC ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218,
CC ECO:0000269|PubMed:22171320}.
CC -!- SIMILARITY: Belongs to the MHC class I family. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-4 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA61311.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA03123.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA14417.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA42438.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X59766; CAA42438.1; ALT_INIT; mRNA.
DR EMBL; D14034; BAA03123.1; ALT_INIT; Genomic_DNA.
DR EMBL; X69953; CAA49574.1; -; Genomic_DNA.
DR EMBL; AC004522; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH236956; EAL23862.1; -; Genomic_DNA.
DR EMBL; CH471091; EAW76621.1; -; Genomic_DNA.
DR EMBL; CH471091; EAW76622.1; -; Genomic_DNA.
DR EMBL; BC005306; AAH05306.1; -; mRNA.
DR EMBL; BC033830; AAH33830.1; -; mRNA.
DR EMBL; D90427; BAA14417.1; ALT_INIT; mRNA.
DR EMBL; M76707; AAA61311.1; ALT_INIT; mRNA.
DR CCDS; CCDS5680.1; -.
DR PIR; A54175; A54175.
DR RefSeq; NP_001176.1; NM_001185.3.
DR PDB; 1T7V; X-ray; 1.95 A; A=21-298.
DR PDB; 1T7W; X-ray; 2.70 A; A=21-298.
DR PDB; 1T7X; X-ray; 3.10 A; A=21-298.
DR PDB; 1T7Y; X-ray; 2.80 A; A=21-298.
DR PDB; 1T7Z; X-ray; 3.00 A; A=21-298.
DR PDB; 1T80; X-ray; 2.10 A; A=21-298.
DR PDB; 1ZAG; X-ray; 2.80 A; A/B/C/D=25-298.
DR PDB; 3ES6; X-ray; 3.23 A; A=21-298.
DR PDB; 6R2U; X-ray; 2.49 A; A/B/C/D/E/F=21-298.
DR PDBsum; 1T7V; -.
DR PDBsum; 1T7W; -.
DR PDBsum; 1T7X; -.
DR PDBsum; 1T7Y; -.
DR PDBsum; 1T7Z; -.
DR PDBsum; 1T80; -.
DR PDBsum; 1ZAG; -.
DR PDBsum; 3ES6; -.
DR PDBsum; 6R2U; -.
DR AlphaFoldDB; P25311; -.
DR SMR; P25311; -.
DR BioGRID; 107040; 144.
DR CORUM; P25311; -.
DR IntAct; P25311; 36.
DR MINT; P25311; -.
DR STRING; 9606.ENSP00000292401; -.
DR DrugBank; DB09130; Copper.
DR DrugBank; DB03721; N-acetyl-alpha-neuraminic acid.
DR CarbonylDB; P25311; -.
DR GlyConnect; 692; 108 N-Linked glycans (3 sites), 1 O-Linked glycan (1 site).
DR GlyGen; P25311; 5 sites, 118 N-linked glycans (4 sites).
DR iPTMnet; P25311; -.
DR PhosphoSitePlus; P25311; -.
DR BioMuta; AZGP1; -.
DR DMDM; 292495049; -.
DR REPRODUCTION-2DPAGE; IPI00166729; -.
DR SWISS-2DPAGE; P25311; -.
DR CPTAC; non-CPTAC-1167; -.
DR CPTAC; non-CPTAC-2709; -.
DR EPD; P25311; -.
DR jPOST; P25311; -.
DR MassIVE; P25311; -.
DR MaxQB; P25311; -.
DR PaxDb; P25311; -.
DR PeptideAtlas; P25311; -.
DR PRIDE; P25311; -.
DR ProteomicsDB; 54267; -.
DR Antibodypedia; 848; 369 antibodies from 33 providers.
DR DNASU; 563; -.
DR Ensembl; ENST00000292401.9; ENSP00000292401.4; ENSG00000160862.13.
DR GeneID; 563; -.
DR KEGG; hsa:563; -.
DR MANE-Select; ENST00000292401.9; ENSP00000292401.4; NM_001185.4; NP_001176.1.
DR UCSC; uc003ush.4; human.
DR CTD; 563; -.
DR DisGeNET; 563; -.
DR GeneCards; AZGP1; -.
DR HGNC; HGNC:910; AZGP1.
DR HPA; ENSG00000160862; Tissue enhanced (liver, salivary gland).
DR MIM; 194460; gene.
DR neXtProt; NX_P25311; -.
DR OpenTargets; ENSG00000160862; -.
DR PharmGKB; PA25203; -.
DR VEuPathDB; HostDB:ENSG00000160862; -.
DR eggNOG; ENOG502RWW3; Eukaryota.
DR GeneTree; ENSGT01040000240396; -.
DR HOGENOM; CLU_047501_0_1_1; -.
DR InParanoid; P25311; -.
DR OMA; YQSWVVV; -.
DR OrthoDB; 912212at2759; -.
DR PhylomeDB; P25311; -.
DR TreeFam; TF336617; -.
DR PathwayCommons; P25311; -.
DR Reactome; R-HSA-5223345; Miscellaneous transport and binding events.
DR SignaLink; P25311; -.
DR BioGRID-ORCS; 563; 35 hits in 1070 CRISPR screens.
DR ChiTaRS; AZGP1; human.
DR EvolutionaryTrace; P25311; -.
DR GeneWiki; AZGP1; -.
DR GenomeRNAi; 563; -.
DR Pharos; P25311; Tbio.
DR PRO; PR:P25311; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; P25311; protein.
DR Bgee; ENSG00000160862; Expressed in parotid gland and 178 other tissues.
DR ExpressionAtlas; P25311; baseline and differential.
DR Genevisible; P25311; HS.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; HDA:BHF-UCL.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0008320; F:protein transmembrane transporter activity; NAS:UniProtKB.
DR GO; GO:0004540; F:ribonuclease activity; NAS:UniProtKB.
DR GO; GO:0002476; P:antigen processing and presentation of endogenous peptide antigen via MHC class Ib; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; IDA:UniProtKB.
DR GO; GO:0001580; P:detection of chemical stimulus involved in sensory perception of bitter taste; IDA:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; NAS:UniProtKB.
DR GO; GO:0001895; P:retina homeostasis; HEP:UniProtKB.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.30.500.10; -; 1.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003006; Ig/MHC_CS.
DR InterPro; IPR003597; Ig_C1-set.
DR InterPro; IPR011161; MHC_I-like_Ag-recog.
DR InterPro; IPR037055; MHC_I-like_Ag-recog_sf.
DR InterPro; IPR011162; MHC_I/II-like_Ag-recog.
DR InterPro; IPR001039; MHC_I_a_a1/a2.
DR Pfam; PF07654; C1-set; 1.
DR Pfam; PF00129; MHC_I; 1.
DR PRINTS; PR01638; MHCCLASSI.
DR SMART; SM00407; IGc1; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR SUPFAM; SSF54452; SSF54452; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS00290; IG_MHC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Pyrrolidone carboxylic acid; Reference proteome; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000269|PubMed:15340161,
FT ECO:0000269|PubMed:3422450"
FT CHAIN 21..298
FT /note="Zinc-alpha-2-glycoprotein"
FT /id="PRO_0000019012"
FT DOMAIN 207..292
FT /note="Ig-like C1-type"
FT MOD_RES 21
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:3422450"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:10206894,
FT ECO:0000269|PubMed:16740002, ECO:0000269|PubMed:18780401,
FT ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218"
FT CARBOHYD 112
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:14760718,
FT ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:16740002,
FT ECO:0000269|PubMed:18780401, ECO:0000269|PubMed:19159218"
FT CARBOHYD 128
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:10206894,
FT ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:15084671,
FT ECO:0000269|PubMed:15477100, ECO:0000269|PubMed:16740002,
FT ECO:0000269|PubMed:18780401, ECO:0000269|PubMed:19139490,
FT ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:22171320"
FT CARBOHYD 259
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:10206894,
FT ECO:0000269|PubMed:15477100, ECO:0000269|PubMed:18930737"
FT DISULFID 123..186
FT DISULFID 225..280
FT CONFLICT 2
FT /note="V -> S (in Ref. 1; CAA42438)"
FT /evidence="ECO:0000305"
FT CONFLICT 5
FT /note="V -> L (in Ref. 1; CAA42438)"
FT /evidence="ECO:0000305"
FT CONFLICT 33
FT /note="I -> V (in Ref. 7; AAH05306)"
FT /evidence="ECO:0000305"
FT CONFLICT 85
FT /note="Q -> E (in Ref. 9; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 96..97
FT /note="Missing (in Ref. 9; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 244
FT /note="E -> Q (in Ref. 9; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 27..39
FT /evidence="ECO:0007829|PDB:1T7V"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:1ZAG"
FT STRAND 46..53
FT /evidence="ECO:0007829|PDB:1T7V"
FT STRAND 56..62
FT /evidence="ECO:0007829|PDB:1T7V"
FT TURN 63..65
FT /evidence="ECO:0007829|PDB:1T7V"
FT HELIX 72..76
FT /evidence="ECO:0007829|PDB:1T7V"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:3ES6"
FT HELIX 83..107
FT /evidence="ECO:0007829|PDB:1T7V"
FT STRAND 116..126
FT /evidence="ECO:0007829|PDB:1T7V"
FT STRAND 129..139
FT /evidence="ECO:0007829|PDB:1T7V"
FT STRAND 142..148
FT /evidence="ECO:0007829|PDB:1T7V"
FT TURN 149..152
FT /evidence="ECO:0007829|PDB:1T7V"
FT STRAND 153..156
FT /evidence="ECO:0007829|PDB:1T7V"
FT HELIX 159..168
FT /evidence="ECO:0007829|PDB:1T7V"
FT HELIX 173..183
FT /evidence="ECO:0007829|PDB:1T7V"
FT HELIX 185..196
FT /evidence="ECO:0007829|PDB:1T7V"
FT HELIX 198..201
FT /evidence="ECO:0007829|PDB:1T7V"
FT STRAND 208..215
FT /evidence="ECO:0007829|PDB:1T7V"
FT STRAND 217..219
FT /evidence="ECO:0007829|PDB:1T7X"
FT STRAND 221..233
FT /evidence="ECO:0007829|PDB:1T7V"
FT STRAND 235..241
FT /evidence="ECO:0007829|PDB:1T7V"
FT STRAND 244..246
FT /evidence="ECO:0007829|PDB:1ZAG"
FT STRAND 249..256
FT /evidence="ECO:0007829|PDB:1T7V"
FT TURN 257..260
FT /evidence="ECO:0007829|PDB:1T7V"
FT STRAND 261..270
FT /evidence="ECO:0007829|PDB:1T7V"
FT STRAND 278..284
FT /evidence="ECO:0007829|PDB:1T7V"
FT STRAND 287..289
FT /evidence="ECO:0007829|PDB:6R2U"
FT STRAND 291..294
FT /evidence="ECO:0007829|PDB:1T7V"
SQ SEQUENCE 298 AA; 34259 MW; 006A153A8E32A0B1 CRC64;
MVRMVPVLLS LLLLLGPAVP QENQDGRYSL TYIYTGLSKH VEDVPAFQAL GSLNDLQFFR
YNSKDRKSQP MGLWRQVEGM EDWKQDSQLQ KAREDIFMET LKDIVEYYND SNGSHVLQGR
FGCEIENNRS SGAFWKYYYD GKDYIEFNKE IPAWVPFDPA AQITKQKWEA EPVYVQRAKA
YLEEECPATL RKYLKYSKNI LDRQDPPSVV VTSHQAPGEK KKLKCLAYDF YPGKIDVHWT
RAGEVQEPEL RGDVLHNGNG TYQSWVVVAV PPQDTAPYSC HVQHSSLAQP LVVPWEAS
