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 27-MAR-2024, entry version 226. 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 163. DR CORUM; P25311; -. DR IntAct; P25311; 38. 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-GlcNAc glycan (1 site). DR GlyCosmos; P25311; 4 sites, 122 glycans. DR GlyGen; P25311; 6 sites, 122 N-linked glycans (4 sites), 1 O-linked glycan (1 site). DR iPTMnet; P25311; -. DR PhosphoSitePlus; P25311; -. DR BioMuta; AZGP1; -. DR DMDM; 292495049; -. DR REPRODUCTION-2DPAGE; IPI00166729; -. DR CPTAC; non-CPTAC-1167; -. DR CPTAC; non-CPTAC-2709; -. DR EPD; P25311; -. DR jPOST; P25311; -. DR MassIVE; P25311; -. DR MaxQB; P25311; -. DR PaxDb; 9606-ENSP00000292401; -. DR PeptideAtlas; P25311; -. DR PRIDE; P25311; -. DR ProteomicsDB; 54267; -. DR Antibodypedia; 848; 393 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 AGR; HGNC:910; -. 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; ENSGT01100000263517; -. DR HOGENOM; CLU_047501_0_1_1; -. DR InParanoid; P25311; -. DR OMA; APYSCYV; -. DR OrthoDB; 3840485at2759; -. 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 1148 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 180 other cell types or tissues. DR ExpressionAtlas; P25311; baseline and differential. 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:RNA nuclease activity; NAS:UniProtKB. 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:0006955; P:immune response; IBA:GO_Central. DR GO; GO:0008285; P:negative regulation of cell population proliferation; NAS:UniProtKB. DR CDD; cd21010; IgC1_MHC-like_ZAG; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 1. DR Gene3D; 3.30.500.10; MHC class I-like antigen recognition-like; 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 PANTHER; PTHR16675; MHC CLASS I-RELATED; 1. DR PANTHER; PTHR16675:SF276; ZINC-ALPHA-2-GLYCOPROTEIN; 1. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR PRINTS; PR01638; MHCCLASSI. DR SMART; SM00407; IGc1; 1. DR SUPFAM; SSF48726; Immunoglobulin; 1. DR SUPFAM; SSF54452; MHC antigen-recognition domain; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. DR SWISS-2DPAGE; P25311; -. DR Genevisible; P25311; HS. 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 //