Full text data of AZGP1
AZGP1
(ZAG, ZNGP1)
[Confidence: low (only semi-automatic identification from reviews)]
Zinc-alpha-2-glycoprotein; Zn-alpha-2-GP; Zn-alpha-2-glycoprotein; Flags: Precursor
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Zinc-alpha-2-glycoprotein; Zn-alpha-2-GP; Zn-alpha-2-glycoprotein; Flags: Precursor
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P25311
ID ZA2G_HUMAN Reviewed; 298 AA.
AC P25311; D6W5T8; O60386; Q5XKQ4; Q8N4N0;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-MAR-2010, sequence version 2.
DT 22-JAN-2014, entry version 146.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT Zn-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,
RT identification of a related pseudogene and relationship to class I
RT major 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.,
RA Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
RA Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
RA Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
RA Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
RA Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
RA Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
RA Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
RA Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
RA Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
RA Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
RA Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
RA 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.,
RA Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
RA Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
RA Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
RA Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
RA Waterston R.H., 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.,
RA Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z.,
RA Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C.,
RA Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J.,
RA Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F.,
RA Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F.,
RA Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H.,
RA Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G.,
RA Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P.,
RA Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J.,
RA Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F.,
RA Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B.,
RA 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.,
RA Mural R.J., 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.,
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 (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
RT project: 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
RT cDNA and chromosomal assignment of its gene.";
RL Biochem. Biophys. Res. Commun. 177:696-703(1991).
RN [9]
RP PROTEIN SEQUENCE OF 21-298.
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.,
RA Putnam F.W., Schmid K.;
RT "Complete amino acid sequence of human plasma Zn-alpha 2-glycoprotein
RT and 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
RT verified 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
RT 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
RT proteins.";
RL J. Biol. Chem. 276:35008-35013(2001).
RN [13]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-128, AND MASS
RP 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 [14]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-112 AND ASN-128, AND MASS
RP 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 [15]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-112, AND MASS
RP 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 [16]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-109; ASN-112 AND ASN-128,
RP AND MASS SPECTROMETRY.
RC TISSUE=Saliva;
RX PubMed=16740002; DOI=10.1021/pr050492k;
RA Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T.,
RA Loo J.A.;
RT "Identification of N-linked glycoproteins in human saliva by
RT glycoprotein 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,
RP AND MASS SPECTROMETRY.
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,
RP 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 [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.,
RA Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y.,
RA Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.;
RT "A strategy for precise and large scale identification of core
RT fucosylated glycoproteins.";
RL Mol. Cell. Proteomics 8:913-923(2009).
RN [20]
RP GLYCOSYLATION AT ASN-128, 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 [21]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), DISULFIDE BONDS, AND
RP GLYCOSYLATION 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 [22]
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-
RT glycoprotein.";
RL J. Struct. Biol. 148:205-213(2004).
RN [23]
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
RT seminal plasma.";
RL J. Mol. Biol. 384:663-672(2008).
CC -!- FUNCTION: Stimulates lipid degradation in adipocytes and causes
CC the extensive fat losses associated with some advanced cancers.
CC May bind polyunsaturated fatty acids.
CC -!- SUBUNIT: Interacts with PIP.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Blood plasma, seminal plasma, urine, saliva,
CC sweat, epithelial cells of various human glands, liver.
CC -!- PTM: N-glycosylated. N-glycan at Asn-128: Hex5HexNAc4.
CC -!- SIMILARITY: Belongs to the MHC class I family.
CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like)
CC domain.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-4 is the initiator.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA61311.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC Sequence=BAA03123.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=BAA14417.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=CAA42438.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
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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 PIR; A54175; A54175.
DR RefSeq; NP_001176.1; NM_001185.3.
DR UniGene; Hs.546239; -.
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=22-298.
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 ProteinModelPortal; P25311; -.
DR SMR; P25311; 25-298.
DR IntAct; P25311; 6.
DR STRING; 9606.ENSP00000292401; -.
DR PhosphoSite; P25311; -.
DR DMDM; 292495049; -.
DR REPRODUCTION-2DPAGE; IPI00166729; -.
DR SWISS-2DPAGE; P25311; -.
DR PaxDb; P25311; -.
DR PRIDE; P25311; -.
DR Ensembl; ENST00000292401; ENSP00000292401; ENSG00000160862.
DR GeneID; 563; -.
DR KEGG; hsa:563; -.
DR UCSC; uc003ush.3; human.
DR CTD; 563; -.
DR GeneCards; GC07M099564; -.
DR HGNC; HGNC:910; AZGP1.
DR HPA; CAB016087; -.
DR HPA; HPA012582; -.
DR MIM; 194460; gene.
DR neXtProt; NX_P25311; -.
DR PharmGKB; PA25203; -.
DR eggNOG; NOG25830; -.
DR HOGENOM; HOG000296917; -.
DR HOVERGEN; HBG016709; -.
DR InParanoid; P25311; -.
DR OMA; NILDRQD; -.
DR OrthoDB; EOG7JT6WQ; -.
DR PhylomeDB; P25311; -.
DR ChiTaRS; AZGP1; human.
DR EvolutionaryTrace; P25311; -.
DR GeneWiki; AZGP1; -.
DR GenomeRNAi; 563; -.
DR NextBio; 2301; -.
DR PRO; PR:P25311; -.
DR ArrayExpress; P25311; -.
DR Bgee; P25311; -.
DR CleanEx; HS_AZGP1; -.
DR Genevestigator; P25311; -.
DR GO; GO:0005615; C:extracellular space; IBA:RefGenome.
DR GO; GO:0042612; C:MHC class I protein complex; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IBA:RefGenome.
DR GO; GO:0003823; F:antigen binding; IBA:RefGenome.
DR GO; GO:0042605; F:peptide antigen binding; IEA:InterPro.
DR GO; GO:0008320; F:protein transmembrane transporter activity; NAS:UniProtKB.
DR GO; GO:0004540; F:ribonuclease activity; NAS:UniProtKB.
DR GO; GO:0019882; P:antigen processing and presentation; IBA:RefGenome.
DR GO; GO:0002474; P:antigen processing and presentation of peptide antigen via MHC class I; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; IDA:UniProtKB.
DR GO; GO:0006955; P:immune response; IEA:InterPro.
DR GO; GO:0008285; P:negative regulation of cell proliferation; NAS:UniProtKB.
DR GO; GO:0001916; P:positive regulation of T cell mediated cytotoxicity; IEA:InterPro.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.30.500.10; -; 1.
DR InterPro; IPR007110; Ig-like_dom.
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; IPR011162; MHC_I/II-like_Ag-recog.
DR InterPro; IPR027648; MHC_I_a.
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; SSF54452; SSF54452; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS00290; IG_MHC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Complete proteome; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Pyrrolidone carboxylic acid;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1 20
FT CHAIN 21 298 Zinc-alpha-2-glycoprotein.
FT /FTId=PRO_0000019012.
FT DOMAIN 207 292 Ig-like C1-type.
FT MOD_RES 21 21 Pyrrolidone carboxylic acid.
FT CARBOHYD 109 109 N-linked (GlcNAc...) (complex).
FT CARBOHYD 112 112 N-linked (GlcNAc...).
FT CARBOHYD 128 128 N-linked (GlcNAc...) (complex).
FT CARBOHYD 259 259 N-linked (GlcNAc...).
FT DISULFID 123 186
FT DISULFID 225 280
FT CONFLICT 2 2 V -> S (in Ref. 1; CAA42438).
FT CONFLICT 5 5 V -> L (in Ref. 1; CAA42438).
FT CONFLICT 33 33 I -> V (in Ref. 7; AAH05306).
FT CONFLICT 85 85 Q -> E (in Ref. 9; AA sequence).
FT CONFLICT 96 97 Missing (in Ref. 9; AA sequence).
FT CONFLICT 244 244 E -> Q (in Ref. 9; AA sequence).
FT STRAND 27 39
FT STRAND 42 44
FT STRAND 46 53
FT STRAND 56 62
FT TURN 63 65
FT HELIX 72 76
FT STRAND 79 81
FT HELIX 83 107
FT STRAND 116 126
FT STRAND 129 139
FT STRAND 142 148
FT TURN 149 152
FT STRAND 153 156
FT HELIX 159 168
FT HELIX 173 183
FT HELIX 185 196
FT HELIX 198 201
FT STRAND 208 215
FT STRAND 217 219
FT STRAND 221 233
FT STRAND 235 241
FT STRAND 244 246
FT STRAND 249 256
FT TURN 257 260
FT STRAND 261 270
FT STRAND 278 284
FT STRAND 291 294
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
//
ID ZA2G_HUMAN Reviewed; 298 AA.
AC P25311; D6W5T8; O60386; Q5XKQ4; Q8N4N0;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-MAR-2010, sequence version 2.
DT 22-JAN-2014, entry version 146.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT Zn-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,
RT identification of a related pseudogene and relationship to class I
RT major 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.,
RA Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
RA Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
RA Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
RA Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
RA Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
RA Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
RA Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
RA Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
RA Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
RA Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
RA Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
RA 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.,
RA Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
RA Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
RA Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
RA Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
RA Waterston R.H., 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.,
RA Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z.,
RA Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C.,
RA Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J.,
RA Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F.,
RA Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F.,
RA Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H.,
RA Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G.,
RA Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P.,
RA Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J.,
RA Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F.,
RA Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B.,
RA 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.,
RA Mural R.J., 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.,
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 (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
RT project: 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
RT cDNA and chromosomal assignment of its gene.";
RL Biochem. Biophys. Res. Commun. 177:696-703(1991).
RN [9]
RP PROTEIN SEQUENCE OF 21-298.
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.,
RA Putnam F.W., Schmid K.;
RT "Complete amino acid sequence of human plasma Zn-alpha 2-glycoprotein
RT and 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
RT verified 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
RT 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
RT proteins.";
RL J. Biol. Chem. 276:35008-35013(2001).
RN [13]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-128, AND MASS
RP 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 [14]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-112 AND ASN-128, AND MASS
RP 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 [15]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-112, AND MASS
RP 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 [16]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-109; ASN-112 AND ASN-128,
RP AND MASS SPECTROMETRY.
RC TISSUE=Saliva;
RX PubMed=16740002; DOI=10.1021/pr050492k;
RA Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T.,
RA Loo J.A.;
RT "Identification of N-linked glycoproteins in human saliva by
RT glycoprotein 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,
RP AND MASS SPECTROMETRY.
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,
RP 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 [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.,
RA Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y.,
RA Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.;
RT "A strategy for precise and large scale identification of core
RT fucosylated glycoproteins.";
RL Mol. Cell. Proteomics 8:913-923(2009).
RN [20]
RP GLYCOSYLATION AT ASN-128, 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 [21]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), DISULFIDE BONDS, AND
RP GLYCOSYLATION 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 [22]
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-
RT glycoprotein.";
RL J. Struct. Biol. 148:205-213(2004).
RN [23]
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
RT seminal plasma.";
RL J. Mol. Biol. 384:663-672(2008).
CC -!- FUNCTION: Stimulates lipid degradation in adipocytes and causes
CC the extensive fat losses associated with some advanced cancers.
CC May bind polyunsaturated fatty acids.
CC -!- SUBUNIT: Interacts with PIP.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Blood plasma, seminal plasma, urine, saliva,
CC sweat, epithelial cells of various human glands, liver.
CC -!- PTM: N-glycosylated. N-glycan at Asn-128: Hex5HexNAc4.
CC -!- SIMILARITY: Belongs to the MHC class I family.
CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like)
CC domain.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-4 is the initiator.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA61311.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC Sequence=BAA03123.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=BAA14417.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=CAA42438.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
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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 PIR; A54175; A54175.
DR RefSeq; NP_001176.1; NM_001185.3.
DR UniGene; Hs.546239; -.
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=22-298.
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 ProteinModelPortal; P25311; -.
DR SMR; P25311; 25-298.
DR IntAct; P25311; 6.
DR STRING; 9606.ENSP00000292401; -.
DR PhosphoSite; P25311; -.
DR DMDM; 292495049; -.
DR REPRODUCTION-2DPAGE; IPI00166729; -.
DR SWISS-2DPAGE; P25311; -.
DR PaxDb; P25311; -.
DR PRIDE; P25311; -.
DR Ensembl; ENST00000292401; ENSP00000292401; ENSG00000160862.
DR GeneID; 563; -.
DR KEGG; hsa:563; -.
DR UCSC; uc003ush.3; human.
DR CTD; 563; -.
DR GeneCards; GC07M099564; -.
DR HGNC; HGNC:910; AZGP1.
DR HPA; CAB016087; -.
DR HPA; HPA012582; -.
DR MIM; 194460; gene.
DR neXtProt; NX_P25311; -.
DR PharmGKB; PA25203; -.
DR eggNOG; NOG25830; -.
DR HOGENOM; HOG000296917; -.
DR HOVERGEN; HBG016709; -.
DR InParanoid; P25311; -.
DR OMA; NILDRQD; -.
DR OrthoDB; EOG7JT6WQ; -.
DR PhylomeDB; P25311; -.
DR ChiTaRS; AZGP1; human.
DR EvolutionaryTrace; P25311; -.
DR GeneWiki; AZGP1; -.
DR GenomeRNAi; 563; -.
DR NextBio; 2301; -.
DR PRO; PR:P25311; -.
DR ArrayExpress; P25311; -.
DR Bgee; P25311; -.
DR CleanEx; HS_AZGP1; -.
DR Genevestigator; P25311; -.
DR GO; GO:0005615; C:extracellular space; IBA:RefGenome.
DR GO; GO:0042612; C:MHC class I protein complex; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IBA:RefGenome.
DR GO; GO:0003823; F:antigen binding; IBA:RefGenome.
DR GO; GO:0042605; F:peptide antigen binding; IEA:InterPro.
DR GO; GO:0008320; F:protein transmembrane transporter activity; NAS:UniProtKB.
DR GO; GO:0004540; F:ribonuclease activity; NAS:UniProtKB.
DR GO; GO:0019882; P:antigen processing and presentation; IBA:RefGenome.
DR GO; GO:0002474; P:antigen processing and presentation of peptide antigen via MHC class I; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; IDA:UniProtKB.
DR GO; GO:0006955; P:immune response; IEA:InterPro.
DR GO; GO:0008285; P:negative regulation of cell proliferation; NAS:UniProtKB.
DR GO; GO:0001916; P:positive regulation of T cell mediated cytotoxicity; IEA:InterPro.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.30.500.10; -; 1.
DR InterPro; IPR007110; Ig-like_dom.
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; IPR011162; MHC_I/II-like_Ag-recog.
DR InterPro; IPR027648; MHC_I_a.
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; SSF54452; SSF54452; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS00290; IG_MHC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Complete proteome; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Pyrrolidone carboxylic acid;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1 20
FT CHAIN 21 298 Zinc-alpha-2-glycoprotein.
FT /FTId=PRO_0000019012.
FT DOMAIN 207 292 Ig-like C1-type.
FT MOD_RES 21 21 Pyrrolidone carboxylic acid.
FT CARBOHYD 109 109 N-linked (GlcNAc...) (complex).
FT CARBOHYD 112 112 N-linked (GlcNAc...).
FT CARBOHYD 128 128 N-linked (GlcNAc...) (complex).
FT CARBOHYD 259 259 N-linked (GlcNAc...).
FT DISULFID 123 186
FT DISULFID 225 280
FT CONFLICT 2 2 V -> S (in Ref. 1; CAA42438).
FT CONFLICT 5 5 V -> L (in Ref. 1; CAA42438).
FT CONFLICT 33 33 I -> V (in Ref. 7; AAH05306).
FT CONFLICT 85 85 Q -> E (in Ref. 9; AA sequence).
FT CONFLICT 96 97 Missing (in Ref. 9; AA sequence).
FT CONFLICT 244 244 E -> Q (in Ref. 9; AA sequence).
FT STRAND 27 39
FT STRAND 42 44
FT STRAND 46 53
FT STRAND 56 62
FT TURN 63 65
FT HELIX 72 76
FT STRAND 79 81
FT HELIX 83 107
FT STRAND 116 126
FT STRAND 129 139
FT STRAND 142 148
FT TURN 149 152
FT STRAND 153 156
FT HELIX 159 168
FT HELIX 173 183
FT HELIX 185 196
FT HELIX 198 201
FT STRAND 208 215
FT STRAND 217 219
FT STRAND 221 233
FT STRAND 235 241
FT STRAND 244 246
FT STRAND 249 256
FT TURN 257 260
FT STRAND 261 270
FT STRAND 278 284
FT STRAND 291 294
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
//
MIM
194460
*RECORD*
*FIELD* NO
194460
*FIELD* TI
*194460 ALPHA-2-GLYCOPROTEIN, ZINC; AZGP1
;;ZINC-ALPHA-2-GLYCOPROTEIN; ZAG; ZA2G
*FIELD* TX
read more
CLONING
Burgi and Schmid (1961) first purified zinc-alpha-2-glycoprotein from
pooled human plasma and studied its physicochemical properties. The
glycoprotein was so named for its electrophoretic mobility in the
alpha-2 region and for its ability to bind zinc ions. The ZAG
glycoprotein has a molecular mass of 41 kD consisting of 18.2%
carbohydrate and a single polypeptide chain.
The complete amino acid sequence and the carbohydrate structure of ZAG
were determined by Araki et al. (1988), who calculated the molecular
mass to be 38,478 Da.
Ueyama et al. (1991) isolated a cDNA clone for human
zinc-alpha-2-glycoprotein. Southern blot analysis suggested the presence
of a single gene encoding the protein.
MAPPING
Using a panel of rodent-human somatic cell hybrids, Ueyama et al. (1991)
assigned the ZAG gene to human chromosome 7.
By fluorescence in situ hybridization, Ueyama et al. (1993) mapped the
functional gene, which they symbolized ZA2G, to 7q22.1. They concluded
that at least one of the pseudogenes is closely linked to the functional
chain.
Pendas et al. (1994) also used fluorescence in situ hybridization to map
the AZGP1 gene to 7q22.
GENE STRUCTURE
Freije et al. (1993) found that the AZGP1 gene spans over 9.7 kb and
that its overall organization and nucleotide sequence resemble those of
the first 4 exons of class I MHC genes (see 142800). However, it differs
from those genes by its lack of coding information for transmembrane and
cytoplasmic domains typical of MHC genes, which is consistent with its
presence as a soluble protein in various physiologic and pathologic
fluids. In addition, it contains a high density of repetitive sequences,
including Alu, MER, and MIR elements, which are not present at
equivalent positions in class I MHC genes. The human genome also
contains a putative AZGP1 pseudogene.
Ueyama et al. (1993) isolated the functional gene and found it to be 9.3
kb long and composed of 4 exons. The first exon codes for the 5-prime
untranslated region, the signal sequence, and the first 6 amino acids.
The second exon codes for domain A, the third for domain B, and the
fourth for domain C and the 3-prime untranslated region. Ueyama et al.
(1993) also isolated 2 pseudogenes retaining exon-intron organization.
GENE FUNCTION
Freije et al. (1991) studied the expression of this protein in benign
and malignant breast tissues.
Freije et al. (1993) suggested that in light of the lack of polymorphism
in the AZGP1 gene in comparison with MHC genes, this human glycoprotein
may have a role in the transport of nonpolymorphic substances or in
intercellular recognition processes.
MOLECULAR GENETICS
Nakayashiki and Katsura (1989) studied ZAG in plasma by polyacrylamide
gel isoelectric focusing followed by immunoblotting with specific
antiserum to ZAG in the Japanese population. Most of 1,224 plasma
samples showed a common, single-band pattern, whereas 16 samples showed
variant double-band patterns which were classified into 4 types. The
desialyzed form of ZAG commonly showed the single band. Differences in
ZAG phenotypes appeared to be due to amino acid substitutions of the ZAG
molecule. Nakayashiki and Katsura (1989) proposed the existence of 5
alleles, designated ZAG*1, ZAG*2, ZAG*3, ZAG*4 and ZAG*5, with
frequencies of 0.9935, 0.0025, 0.0016, 0.0004, and 0.0020, respectively.
The codominant transmission of the rare alleles ZAG*3 and ZAG*4 was
confirmed in family studies.
*FIELD* SA
Kamboh and Ferrell (1986)
*FIELD* RF
1. Araki, T.; Gejyo, F.; Takagaki, K.; Haupt, H.; Schwick, H. G.;
Burgi, W.; Marti, T.; Schaller, J.; Rickli, E.; Brossmer, R.; Atkinson,
P. H.; Putnam, F. W.; Schmid, K.: Complete amino acid sequence of
human plasma Zn-alpha(2)-glycoprotein and its homology to histocompatibility
antigens. Proc. Nat. Acad. Sci. 85: 679-683, 1988.
2. Burgi, W.; Schmid, K.: Preparation and properties of Zn-alpha(2)-glycoprotein
of normal human plasma. J. Biol. Chem. 236: 1066-1074, 1961.
3. Freije, J. P.; Fueyo, A.; Uria, J.; Lopez-Otin, C.: Human Zn-alpha-2-glycoprotein
cDNA cloning and expression analysis in benign and malignant breast
tissues. FEBS Lett. 290: 247-249, 1991.
4. Freije, J. P.; Fueyo, A.; Uria, J. A.; Velasco, G.; Sanchez, L.
M.; Lopez-Boado, Y. S.; Lopez-Otin, C.: Human Zn-alpha-2-glycoprotein:
complete genomic sequence, identification of a related pseudogene
and relationship to class I major histocompatibility complex genes. Genomics 18:
575-587, 1993.
5. Kamboh, M. I.; Ferrell, R. E.: Genetic studies of low-abundance
human plasma proteins. I. Microheterogeneity of zinc-alpha(2)-glycoprotein
in biological fluids. Biochem. Genet. 24: 849-857, 1986.
6. Nakayashiki, N.; Katsura, S.: Four variants of human plasma Zn-alpha(2)-glycoprotein
(ZAG) in the Japanese population. Hum. Genet. 82: 293-295, 1989.
7. Pendas, A. M.; Matilla, T.; Uria, J. A.; Freije, J. P.; Fueyo,
A.; Estivill, X.; Lopez-Otin, C.: Mapping of the human Zn-alpha-2-glycoprotein
gene (AZGP1) to chromosome 7q22 by in situ hybridization. Cytogenet.
Cell Genet. 66: 263-266, 1994.
8. Ueyama, H.; Han-Xiang, D.; Ohkubo, I.: Molecular cloning and chromosomal
assignment of the gene for human Zn-alpha-2-glycoprotein. Biochemistry 32:
12968-12976, 1993.
9. Ueyama, H.; Niwa, M.; Tada, T.; Sasaki, M.; Ohkubo, I.: Cloning
and nucleotide sequence of a human Zn-alpha(2)-glycoprotein cDNA and
chromosomal assignment of its gene. Biochem. Biophys. Res. Commun. 177:
696-703, 1991.
*FIELD* CD
Victor A. McKusick: 8/7/1989
*FIELD* ED
carol: 05/29/2009
carol: 5/8/2003
jason: 6/28/1994
carol: 2/16/1994
carol: 4/16/1993
supermim: 3/16/1992
carol: 11/27/1991
carol: 9/4/1991
*RECORD*
*FIELD* NO
194460
*FIELD* TI
*194460 ALPHA-2-GLYCOPROTEIN, ZINC; AZGP1
;;ZINC-ALPHA-2-GLYCOPROTEIN; ZAG; ZA2G
*FIELD* TX
read more
CLONING
Burgi and Schmid (1961) first purified zinc-alpha-2-glycoprotein from
pooled human plasma and studied its physicochemical properties. The
glycoprotein was so named for its electrophoretic mobility in the
alpha-2 region and for its ability to bind zinc ions. The ZAG
glycoprotein has a molecular mass of 41 kD consisting of 18.2%
carbohydrate and a single polypeptide chain.
The complete amino acid sequence and the carbohydrate structure of ZAG
were determined by Araki et al. (1988), who calculated the molecular
mass to be 38,478 Da.
Ueyama et al. (1991) isolated a cDNA clone for human
zinc-alpha-2-glycoprotein. Southern blot analysis suggested the presence
of a single gene encoding the protein.
MAPPING
Using a panel of rodent-human somatic cell hybrids, Ueyama et al. (1991)
assigned the ZAG gene to human chromosome 7.
By fluorescence in situ hybridization, Ueyama et al. (1993) mapped the
functional gene, which they symbolized ZA2G, to 7q22.1. They concluded
that at least one of the pseudogenes is closely linked to the functional
chain.
Pendas et al. (1994) also used fluorescence in situ hybridization to map
the AZGP1 gene to 7q22.
GENE STRUCTURE
Freije et al. (1993) found that the AZGP1 gene spans over 9.7 kb and
that its overall organization and nucleotide sequence resemble those of
the first 4 exons of class I MHC genes (see 142800). However, it differs
from those genes by its lack of coding information for transmembrane and
cytoplasmic domains typical of MHC genes, which is consistent with its
presence as a soluble protein in various physiologic and pathologic
fluids. In addition, it contains a high density of repetitive sequences,
including Alu, MER, and MIR elements, which are not present at
equivalent positions in class I MHC genes. The human genome also
contains a putative AZGP1 pseudogene.
Ueyama et al. (1993) isolated the functional gene and found it to be 9.3
kb long and composed of 4 exons. The first exon codes for the 5-prime
untranslated region, the signal sequence, and the first 6 amino acids.
The second exon codes for domain A, the third for domain B, and the
fourth for domain C and the 3-prime untranslated region. Ueyama et al.
(1993) also isolated 2 pseudogenes retaining exon-intron organization.
GENE FUNCTION
Freije et al. (1991) studied the expression of this protein in benign
and malignant breast tissues.
Freije et al. (1993) suggested that in light of the lack of polymorphism
in the AZGP1 gene in comparison with MHC genes, this human glycoprotein
may have a role in the transport of nonpolymorphic substances or in
intercellular recognition processes.
MOLECULAR GENETICS
Nakayashiki and Katsura (1989) studied ZAG in plasma by polyacrylamide
gel isoelectric focusing followed by immunoblotting with specific
antiserum to ZAG in the Japanese population. Most of 1,224 plasma
samples showed a common, single-band pattern, whereas 16 samples showed
variant double-band patterns which were classified into 4 types. The
desialyzed form of ZAG commonly showed the single band. Differences in
ZAG phenotypes appeared to be due to amino acid substitutions of the ZAG
molecule. Nakayashiki and Katsura (1989) proposed the existence of 5
alleles, designated ZAG*1, ZAG*2, ZAG*3, ZAG*4 and ZAG*5, with
frequencies of 0.9935, 0.0025, 0.0016, 0.0004, and 0.0020, respectively.
The codominant transmission of the rare alleles ZAG*3 and ZAG*4 was
confirmed in family studies.
*FIELD* SA
Kamboh and Ferrell (1986)
*FIELD* RF
1. Araki, T.; Gejyo, F.; Takagaki, K.; Haupt, H.; Schwick, H. G.;
Burgi, W.; Marti, T.; Schaller, J.; Rickli, E.; Brossmer, R.; Atkinson,
P. H.; Putnam, F. W.; Schmid, K.: Complete amino acid sequence of
human plasma Zn-alpha(2)-glycoprotein and its homology to histocompatibility
antigens. Proc. Nat. Acad. Sci. 85: 679-683, 1988.
2. Burgi, W.; Schmid, K.: Preparation and properties of Zn-alpha(2)-glycoprotein
of normal human plasma. J. Biol. Chem. 236: 1066-1074, 1961.
3. Freije, J. P.; Fueyo, A.; Uria, J.; Lopez-Otin, C.: Human Zn-alpha-2-glycoprotein
cDNA cloning and expression analysis in benign and malignant breast
tissues. FEBS Lett. 290: 247-249, 1991.
4. Freije, J. P.; Fueyo, A.; Uria, J. A.; Velasco, G.; Sanchez, L.
M.; Lopez-Boado, Y. S.; Lopez-Otin, C.: Human Zn-alpha-2-glycoprotein:
complete genomic sequence, identification of a related pseudogene
and relationship to class I major histocompatibility complex genes. Genomics 18:
575-587, 1993.
5. Kamboh, M. I.; Ferrell, R. E.: Genetic studies of low-abundance
human plasma proteins. I. Microheterogeneity of zinc-alpha(2)-glycoprotein
in biological fluids. Biochem. Genet. 24: 849-857, 1986.
6. Nakayashiki, N.; Katsura, S.: Four variants of human plasma Zn-alpha(2)-glycoprotein
(ZAG) in the Japanese population. Hum. Genet. 82: 293-295, 1989.
7. Pendas, A. M.; Matilla, T.; Uria, J. A.; Freije, J. P.; Fueyo,
A.; Estivill, X.; Lopez-Otin, C.: Mapping of the human Zn-alpha-2-glycoprotein
gene (AZGP1) to chromosome 7q22 by in situ hybridization. Cytogenet.
Cell Genet. 66: 263-266, 1994.
8. Ueyama, H.; Han-Xiang, D.; Ohkubo, I.: Molecular cloning and chromosomal
assignment of the gene for human Zn-alpha-2-glycoprotein. Biochemistry 32:
12968-12976, 1993.
9. Ueyama, H.; Niwa, M.; Tada, T.; Sasaki, M.; Ohkubo, I.: Cloning
and nucleotide sequence of a human Zn-alpha(2)-glycoprotein cDNA and
chromosomal assignment of its gene. Biochem. Biophys. Res. Commun. 177:
696-703, 1991.
*FIELD* CD
Victor A. McKusick: 8/7/1989
*FIELD* ED
carol: 05/29/2009
carol: 5/8/2003
jason: 6/28/1994
carol: 2/16/1994
carol: 4/16/1993
supermim: 3/16/1992
carol: 11/27/1991
carol: 9/4/1991