ZA2G_MOUSE
ID ZA2G_MOUSE Reviewed; 307 AA.
AC Q64726; Q9DBB7;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 172.
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;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Liver;
RX PubMed=7852290; DOI=10.1093/oxfordjournals.jbchem.a124579;
RA Ueyama H., Naitoh H., Ohkubo I.;
RT "Structure and expression of rat and mouse mRNAs for Zn-alpha 2-
RT glycoprotein.";
RL J. Biochem. 116:677-681(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/SvJ;
RA Wanner V., Bahram S.;
RT "The mouse ZAG gene.";
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=KK/Ta; TISSUE=Kidney;
RA Gohda T.;
RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Liver;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Liver;
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 235-304.
RC STRAIN=C57BL/6J;
RX PubMed=7797272; DOI=10.1007/bf00164991;
RA Noguchi M., Kitabatake A., Ishibashi T., Kasahara M.;
RT "The MHC class I-like Zn-alpha 2-glycoprotein gene maps to mouse chromosome
RT 5.";
RL Immunogenetics 42:72-74(1995).
RN [7]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-190.
RC STRAIN=C57BL/6J; TISSUE=Plasma;
RX PubMed=17330941; DOI=10.1021/pr0604559;
RA Bernhard O.K., Kapp E.A., Simpson R.J.;
RT "Enhanced analysis of the mouse plasma proteome using cysteine-containing
RT tryptic glycopeptides.";
RL J. Proteome Res. 6:987-995(2007).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Liver, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Stimulates lipid degradation in adipocytes and causes the
CC extensive fat losses associated with some advanced cancers.
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with PIP. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the MHC class I family. {ECO:0000305}.
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DR EMBL; D21059; BAA04638.1; -; mRNA.
DR EMBL; AF281658; AAQ14325.1; -; Genomic_DNA.
DR EMBL; AY248694; AAO93093.1; -; mRNA.
DR EMBL; AK005051; BAB23777.1; -; mRNA.
DR EMBL; BC061646; AAH61646.1; -; mRNA.
DR EMBL; D44593; BAA07996.1; -; Genomic_DNA.
DR CCDS; CCDS19783.1; -.
DR PIR; JX0352; JX0352.
DR RefSeq; NP_038506.2; NM_013478.2.
DR AlphaFoldDB; Q64726; -.
DR SMR; Q64726; -.
DR BioGRID; 198289; 3.
DR STRING; 10090.ENSMUSP00000038559; -.
DR GlyGen; Q64726; 3 sites.
DR iPTMnet; Q64726; -.
DR PhosphoSitePlus; Q64726; -.
DR CPTAC; non-CPTAC-3391; -.
DR CPTAC; non-CPTAC-3392; -.
DR jPOST; Q64726; -.
DR MaxQB; Q64726; -.
DR PaxDb; Q64726; -.
DR PeptideAtlas; Q64726; -.
DR PRIDE; Q64726; -.
DR ProteomicsDB; 275261; -.
DR Antibodypedia; 848; 369 antibodies from 33 providers.
DR DNASU; 12007; -.
DR Ensembl; ENSMUST00000035390; ENSMUSP00000038559; ENSMUSG00000037053.
DR GeneID; 12007; -.
DR KEGG; mmu:12007; -.
DR UCSC; uc009aeh.2; mouse.
DR CTD; 563; -.
DR MGI; MGI:103163; Azgp1.
DR VEuPathDB; HostDB:ENSMUSG00000037053; -.
DR eggNOG; ENOG502RWW3; Eukaryota.
DR GeneTree; ENSGT01040000240396; -.
DR HOGENOM; CLU_047501_0_1_1; -.
DR InParanoid; Q64726; -.
DR OMA; YQSWVVV; -.
DR OrthoDB; 912212at2759; -.
DR PhylomeDB; Q64726; -.
DR TreeFam; TF336617; -.
DR Reactome; R-MMU-5223345; Miscellaneous transport and binding events.
DR BioGRID-ORCS; 12007; 1 hit in 78 CRISPR screens.
DR ChiTaRS; Azgp1; mouse.
DR PRO; PR:Q64726; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q64726; protein.
DR Bgee; ENSMUSG00000037053; Expressed in left lobe of liver and 82 other tissues.
DR ExpressionAtlas; Q64726; baseline and differential.
DR Genevisible; Q64726; MM.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
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; ISS:UniProtKB.
DR GO; GO:0001580; P:detection of chemical stimulus involved in sensory perception of bitter taste; ISO:MGI.
DR GO; GO:0040014; P:regulation of multicellular organism growth; NAS: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; 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 SUPFAM; SSF48726; SSF48726; 1.
DR SUPFAM; SSF54452; SSF54452; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Pyrrolidone carboxylic acid;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000250"
FT CHAIN 18..307
FT /note="Zinc-alpha-2-glycoprotein"
FT /id="PRO_0000019013"
FT DOMAIN 202..287
FT /note="Ig-like C1-type"
FT MOD_RES 18
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250|UniProtKB:P25311"
FT CARBOHYD 123
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 190
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17330941"
FT CARBOHYD 254
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 118..181
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 220..275
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CONFLICT 24
FT /note="Y -> S (in Ref. 1; BAB23777 and 5; AAH61646)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 307 AA; 35332 MW; A116304EFE10F814 CRC64;
MVPVLLSLPL LLGPAVFQET GSYYLTFLYT GLSRPSKGFP RFQATAFLND QAFFHYNSNS
GKAEPVGPWS QVEGMEDWEK ESQLQRAREE IFLVTLKDIM DYYKDTTGSH TFQGMFGCEI
TNNRSSGAVW RYAYDGEDFI EFNKEIPAWI PLDPAAANTK LKWEAEKVYV QRAKAYLEEE
CPEMLKRYLN YSRSHLDRID PPTVTITSRV IPGGNRIFKC LAYGFYPQRI SLHWNKANKK
LAFEPERGVF PNGNGTYLSW AEVEVSPQDI DPFFCLIDHR GFSQSLSVQW DRTRKVKDEN
NVVAQPQ
