ID   ZA2G_RAT                Reviewed;         296 AA.
AC   Q63678; Q63523;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 137.
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   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley; 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 [MRNA] OF 4-296.
RC   TISSUE=Liver;
RX   PubMed=8056339; DOI=10.1016/0378-1119(94)90014-0;
RA   Fueyo A., Uria J.A., Freije J.M.P., Lopez-Otin C.;
RT   "Cloning and expression analysis of the cDNA encoding rat Zn-alpha 2-
RT   glycoprotein.";
RL   Gene 145:245-249(1994).
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   -!- TISSUE SPECIFICITY: Expressed in liver, but not in a wide number of
CC       tissues, including prostate, mammary gland, kidney, intestine, lung,
CC       pancreas, ovary, uterus, thyroid, placenta, spleen, brain and heart.
CC   -!- SIMILARITY: Belongs to the MHC class I family. {ECO:0000305}.
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DR   EMBL; D21058; BAA04637.1; -; mRNA.
DR   EMBL; X75309; CAA53057.1; -; mRNA.
DR   PIR; JX0353; JX0353.
DR   AlphaFoldDB; Q63678; -.
DR   SMR; Q63678; -.
DR   STRING; 10116.ENSRNOP00000001801; -.
DR   GlyGen; Q63678; 2 sites.
DR   PhosphoSitePlus; Q63678; -.
DR   PaxDb; Q63678; -.
DR   PRIDE; Q63678; -.
DR   UCSC; RGD:2187; rat.
DR   RGD; 2187; Azgp1.
DR   eggNOG; ENOG502RWW3; Eukaryota.
DR   InParanoid; Q63678; -.
DR   PhylomeDB; Q63678; -.
DR   Reactome; R-RNO-5223345; Miscellaneous transport and binding events.
DR   PRO; PR:Q63678; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR   GO; GO:0005615; C:extracellular space; ISO:RGD.
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:RGD.
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   SMART; SM00407; IGc1; 1.
DR   SUPFAM; SSF48726; SSF48726; 1.
DR   SUPFAM; SSF54452; SSF54452; 1.
DR   PROSITE; PS50835; IG_LIKE; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Pyrrolidone carboxylic acid;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000250"
FT   CHAIN           18..296
FT                   /note="Zinc-alpha-2-glycoprotein"
FT                   /id="PRO_0000019014"
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        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        120
FT                   /note="I -> S (in Ref. 2; CAA53057)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        194
FT                   /note="S -> C (in Ref. 2; CAA53057)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   296 AA;  34017 MW;  1259467DD18D4E3A CRC64;
     MVPVLLSLPL LLGPAVLQET GSYSLIFLYT GLSRPSKGLP RFQATAFLND QAFFHYNSNS
     GKAEPVEPWS HVEGMEDWEK ESQLQRAREE IFLVTLKDIM DYYEDSTGSH TFQGMFGCEI
     TNNRSSGAVW RYAYDGEDFI EFNKEIPAWI PLDPAAANTK LKWEAEKVYV QRAKAYLEEE
     CPTMLKKYLT YSRSHLDRTD PPTVKITSRV APGRNRIFRC LAYDFYPQRI SLHWNQASKK
     LASEPERGVF PNGNGTYLSW MEVEVPPQNR DPFVCHIEHK GLSQSLSVQW DEKSKV