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 27-MAR-2024, entry version 144.
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 GlyCosmos; Q63678; 2 sites, No reported glycans.
DR GlyGen; Q63678; 2 sites.
DR PhosphoSitePlus; Q63678; -.
DR PaxDb; 10116-ENSRNOP00000001801; -.
DR Ensembl; ENSRNOT00055019154; ENSRNOP00055015429; ENSRNOG00055011286.
DR Ensembl; ENSRNOT00060043414; ENSRNOP00060035965; ENSRNOG00060024999.
DR Ensembl; ENSRNOT00065000074; ENSRNOP00065000074; ENSRNOG00065000046.
DR UCSC; RGD:2187; rat.
DR AGR; RGD:2187; -.
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:0007155; P:cell adhesion; ISS:UniProtKB.
DR GO; GO:0032869; P:cellular response to insulin stimulus; IEP:RGD.
DR GO; GO:0071286; P:cellular response to magnesium ion; IEP:RGD.
DR GO; GO:0001580; P:detection of chemical stimulus involved in sensory perception of bitter taste; ISO:RGD.
DR GO; GO:0006955; P:immune response; IBA:GO_Central.
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; 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.
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
//
