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ZA2G_BOVIN
ID   ZA2G_BOVIN              Reviewed;         299 AA.
AC   Q3ZCH5;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 124.
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   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Mammary gland;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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 {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the MHC class I family. {ECO:0000305}.
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DR   EMBL; BC102237; AAI02238.1; -; mRNA.
DR   RefSeq; NP_001029503.1; NM_001034331.1.
DR   AlphaFoldDB; Q3ZCH5; -.
DR   SMR; Q3ZCH5; -.
DR   STRING; 9913.ENSBTAP00000037042; -.
DR   PaxDb; Q3ZCH5; -.
DR   PeptideAtlas; Q3ZCH5; -.
DR   PRIDE; Q3ZCH5; -.
DR   GeneID; 508800; -.
DR   KEGG; bta:508800; -.
DR   CTD; 563; -.
DR   eggNOG; ENOG502RWW3; Eukaryota.
DR   HOGENOM; CLU_047501_0_1_1; -.
DR   InParanoid; Q3ZCH5; -.
DR   OrthoDB; 912212at2759; -.
DR   TreeFam; TF336617; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0002476; P:antigen processing and presentation of endogenous peptide antigen via MHC class Ib; IBA:GO_Central.
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; 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   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.
DR   PROSITE; PS00290; IG_MHC; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..299
FT                   /note="Zinc-alpha-2-glycoprotein"
FT                   /id="PRO_0000317709"
FT   DOMAIN          204..289
FT                   /note="Ig-like C1-type"
FT   CARBOHYD        24
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        125
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        256
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        120..183
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        222..277
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ   SEQUENCE   299 AA;  33852 MW;  55A2D1179A8FDB54 CRC64;
     MVPVLLALLL LLGPAVSEET QAGNYSLSFL YTGLSKPREG FPSFQAVAYL NDQPFFHYNS
     EGRRAEPLAP WSQVEGMEDW EKESALQRAR EDIFMETLSD IMDYYKDREG SHTFQGAFGC
     ELRNNESSGA FWGYAYDGQD FIKFDKEIPA WVPLDPAAQN TKRKWEAEAV YVQRAKAYLE
     EECPGMLRRY LPYSRTHLDR QESPSVSVTG HAAPGHKRTL KCLAYDFYPR SIGLHWTRAG
     DAQEAESGGD VLPSGNGTYQ SWVVVGVPPE DQAPYSCHVE HRSLTRPLTV PWDPRQQAE
 
 
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