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RET4_PANTR
ID   RET4_PANTR              Reviewed;         201 AA.
AC   P61641;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2004, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Retinol-binding protein 4;
DE   AltName: Full=Plasma retinol-binding protein;
DE            Short=PRBP;
DE            Short=RBP;
DE   Flags: Precursor;
GN   Name=RBP4;
OS   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9598;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Maekawa K., Kojima T., Fujiyama A., Hattori M., Sakaki Y.;
RT   "Chimpanzee DNA sequence of RP43-36M02, complete sequence.";
RL   Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Retinol-binding protein that mediates retinol transport in
CC       blood plasma. Delivers retinol from the liver stores to the peripheral
CC       tissues. Transfers the bound all-trans retinol to STRA6, that then
CC       facilitates retinol transport across the cell membrane.
CC       {ECO:0000250|UniProtKB:P02753}.
CC   -!- SUBUNIT: Interacts with TTR. Interaction with TTR prevents its loss by
CC       filtration through the kidney glomeruli. Interacts with STRA6.
CC       {ECO:0000250|UniProtKB:P02753}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02753}.
CC   -!- SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.
CC       {ECO:0000305}.
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DR   EMBL; AB124586; BAD16621.1; -; Genomic_DNA.
DR   RefSeq; NP_001038960.1; NM_001045495.1.
DR   RefSeq; XP_009457151.1; XM_009458876.2.
DR   RefSeq; XP_009457152.1; XM_009458877.2.
DR   AlphaFoldDB; P61641; -.
DR   BMRB; P61641; -.
DR   SMR; P61641; -.
DR   STRING; 9598.ENSPTRP00000004830; -.
DR   PaxDb; P61641; -.
DR   Ensembl; ENSPTRT00000005226; ENSPTRP00000004830; ENSPTRG00000002768.
DR   GeneID; 450617; -.
DR   KEGG; ptr:450617; -.
DR   CTD; 5950; -.
DR   VGNC; VGNC:5717; RBP4.
DR   eggNOG; ENOG502RXEW; Eukaryota.
DR   GeneTree; ENSGT00510000047107; -.
DR   HOGENOM; CLU_094618_0_0_1; -.
DR   InParanoid; P61641; -.
DR   OMA; FATFEDT; -.
DR   OrthoDB; 1631943at2759; -.
DR   TreeFam; TF331445; -.
DR   Proteomes; UP000002277; Chromosome 10.
DR   Bgee; ENSPTRG00000002768; Expressed in liver and 15 other tissues.
DR   GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR   GO; GO:0016918; F:retinal binding; IEA:UniProtKB-KW.
DR   GO; GO:0019841; F:retinol binding; IBA:GO_Central.
DR   GO; GO:0034632; F:retinol transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0001654; P:eye development; IEA:Ensembl.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:Ensembl.
DR   GO; GO:0042593; P:glucose homeostasis; IEA:Ensembl.
DR   GO; GO:0030277; P:maintenance of gastrointestinal epithelium; IEA:Ensembl.
DR   GO; GO:0032024; P:positive regulation of insulin secretion; IEA:Ensembl.
DR   GO; GO:0032526; P:response to retinoic acid; IEA:Ensembl.
DR   GO; GO:0042572; P:retinol metabolic process; IEA:Ensembl.
DR   GO; GO:0034633; P:retinol transport; IBA:GO_Central.
DR   Gene3D; 2.40.128.20; -; 1.
DR   InterPro; IPR012674; Calycin.
DR   InterPro; IPR022271; Lipocalin_ApoD.
DR   InterPro; IPR022272; Lipocalin_CS.
DR   InterPro; IPR000566; Lipocln_cytosolic_FA-bd_dom.
DR   InterPro; IPR002449; Retinol-bd/Purpurin.
DR   PANTHER; PTHR11873; PTHR11873; 1.
DR   Pfam; PF00061; Lipocalin; 1.
DR   PIRSF; PIRSF036893; Lipocalin_ApoD; 1.
DR   PIRSF; PIRSF500204; RBP_purpurin; 1.
DR   PRINTS; PR01174; RETINOLBNDNG.
DR   SUPFAM; SSF50814; SSF50814; 1.
DR   PROSITE; PS00213; LIPOCALIN; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Methylation; Reference proteome; Retinol-binding; Secreted;
KW   Signal; Transport; Vitamin A.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000250|UniProtKB:P02753"
FT   CHAIN           19..201
FT                   /note="Retinol-binding protein 4"
FT                   /id="PRO_0000017967"
FT   BINDING         116
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P27485"
FT   MOD_RES         139
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q00724"
FT   DISULFID        22..178
FT                   /evidence="ECO:0000250|UniProtKB:P02753"
FT   DISULFID        88..192
FT                   /evidence="ECO:0000250|UniProtKB:P02753"
FT   DISULFID        138..147
FT                   /evidence="ECO:0000250|UniProtKB:P02753"
SQ   SEQUENCE   201 AA;  23010 MW;  660C6DD8CC9B811A CRC64;
     MKWVWALLLL AALGSGRAER DCRVSSFRVK ENFDKARFSG TWYAMAKKDP EGLFLQDNIV
     AEFSVDETGQ MSATAKGRVR LLNNWDVCAD MVGTFTDTED PAKFKMKYWG VASFLQKGND
     DHWIVDTDYD TYAVQYSCRL LNLDGTCADS YSFVFSRDPN GLPPEAQKIV RQRQEELCLA
     RQYRLIVHNG YCDGRSERNL L
 
 
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