RET1_BOVIN
ID RET1_BOVIN Reviewed; 135 AA.
AC P02694; Q53J07; Q9TS50;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Retinol-binding protein 1;
DE AltName: Full=Cellular retinol-binding protein;
DE Short=CRBP;
DE AltName: Full=Cellular retinol-binding protein I;
DE Short=CRBP-I;
GN Name=RBP1;
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 [MRNA].
RA Jian C.;
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 2-135, AND FUNCTION.
RC TISSUE=Testis;
RX PubMed=7744071; DOI=10.1111/j.1432-1033.1995.tb20489.x;
RA Malpeli G., Stoppini M., Zapponi M.C., Folli C., Berni R.;
RT "Interactions with retinol and retinoids of bovine cellular retinol-binding
RT protein.";
RL Eur. J. Biochem. 229:486-493(1995).
RN [4]
RP PROTEIN SEQUENCE OF 2-31.
RC TISSUE=Retina;
RX PubMed=6269887; DOI=10.1016/0014-5793(81)80655-2;
RA Crabb J.W., Saari J.C.;
RT "N-terminal sequence homology among retinoid-binding proteins from bovine
RT retina.";
RL FEBS Lett. 130:15-18(1981).
CC -!- FUNCTION: Cytoplasmic retinol-binding protein (PubMed:7744071). Accepts
CC retinol from the transport protein STRA6, and thereby contributes to
CC retinol uptake, storage and retinoid homeostasis.
CC {ECO:0000250|UniProtKB:P09455, ECO:0000269|PubMed:7744071}.
CC -!- SUBUNIT: Interacts (only as retinol-free apoprotein) with STRA6.
CC {ECO:0000250|UniProtKB:P09455}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q00915}. Lipid
CC droplet {ECO:0000250|UniProtKB:Q00915}.
CC -!- DOMAIN: Forms a beta-barrel structure that accommodates hydrophobic
CC ligands in its interior. {ECO:0000250|UniProtKB:P09455}.
CC -!- SIMILARITY: Belongs to the calycin superfamily. Fatty-acid binding
CC protein (FABP) family. {ECO:0000305}.
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DR EMBL; AF502256; AAQ07459.1; -; mRNA.
DR EMBL; BC109589; AAI09590.1; -; mRNA.
DR PIR; S69360; S69360.
DR RefSeq; NP_001020514.1; NM_001025343.1.
DR AlphaFoldDB; P02694; -.
DR SMR; P02694; -.
DR PaxDb; P02694; -.
DR PRIDE; P02694; -.
DR GeneID; 537379; -.
DR KEGG; bta:537379; -.
DR CTD; 5947; -.
DR eggNOG; KOG4015; Eukaryota.
DR HOGENOM; CLU_113772_5_1_1; -.
DR InParanoid; P02694; -.
DR OrthoDB; 1377380at2759; -.
DR TreeFam; TF316894; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005811; C:lipid droplet; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:1904768; F:all-trans-retinol binding; IDA:UniProtKB.
DR GO; GO:0005504; F:fatty acid binding; IBA:GO_Central.
DR GO; GO:0016918; F:retinal binding; IEA:UniProtKB-KW.
DR GO; GO:0015908; P:fatty acid transport; IBA:GO_Central.
DR GO; GO:0055088; P:lipid homeostasis; ISS:UniProtKB.
DR GO; GO:0002138; P:retinoic acid biosynthetic process; IEA:InterPro.
DR GO; GO:0042572; P:retinol metabolic process; ISS:AgBase.
DR GO; GO:0006776; P:vitamin A metabolic process; ISS:UniProtKB.
DR Gene3D; 2.40.128.20; -; 1.
DR InterPro; IPR012674; Calycin.
DR InterPro; IPR031264; CRBP1.
DR InterPro; IPR000463; Fatty_acid-bd.
DR InterPro; IPR031259; ILBP.
DR InterPro; IPR000566; Lipocln_cytosolic_FA-bd_dom.
DR PANTHER; PTHR11955; PTHR11955; 1.
DR PANTHER; PTHR11955:SF56; PTHR11955:SF56; 1.
DR Pfam; PF00061; Lipocalin; 1.
DR PRINTS; PR00178; FATTYACIDBP.
DR SUPFAM; SSF50814; SSF50814; 1.
DR PROSITE; PS00214; FABP; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Lipid droplet; Reference proteome;
KW Retinol-binding; Transport; Vitamin A.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:6269887,
FT ECO:0000269|PubMed:7744071"
FT CHAIN 2..135
FT /note="Retinol-binding protein 1"
FT /id="PRO_0000067391"
FT REGION 22..32
FT /note="Important for interaction with STRA6"
FT /evidence="ECO:0000250|UniProtKB:P09455"
FT BINDING 41
FT /ligand="all-trans-retinol"
FT /ligand_id="ChEBI:CHEBI:17336"
FT /evidence="ECO:0000250|UniProtKB:P09455"
FT BINDING 63
FT /ligand="all-trans-retinol"
FT /ligand_id="ChEBI:CHEBI:17336"
FT /evidence="ECO:0000250|UniProtKB:P09455"
FT BINDING 109
FT /ligand="all-trans-retinol"
FT /ligand_id="ChEBI:CHEBI:17336"
FT /evidence="ECO:0000250|UniProtKB:P09455"
FT CONFLICT 23
FT /note="A -> G (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 119
FT /note="E -> L (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 135
FT /note="N -> H (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 135 AA; 15823 MW; E797084266BEA2B3 CRC64;
MPVDFTGYWK MLANENFEEY LRALDVNVAL RKIANLLKPD KEIVQEGDHM IIRTLSTFRN
YIMDFQVGKE FEEDLTGIDD RKCMTTVSWD GDKLECVQKG EKEGRGWTQW IEGDELHLEM
RVEGVVCKQV FKKVN
