RET1_RAT
ID RET1_RAT Reviewed; 135 AA.
AC P02696;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 163.
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; Synonyms=Rbp-1;
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].
RX PubMed=3472205; DOI=10.1073/pnas.84.10.3209;
RA Sherman D.R., Lloyd R.S., Chytil F.;
RT "Rat cellular retinol-binding protein: cDNA sequence and rapid retinol-
RT dependent accumulation of mRNA.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:3209-3213(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3584109; DOI=10.1016/s0021-9258(18)48212-9;
RA Levin M.S., Li E., Ong D.E., Gordon J.I.;
RT "Comparison of the tissue-specific expression and developmental regulation
RT of two closely linked rodent genes encoding cytosolic retinol-binding
RT proteins.";
RL J. Biol. Chem. 262:7118-7124(1987).
RN [3]
RP PROTEIN SEQUENCE OF 2-135.
RC TISSUE=Liver;
RX PubMed=4039728; DOI=10.1016/s0021-9258(18)88998-0;
RA Sundelin J., Anundi H., Traegaardh L., Eriksson U., Lind P., Ronne H.,
RA Peterson P.A., Rask L.;
RT "The primary structure of rat liver cellular retinol-binding protein.";
RL J. Biol. Chem. 260:6488-6493(1985).
RN [4]
RP PROTEIN SEQUENCE OF 2-51.
RC TISSUE=Testis;
RX PubMed=6541654; DOI=10.1016/s0021-9258(18)90717-9;
RA Eriksson U., Das K., Busch C., Nordlinder H., Rask L., Sundelin J.,
RA Sallstrom J., Peterson P.A.;
RT "Cellular retinol-binding protein. Quantitation and distribution.";
RL J. Biol. Chem. 259:13464-13470(1984).
RN [5]
RP PROTEIN SEQUENCE OF 2-35.
RC TISSUE=Liver;
RX PubMed=6942701; DOI=10.1111/j.1749-6632.1981.tb12739.x;
RA Rask L., Anundi H., Boehme J., Eriksson U., Ronne H., Sege K.,
RA Peterson P.A.;
RT "Structural and functional studies of vitamin A-binding proteins.";
RL Ann. N. Y. Acad. Sci. 359:79-90(1981).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH ALL-TRANS-RETINOL,
RP FUNCTION, AND DOMAIN.
RX PubMed=7683727; DOI=10.1006/jmbi.1993.1238;
RA Cowan S.W., Newcomer M.E., Jones T.A.;
RT "Crystallographic studies on a family of cellular lipophilic transport
RT proteins. Refinement of P2 myelin protein and the structure determination
RT and refinement of cellular retinol-binding protein in complex with all-
RT trans-retinol.";
RL J. Mol. Biol. 230:1225-1246(1993).
RN [7] {ECO:0007744|PDB:1JBH, ECO:0007744|PDB:1KGL}
RP STRUCTURE BY NMR.
RX PubMed=11934897; DOI=10.1074/jbc.m201994200;
RA Franzoni L., Lucke C., Perez C., Cavazzini D., Rademacher M., Ludwig C.,
RA Spisni A., Rossi G.L., Ruterjans H.;
RT "Structure and backbone dynamics of Apo- and holo-cellular retinol-binding
RT protein in solution.";
RL J. Biol. Chem. 277:21983-21997(2002).
RN [8] {ECO:0007744|PDB:1MX7, ECO:0007744|PDB:1MX8}
RP STRUCTURE BY NMR IN COMPLEX WITH RETINOL, FUNCTION, AND DOMAIN.
RX PubMed=12850148; DOI=10.1016/s0022-2836(03)00629-6;
RA Lu J., Cistola D.P., Li E.;
RT "Two homologous rat cellular retinol-binding proteins differ in local
RT conformational flexibility.";
RL J. Mol. Biol. 330:799-812(2003).
CC -!- FUNCTION: Cytoplasmic retinol-binding protein (PubMed:7683727,
CC PubMed:12850148). Accepts retinol from the transport protein STRA6, and
CC thereby contributes to retinol uptake, storage and retinoid homeostasis
CC (By similarity). {ECO:0000250|UniProtKB:P09455,
CC ECO:0000269|PubMed:12850148, ECO:0000269|PubMed:7683727}.
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:0000269|PubMed:12850148,
CC ECO:0000269|PubMed:7683727}.
CC -!- SIMILARITY: Belongs to the calycin superfamily. Fatty-acid binding
CC protein (FABP) family. {ECO:0000305}.
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DR EMBL; M16459; AAA42021.1; -; mRNA.
DR EMBL; M19257; AAA40962.1; -; mRNA.
DR PIR; A29570; RJRTO.
DR RefSeq; NP_036865.1; NM_012733.4.
DR PDB; 1CRB; X-ray; 2.10 A; A=2-135.
DR PDB; 1JBH; NMR; -; A=1-135.
DR PDB; 1KGL; NMR; -; A=1-135.
DR PDB; 1MX7; NMR; -; A=2-135.
DR PDB; 1MX8; NMR; -; A=2-135.
DR PDBsum; 1CRB; -.
DR PDBsum; 1JBH; -.
DR PDBsum; 1KGL; -.
DR PDBsum; 1MX7; -.
DR PDBsum; 1MX8; -.
DR AlphaFoldDB; P02696; -.
DR BMRB; P02696; -.
DR SMR; P02696; -.
DR STRING; 10116.ENSRNOP00000018622; -.
DR iPTMnet; P02696; -.
DR PhosphoSitePlus; P02696; -.
DR PaxDb; P02696; -.
DR PRIDE; P02696; -.
DR Ensembl; ENSRNOT00000018622; ENSRNOP00000018622; ENSRNOG00000013794.
DR GeneID; 25056; -.
DR KEGG; rno:25056; -.
DR UCSC; RGD:3543; rat.
DR CTD; 5947; -.
DR RGD; 3543; Rbp1.
DR eggNOG; KOG4015; Eukaryota.
DR GeneTree; ENSGT00940000159675; -.
DR HOGENOM; CLU_113772_5_1_1; -.
DR InParanoid; P02696; -.
DR OMA; CMTTINW; -.
DR OrthoDB; 1377380at2759; -.
DR PhylomeDB; P02696; -.
DR TreeFam; TF316894; -.
DR Reactome; R-RNO-2453902; The canonical retinoid cycle in rods (twilight vision).
DR Reactome; R-RNO-975634; Retinoid metabolism and transport.
DR EvolutionaryTrace; P02696; -.
DR PRO; PR:P02696; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Bgee; ENSRNOG00000013794; Expressed in liver and 19 other tissues.
DR Genevisible; P02696; RN.
DR GO; GO:0044297; C:cell body; IDA:RGD.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0005811; C:lipid droplet; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:1904768; F:all-trans-retinol binding; ISS: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:0019841; F:retinol binding; IDA:RGD.
DR GO; GO:0015908; P:fatty acid transport; IBA:GO_Central.
DR GO; GO:0055088; P:lipid homeostasis; ISS:UniProtKB.
DR GO; GO:0030852; P:regulation of granulocyte differentiation; ISO:RGD.
DR GO; GO:0033189; P:response to vitamin A; ISO:RGD.
DR GO; GO:0002138; P:retinoic acid biosynthetic process; IEP:RGD.
DR GO; GO:0042573; P:retinoic acid metabolic process; ISO:RGD.
DR GO; GO:0042572; P:retinol metabolic process; IDA:RGD.
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 3D-structure; Cytoplasm; Direct protein sequencing; Lipid droplet;
KW Reference proteome; Retinol-binding; Transport; Vitamin A.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:4039728,
FT ECO:0000269|PubMed:6541654, ECO:0000269|PubMed:6942701"
FT CHAIN 2..135
FT /note="Retinol-binding protein 1"
FT /id="PRO_0000067394"
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:0007744|PDB:1MX8"
FT BINDING 109
FT /ligand="all-trans-retinol"
FT /ligand_id="ChEBI:CHEBI:17336"
FT /evidence="ECO:0007744|PDB:1CRB"
FT STRAND 7..16
FT /evidence="ECO:0007829|PDB:1CRB"
FT HELIX 17..22
FT /evidence="ECO:0007829|PDB:1CRB"
FT TURN 23..25
FT /evidence="ECO:0007829|PDB:1CRB"
FT HELIX 28..36
FT /evidence="ECO:0007829|PDB:1CRB"
FT STRAND 40..46
FT /evidence="ECO:0007829|PDB:1CRB"
FT STRAND 49..55
FT /evidence="ECO:0007829|PDB:1CRB"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:1MX7"
FT STRAND 61..66
FT /evidence="ECO:0007829|PDB:1CRB"
FT STRAND 71..74
FT /evidence="ECO:0007829|PDB:1CRB"
FT TURN 76..79
FT /evidence="ECO:0007829|PDB:1CRB"
FT STRAND 82..90
FT /evidence="ECO:0007829|PDB:1CRB"
FT STRAND 93..102
FT /evidence="ECO:0007829|PDB:1CRB"
FT STRAND 106..112
FT /evidence="ECO:0007829|PDB:1CRB"
FT STRAND 115..122
FT /evidence="ECO:0007829|PDB:1CRB"
FT STRAND 125..133
FT /evidence="ECO:0007829|PDB:1CRB"
SQ SEQUENCE 135 AA; 15834 MW; 680CCE3284BD28B7 CRC64;
MPVDFNGYWK MLSNENFEEY LRALDVNVAL RKIANLLKPD KEIVQDGDHM IIRTLSTFRN
YIMDFQVGKE FEEDLTGIDD RKCMTTVSWD GDKLQCVQKG EKEGRGWTQW IEGDELHLEM
RAEGVTCKQV FKKVH
