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 02-SEP-2026, entry version 178. 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:12850148, CC PubMed:7683727). 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M16459; AAA42021.1; -; mRNA. DR EMBL; M19257; AAA40962.1; -; mRNA. DR PIR; A29570; RJRTO. DR RefSeq; NP_036865.1; NM_012733.5. 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 AlphaFoldDB; P02696; -. DR BMRB; P02696; -. DR SMR; P02696; -. DR FunCoup; P02696; 73. DR STRING; 10116.ENSRNOP00000018622; -. DR iPTMnet; P02696; -. DR PhosphoSitePlus; P02696; -. DR PaxDb; 10116-ENSRNOP00000018622; -. DR Ensembl; ENSRNOT00055029720; ENSRNOP00055023881; ENSRNOG00055017567. DR Ensembl; ENSRNOT00060014974; ENSRNOP00060011617; ENSRNOG00060008934. DR Ensembl; ENSRNOT00065010140; ENSRNOP00065007405; ENSRNOG00065006568. DR GeneID; 25056; -. DR KEGG; rno:25056; -. DR UCSC; RGD:3543; rat. DR AGR; RGD:3543; -. DR CTD; 5947; -. DR RGD; 3543; Rbp1. DR eggNOG; KOG4015; Eukaryota. DR HOGENOM; CLU_113772_5_1_1; -. DR InParanoid; P02696; -. DR OMA; DRKCMTC; -. DR OrthoDB; 354351at2759; -. DR PhylomeDB; P02696; -. 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 cell types or tissues. DR ExpressionAtlas; P02696; baseline and differential. DR GO; GO:0044297; C:cell body; IDA:RGD. DR GO; GO:0005737; C:cytoplasm; IDA:RGD. DR GO; GO:0005829; C:cytosol; ISO:RGD. 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; ISS:UniProtKB. DR GO; GO:0005504; F:fatty acid binding; IBA:GO_Central. 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:0019915; P:lipid storage; ISO:RGD. DR GO; GO:0030852; P:regulation of granulocyte differentiation; ISO:RGD. DR GO; GO:0080021; P:response to benzoic acid; IEP:RGD. DR GO; GO:0032526; P:response to retinoic acid; IEP:RGD. DR GO; GO:0033189; P:response to vitamin A; ISO:RGD. DR GO; GO:0002138; P:retinoic acid biosynthetic process; IEA:InterPro. DR GO; GO:0042573; P:retinoic acid metabolic process; ISO:RGD. DR GO; GO:0001523; P:retinoid 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 CDD; cd19462; CRBP1; 1. DR FunFam; 2.40.128.20:FF:000001; Fatty acid-binding protein, adipocyte; 1. 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; FATTY ACID BINDING PROTEIN; 1. DR Pfam; PF00061; Lipocalin; 1. DR PRINTS; PR00178; FATTYACIDBP. DR SUPFAM; SSF50814; Lipocalins; 1. DR PROSITE; PS00214; FABP; 1. DR PDBsum; 1CRB; -. DR PDBsum; 1JBH; -. DR PDBsum; 1KGL; -. DR PDBsum; 1MX7; -. DR PDBsum; 1MX8; -. 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 //