RET2_RAT
ID RET2_RAT Reviewed; 134 AA.
AC P06768;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Retinol-binding protein 2;
DE AltName: Full=Cellular retinol-binding protein II;
DE Short=CRBP-II;
GN Name=Rbp2; Synonyms=Crbpii;
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 [GENOMIC DNA].
RX PubMed=3029082; DOI=10.1016/s0021-9258(18)61526-1;
RA Demmer L.A., Birkenmeier E.H., Sweetser D.A., Levin M.S., Zollman S.,
RA Sparkes R.S., Mohandas T., Lusis A.J., Gordon J.I.;
RT "The cellular retinol binding protein II gene. Sequence analysis of the rat
RT gene, chromosomal localization in mice and humans, and documentation of its
RT close linkage to the cellular retinol binding protein gene.";
RL J. Biol. Chem. 262:2458-2467(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3461459; DOI=10.1073/pnas.83.16.5779;
RA Li E., Demmer L.A., Sweetser D.A., Ong D.E., Gordon J.I.;
RT "Rat cellular retinol-binding protein II: use of a cloned cDNA to define
RT its primary structure, tissue-specific expression, and developmental
RT regulation.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:5779-5783(1986).
RN [3]
RP PROTEIN SEQUENCE OF 2-134.
RX PubMed=2645288; DOI=10.1016/s0021-9258(19)84985-2;
RA Schaefer W.H., Kakkad B., Crow J.A., Blair I.A., Ong D.E.;
RT "Purification, primary structure characterization, and cellular
RT distribution of two forms of cellular retinol-binding protein, type II from
RT adult rat small intestine.";
RL J. Biol. Chem. 264:4212-4221(1989).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH ALL-TRANS-RETINOL.
RX PubMed=8487303; DOI=10.1006/jmbi.1993.1239;
RA Winter N.S., Bratt J.M., Banaszak L.J.;
RT "Crystal structures of holo and apo-cellular retinol-binding protein II.";
RL J. Mol. Biol. 230:1247-1259(1993).
RN [5]
RP STRUCTURE BY NMR.
RX PubMed=10047490; DOI=10.1006/jmbi.1999.2544;
RA Lu J., Lin C.L., Tang C., Ponder J.W., Kao J.L., Cistola D.P., Li E.;
RT "The structure and dynamics of rat apo-cellular retinol-binding protein II
RT in solution: comparison with the X-ray structure.";
RL J. Mol. Biol. 286:1179-1195(1999).
CC -!- FUNCTION: Intracellular transport of retinol.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- DOMAIN: Forms a beta-barrel structure that accommodates hydrophobic
CC ligands in its interior.
CC -!- SIMILARITY: Belongs to the calycin superfamily. Fatty-acid binding
CC protein (FABP) family. {ECO:0000305}.
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DR EMBL; M13949; AAA42022.1; -; mRNA.
DR EMBL; M16402; AAA40963.1; ALT_SEQ; Genomic_DNA.
DR EMBL; M16400; AAA40963.1; JOINED; Genomic_DNA.
DR EMBL; M16401; AAA40963.1; JOINED; Genomic_DNA.
DR PIR; A92626; A29065.
DR RefSeq; NP_036772.2; NM_012640.2.
DR RefSeq; XP_006243669.1; XM_006243607.1.
DR RefSeq; XP_017450964.1; XM_017595475.1.
DR PDB; 1B4M; NMR; -; A=1-134.
DR PDB; 1EII; NMR; -; A=1-134.
DR PDB; 1OPA; X-ray; 1.90 A; A/B=1-134.
DR PDB; 1OPB; X-ray; 1.90 A; A/B/C/D=1-134.
DR PDBsum; 1B4M; -.
DR PDBsum; 1EII; -.
DR PDBsum; 1OPA; -.
DR PDBsum; 1OPB; -.
DR AlphaFoldDB; P06768; -.
DR BMRB; P06768; -.
DR SMR; P06768; -.
DR STRING; 10116.ENSRNOP00000018755; -.
DR PaxDb; P06768; -.
DR Ensembl; ENSRNOT00000018755; ENSRNOP00000018755; ENSRNOG00000013932.
DR GeneID; 24710; -.
DR KEGG; rno:24710; -.
DR UCSC; RGD:3544; rat.
DR CTD; 5948; -.
DR RGD; 3544; Rbp2.
DR eggNOG; KOG4015; Eukaryota.
DR GeneTree; ENSGT00940000160165; -.
DR HOGENOM; CLU_113772_5_1_1; -.
DR InParanoid; P06768; -.
DR OMA; HWIEGDI; -.
DR OrthoDB; 1417203at2759; -.
DR PhylomeDB; P06768; -.
DR TreeFam; TF316894; -.
DR Reactome; R-RNO-975634; Retinoid metabolism and transport.
DR EvolutionaryTrace; P06768; -.
DR PRO; PR:P06768; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Bgee; ENSRNOG00000013932; Expressed in jejunum and 14 other tissues.
DR Genevisible; P06768; RN.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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:0042572; P:retinol metabolic process; TAS:RGD.
DR Gene3D; 2.40.128.20; -; 1.
DR InterPro; IPR012674; Calycin.
DR InterPro; IPR000463; Fatty_acid-bd.
DR InterPro; IPR031259; ILBP.
DR InterPro; IPR000566; Lipocln_cytosolic_FA-bd_dom.
DR PANTHER; PTHR11955; PTHR11955; 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; Reference proteome;
KW Retinol-binding; Transport; Vitamin A.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2645288"
FT CHAIN 2..134
FT /note="Retinol-binding protein 2"
FT /id="PRO_0000067398"
FT BINDING 41
FT /ligand="all-trans-retinol"
FT /ligand_id="ChEBI:CHEBI:17336"
FT /evidence="ECO:0000250|UniProtKB:P50120"
FT BINDING 109
FT /ligand="all-trans-retinol"
FT /ligand_id="ChEBI:CHEBI:17336"
FT /evidence="ECO:0000269|PubMed:8487303"
FT STRAND 7..16
FT /evidence="ECO:0007829|PDB:1OPA"
FT HELIX 17..23
FT /evidence="ECO:0007829|PDB:1OPA"
FT HELIX 28..34
FT /evidence="ECO:0007829|PDB:1OPA"
FT STRAND 40..46
FT /evidence="ECO:0007829|PDB:1OPA"
FT STRAND 49..55
FT /evidence="ECO:0007829|PDB:1OPA"
FT STRAND 60..66
FT /evidence="ECO:0007829|PDB:1OPA"
FT STRAND 71..74
FT /evidence="ECO:0007829|PDB:1OPA"
FT TURN 76..79
FT /evidence="ECO:0007829|PDB:1OPA"
FT STRAND 82..90
FT /evidence="ECO:0007829|PDB:1OPA"
FT STRAND 93..102
FT /evidence="ECO:0007829|PDB:1OPA"
FT STRAND 106..112
FT /evidence="ECO:0007829|PDB:1OPA"
FT STRAND 115..122
FT /evidence="ECO:0007829|PDB:1OPA"
FT STRAND 125..133
FT /evidence="ECO:0007829|PDB:1OPA"
SQ SEQUENCE 134 AA; 15585 MW; 68491539A0115208 CRC64;
MTKDQNGTWE MESNENFEGY MKALDIDFAT RKIAVRLTQT KIIVQDGDNF KTKTNSTFRN
YDLDFTVGVE FDEHTKGLDG RNVKTLVTWE GNTLVCVQKG EKENRGWKQW VEGDKLYLEL
TCGDQVCRQV FKKK
