RABP1_BOVIN
ID RABP1_BOVIN Reviewed; 137 AA.
AC P62964; P02695; P02697; P15780; Q2KI87; Q5PXY6;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Cellular retinoic acid-binding protein 1;
DE AltName: Full=Cellular retinoic acid-binding protein I;
DE Short=CRABP-I;
GN Name=CRABP1;
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].
RC TISSUE=Adrenal gland;
RX PubMed=2833392; DOI=10.1111/j.1432-1033.1988.tb13964.x;
RA Nilsson M.H.L., Spurr N.K., Saksena P., Busch C., Nordlinder H.,
RA Peterson P.A., Rask L., Sundelin J.;
RT "Isolation and characterization of a cDNA clone corresponding to bovine
RT cellular retinoic-acid-binding protein and chromosomal localization of the
RT corresponding human gene.";
RL Eur. J. Biochem. 173:45-51(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3039499; DOI=10.1073/pnas.84.16.5645;
RA Shubeita H.E., Sambrook J.F., McCormick A.M.;
RT "Molecular cloning and analysis of functional cDNA and genomic clones
RT encoding bovine cellular retinoic acid-binding protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:5645-5649(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2856408; DOI=10.1210/mend-1-8-526;
RA Wei L.-N., Mertz J.R., Goodman D.S., Nguyen-Huu M.C.;
RT "Cellular retinoic acid- and cellular retinol-binding proteins:
RT complementary deoxyribonucleic acid cloning, chromosomal assignment, and
RT tissue specific expression.";
RL Mol. Endocrinol. 1:526-534(1987).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Jeong Y.-H., Lee S.-M., Park H.-Y., Kim H.-M., Yoon D.-H., Chung E.-R.,
RA Kang M.-J.;
RT "Bovine cellular retinoic acid binding protein 1.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Kidney;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP PROTEIN SEQUENCE OF 2-137.
RC TISSUE=Adrenal gland;
RX PubMed=2581956; DOI=10.1016/s0021-9258(18)88999-2;
RA Sundelin J., Das S.R., Eriksson U., Rask L., Peterson P.A.;
RT "The primary structure of bovine cellular retinoic acid-binding protein.";
RL J. Biol. Chem. 260:6494-6499(1985).
RN [7]
RP PROTEIN SEQUENCE OF 2-30.
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).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX PubMed=7704533; DOI=10.1016/s0969-2126(94)00125-1;
RA Kleywegt G.J., Bergfors T., Senn H., le Motte P., Gsell B., Shudo K.,
RA Jones T.A.;
RT "Crystal structures of cellular retinoic acid binding proteins I and II in
RT complex with all-trans-retinoic acid and a synthetic retinoid.";
RL Structure 2:1241-1258(1994).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
RX PubMed=10531482; DOI=10.1107/s0907444999011026;
RA Chaudhuri B.N., Kleywegt G.J., Broutin-L'Hermite I., Bergfors T., Senn H.,
RA Le Motte P., Partouche O., Jones T.A.;
RT "Structures of cellular retinoic acid binding proteins I and II in complex
RT with synthetic retinoids.";
RL Acta Crystallogr. D 55:1850-1857(1999).
CC -!- FUNCTION: Cytosolic CRABPs may regulate the access of retinoic acid to
CC the nuclear retinoic acid receptors.
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; X07436; CAA30317.1; -; mRNA.
DR EMBL; M17253; AAA30469.1; -; mRNA.
DR EMBL; M36808; AAA30470.1; -; mRNA.
DR EMBL; AY821681; AAV84003.1; -; mRNA.
DR EMBL; BC112728; AAI12729.1; -; mRNA.
DR PIR; A32704; RJBOA.
DR RefSeq; NP_851371.1; NM_181028.2.
DR PDB; 2CBR; X-ray; 2.80 A; A=2-137.
DR PDBsum; 2CBR; -.
DR AlphaFoldDB; P62964; -.
DR BMRB; P62964; -.
DR SMR; P62964; -.
DR STRING; 9913.ENSBTAP00000017158; -.
DR PaxDb; P62964; -.
DR PeptideAtlas; P62964; -.
DR PRIDE; P62964; -.
DR Ensembl; ENSBTAT00000017158; ENSBTAP00000017158; ENSBTAG00000012909.
DR GeneID; 282201; -.
DR KEGG; bta:282201; -.
DR CTD; 1381; -.
DR VEuPathDB; HostDB:ENSBTAG00000012909; -.
DR VGNC; VGNC:27685; CRABP1.
DR eggNOG; KOG4015; Eukaryota.
DR GeneTree; ENSGT00940000159422; -.
DR HOGENOM; CLU_113772_0_2_1; -.
DR InParanoid; P62964; -.
DR OMA; EINFRIG; -.
DR OrthoDB; 1443155at2759; -.
DR TreeFam; TF316894; -.
DR Reactome; R-BTA-5365859; RA biosynthesis pathway.
DR EvolutionaryTrace; P62964; -.
DR Proteomes; UP000009136; Chromosome 21.
DR Bgee; ENSBTAG00000012909; Expressed in retina and 92 other tissues.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; IDA:CAFA.
DR GO; GO:0005504; F:fatty acid binding; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IDA:CAFA.
DR GO; GO:0016918; F:retinal binding; IEA:UniProtKB-KW.
DR GO; GO:0001972; F:retinoic acid binding; IDA:CAFA.
DR GO; GO:0019841; F:retinol binding; IEA:UniProtKB-KW.
DR GO; GO:0015908; P:fatty acid transport; IBA:GO_Central.
DR GO; GO:0034653; P:retinoic acid catabolic process; IEA:InterPro.
DR Gene3D; 2.40.128.20; -; 1.
DR InterPro; IPR012674; Calycin.
DR InterPro; IPR031279; CRABP1.
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:SF62; PTHR11955:SF62; 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:2581956,
FT ECO:0000269|PubMed:6269887"
FT CHAIN 2..137
FT /note="Cellular retinoic acid-binding protein 1"
FT /id="PRO_0000067405"
FT BINDING 132..134
FT /ligand="all-trans-retinoate"
FT /ligand_id="ChEBI:CHEBI:35291"
FT CONFLICT 117
FT /note="D -> DD (in Ref. 2; AAA30469)"
FT /evidence="ECO:0000305"
FT STRAND 6..15
FT /evidence="ECO:0007829|PDB:2CBR"
FT HELIX 16..22
FT /evidence="ECO:0007829|PDB:2CBR"
FT HELIX 27..38
FT /evidence="ECO:0007829|PDB:2CBR"
FT STRAND 41..47
FT /evidence="ECO:0007829|PDB:2CBR"
FT STRAND 50..56
FT /evidence="ECO:0007829|PDB:2CBR"
FT STRAND 61..67
FT /evidence="ECO:0007829|PDB:2CBR"
FT STRAND 72..75
FT /evidence="ECO:0007829|PDB:2CBR"
FT STRAND 81..90
FT /evidence="ECO:0007829|PDB:2CBR"
FT STRAND 93..103
FT /evidence="ECO:0007829|PDB:2CBR"
FT STRAND 108..115
FT /evidence="ECO:0007829|PDB:2CBR"
FT STRAND 118..125
FT /evidence="ECO:0007829|PDB:2CBR"
FT STRAND 128..136
FT /evidence="ECO:0007829|PDB:2CBR"
SQ SEQUENCE 137 AA; 15592 MW; A3DB0494D88943B4 CRC64;
MPNFAGTWKM RSSENFDELL KALGVNAMLR KVAVAAASKP HVEIRQDGDQ FYIKTSTTVR
TTEINFKVGE GFEEETVDGR KCRSLPTWEN ENKIHCTQTL LEGDGPKTYW TRELANDELI
LTFGADDVVC TRIYVRE
