ID RABP1_CHICK Reviewed; 137 AA.
AC P40220; O42405; Q5R2I9;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 27-MAR-2024, entry version 135.
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 Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=15642085; DOI=10.1111/j.1525-142x.2005.05002.x;
RA Kuraku S., Usuda R., Kuratani S.;
RT "Comprehensive survey of carapacial ridge-specific genes in turtle implies
RT co-option of some regulatory genes in carapace evolution.";
RL Evol. Dev. 7:3-17(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-121.
RX PubMed=9608736; DOI=10.1023/a:1008864224100;
RA Kleinjan D.A., Dekker S., Guy J.A., Grosveld F.G.;
RT "Cloning and sequencing of the CRABP-I locus from chicken and pufferfish:
RT analysis of the promoter regions in transgenic mice.";
RL Transgenic Res. 7:85-94(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 10-113.
RX PubMed=1966833; DOI=10.1242/dev.110.2.371;
RA Vaessen M.-J., Meijers J.H.C., Bootsma D., Geurts van Kessel A.;
RT "The cellular retinoic-acid-binding protein is expressed in tissues
RT associated with retinoic-acid-induced malformations.";
RL Development 110:371-378(1990).
RN [4]
RP SEQUENCE REVISION.
RA Vaessen M.-J.;
RL Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the calycin superfamily. Fatty-acid binding
CC protein (FABP) family. {ECO:0000305}.
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DR EMBL; AB124570; BAD74120.1; -; mRNA.
DR EMBL; Y12243; CAA72930.1; -; Genomic_DNA.
DR EMBL; Y12244; CAA72930.1; JOINED; Genomic_DNA.
DR EMBL; X53701; CAA37738.2; -; mRNA.
DR PIR; A61629; A61629.
DR PIR; S13796; S13796.
DR RefSeq; NP_001025710.1; NM_001030539.1.
DR AlphaFoldDB; P40220; -.
DR SMR; P40220; -.
DR STRING; 9031.ENSGALP00000033996; -.
DR BindingDB; P40220; -.
DR ChEMBL; CHEMBL4945; -.
DR DrugCentral; P40220; -.
DR PaxDb; 9031-ENSGALP00000033996; -.
DR GeneID; 374211; -.
DR KEGG; gga:374211; -.
DR CTD; 1381; -.
DR VEuPathDB; HostDB:geneid_374211; -.
DR eggNOG; KOG4015; Eukaryota.
DR HOGENOM; CLU_113772_0_2_1; -.
DR InParanoid; P40220; -.
DR OMA; THWTREL; -.
DR OrthoDB; 46617at2759; -.
DR PhylomeDB; P40220; -.
DR Reactome; R-GGA-5365859; RA biosynthesis pathway.
DR PRO; PR:P40220; -.
DR Proteomes; UP000000539; Chromosome 10.
DR Bgee; ENSGALG00000003193; Expressed in spermatid and 8 other cell types or tissues.
DR ExpressionAtlas; P40220; baseline and differential.
DR GO; GO:0030424; C:axon; IDA:AgBase.
DR GO; GO:0070852; C:cell body fiber; IDA:AgBase.
DR GO; GO:0005829; C:cytosol; IDA:AgBase.
DR GO; GO:0043005; C:neuron projection; IDA:AgBase.
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:0001972; F:retinoic acid binding; IDA:AgBase.
DR GO; GO:0005501; F:retinoid binding; IDA:WormBase.
DR GO; GO:0019841; F:retinol binding; IEA:UniProtKB-KW.
DR GO; GO:0015908; P:fatty acid transport; IBA:GO_Central.
DR CDD; cd19460; CRABP1; 1.
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:SF62; CELLULAR RETINOIC ACID-BINDING PROTEIN 1; 1.
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.
PE 2: Evidence at transcript level;
KW Cytoplasm; Reference proteome; Retinol-binding; Transport; Vitamin A.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..137
FT /note="Cellular retinoic acid-binding protein 1"
FT /id="PRO_0000067409"
FT MOTIF 21..31
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT BINDING 132..134
FT /ligand="all-trans-retinoate"
FT /ligand_id="ChEBI:CHEBI:35291"
FT /evidence="ECO:0000250"
FT CONFLICT 6
FT /note="G -> R (in Ref. 2; CAA72930)"
FT /evidence="ECO:0000305"
FT CONFLICT 10..12
FT /note="MRS -> NSG (in Ref. 3; CAA37738)"
FT /evidence="ECO:0000305"
FT CONFLICT 113
FT /note="E -> I (in Ref. 3; CAA37738)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 137 AA; 15663 MW; A2480C82A0A9C7E4 CRC64;
MPNFAGTWKM RSSENFDELL KALGVNAMLR KVAVAAASKP HVEIRQDGDQ FYIKTSTTVR
TTEINFKIGE SFEEETVDGR KCRSLATWEN ENKIYCKQTL IEGDGPKTYW TRELANDELI
LTFGADDVVC TRIYVRE
//
