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RABP1_CHICK
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   03-AUG-2022, entry version 129.
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; P40220; -.
DR   Ensembl; ENSGALT00000034639; ENSGALP00000033996; ENSGALG00000003193.
DR   GeneID; 374211; -.
DR   KEGG; gga:374211; -.
DR   CTD; 1381; -.
DR   VEuPathDB; HostDB:geneid_374211; -.
DR   eggNOG; KOG4015; Eukaryota.
DR   GeneTree; ENSGT00940000159422; -.
DR   HOGENOM; CLU_113772_0_2_1; -.
DR   InParanoid; P40220; -.
DR   OMA; EINFRIG; -.
DR   OrthoDB; 1443155at2759; -.
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 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   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   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
 
 
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