RABP1_MOUSE
ID RABP1_MOUSE Reviewed; 137 AA.
AC P62965; P02695; P02697; P15780; Q3UN78;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 144.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2538228;
RA Stoner C.M., Gudas L.J.;
RT "Mouse cellular retinoic acid binding protein: cloning, complementary DNA
RT sequence, and messenger RNA expression during the retinoic acid-induced
RT differentiation of F9 wild type and RA-3-10 mutant teratocarcinoma cells.";
RL Cancer Res. 49:1497-1504(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2171550; DOI=10.1089/dna.1990.9.471;
RA Wei L.-N., Tsao J.L., Chu Y.S., Jeannotte L., Nguyen-Huu M.C.;
RT "Molecular cloning and transcriptional mapping of the mouse cellular
RT retinoic acid-binding protein gene.";
RL DNA Cell Biol. 9:471-478(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2547683; DOI=10.1111/j.1432-0436.1989.tb00819.x;
RA Vaessen M.J., Kootwijk E., Mummery C., Hilkens J., Bootsma D.,
RA Geurts van Kessel A.;
RT "Preferential expression of cellular retinoic acid binding protein in a
RT subpopulation of neural cells in the developing mouse embryo.";
RL Differentiation 40:99-105(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 66-137.
RX PubMed=2546063; DOI=10.1210/mend-3-3-454;
RA Wei L.-N., Blaner W.S., Goodman D.S., Nguyen-Huu M.C.;
RT "Regulation of the cellular retinoid-binding proteins and their messenger
RT ribonucleic acids during P19 embryonal carcinoma cell differentiation
RT induced by retinoic acid.";
RL Mol. Endocrinol. 3:454-463(1989).
RN [6]
RP MUTAGENESIS.
RX PubMed=1377826; DOI=10.1002/prot.340130202;
RA Zhang J., Liu Z.-P., Jones A., Gierasch L.M., Sambrook J.F.;
RT "Mutating the charged residues in the binding pocket of cellular retinoic
RT acid-binding protein simultaneously reduces its binding affinity to
RT retinoic acid and increases its thermostability.";
RL Proteins 13:87-99(1992).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 (2.7 ANGSTROMS).
RX PubMed=7563063; DOI=10.1006/jmbi.1995.0509;
RA Thompson J.R., Bratt J.M., Banaszak L.J.;
RT "Crystal structure of cellular retinoic acid binding protein I shows
RT increased access to the binding cavity due to formation of an
RT intermolecular beta-sheet.";
RL J. Mol. Biol. 252:433-446(1995).
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; X15481; CAA33509.1; -; mRNA.
DR EMBL; M58015; AAA40027.1; -; Genomic_DNA.
DR EMBL; M58013; AAA40027.1; JOINED; Genomic_DNA.
DR EMBL; M58014; AAA40027.1; JOINED; Genomic_DNA.
DR EMBL; X51715; CAA36011.1; -; Genomic_DNA.
DR EMBL; X51716; CAA36011.1; JOINED; Genomic_DNA.
DR EMBL; X51717; CAA36011.1; JOINED; Genomic_DNA.
DR EMBL; X15789; CAA33790.1; -; mRNA.
DR EMBL; AK045283; BAC32295.1; -; mRNA.
DR EMBL; AK144397; BAE25869.1; -; mRNA.
DR EMBL; M31552; AAA37453.1; -; mRNA.
DR CCDS; CCDS23195.1; -.
DR PIR; A35825; A35825.
DR RefSeq; NP_038524.1; NM_013496.3.
DR PDB; 1CBI; X-ray; 2.70 A; A/B=2-137.
DR PDB; 1CBR; X-ray; 2.90 A; A/B=2-137.
DR PDBsum; 1CBI; -.
DR PDBsum; 1CBR; -.
DR AlphaFoldDB; P62965; -.
DR BMRB; P62965; -.
DR SMR; P62965; -.
DR STRING; 10090.ENSMUSP00000034830; -.
DR BindingDB; P62965; -.
DR ChEMBL; CHEMBL3208; -.
DR DrugCentral; P62965; -.
DR iPTMnet; P62965; -.
DR PhosphoSitePlus; P62965; -.
DR REPRODUCTION-2DPAGE; IPI00230721; -.
DR REPRODUCTION-2DPAGE; P62965; -.
DR MaxQB; P62965; -.
DR PaxDb; P62965; -.
DR PeptideAtlas; P62965; -.
DR PRIDE; P62965; -.
DR ProteomicsDB; 300293; -.
DR Antibodypedia; 1541; 258 antibodies from 30 providers.
DR DNASU; 12903; -.
DR Ensembl; ENSMUST00000034830; ENSMUSP00000034830; ENSMUSG00000032291.
DR GeneID; 12903; -.
DR KEGG; mmu:12903; -.
DR UCSC; uc009prp.2; mouse.
DR CTD; 1381; -.
DR MGI; MGI:88490; Crabp1.
DR VEuPathDB; HostDB:ENSMUSG00000032291; -.
DR eggNOG; KOG4015; Eukaryota.
DR GeneTree; ENSGT00940000159422; -.
DR HOGENOM; CLU_113772_0_2_1; -.
DR InParanoid; P62965; -.
DR OMA; EINFRIG; -.
DR OrthoDB; 1443155at2759; -.
DR PhylomeDB; P62965; -.
DR TreeFam; TF316894; -.
DR Reactome; R-MMU-5365859; RA biosynthesis pathway.
DR BioGRID-ORCS; 12903; 3 hits in 77 CRISPR screens.
DR ChiTaRS; Crabp1; mouse.
DR EvolutionaryTrace; P62965; -.
DR PRO; PR:P62965; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; P62965; protein.
DR Bgee; ENSMUSG00000032291; Expressed in otic placode and 251 other tissues.
DR Genevisible; P62965; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0005501; F:retinoid binding; TAS:MGI.
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 DisProt; DP00340; -.
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; Reference proteome; Retinol-binding; Transport;
KW Vitamin A.
FT CHAIN 1..137
FT /note="Cellular retinoic acid-binding protein 1"
FT /id="PRO_0000067407"
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 STRAND 6..15
FT /evidence="ECO:0007829|PDB:1CBI"
FT HELIX 16..22
FT /evidence="ECO:0007829|PDB:1CBI"
FT HELIX 27..36
FT /evidence="ECO:0007829|PDB:1CBI"
FT STRAND 41..47
FT /evidence="ECO:0007829|PDB:1CBI"
FT STRAND 50..56
FT /evidence="ECO:0007829|PDB:1CBI"
FT STRAND 61..67
FT /evidence="ECO:0007829|PDB:1CBI"
FT STRAND 72..75
FT /evidence="ECO:0007829|PDB:1CBI"
FT STRAND 81..90
FT /evidence="ECO:0007829|PDB:1CBI"
FT STRAND 93..103
FT /evidence="ECO:0007829|PDB:1CBI"
FT STRAND 108..115
FT /evidence="ECO:0007829|PDB:1CBI"
FT STRAND 118..125
FT /evidence="ECO:0007829|PDB:1CBI"
FT STRAND 128..136
FT /evidence="ECO:0007829|PDB:1CBI"
SQ SEQUENCE 137 AA; 15592 MW; A3DB0494D88943B4 CRC64;
MPNFAGTWKM RSSENFDELL KALGVNAMLR KVAVAAASKP HVEIRQDGDQ FYIKTSTTVR
TTEINFKVGE GFEEETVDGR KCRSLPTWEN ENKIHCTQTL LEGDGPKTYW TRELANDELI
LTFGADDVVC TRIYVRE
