RET1_MOUSE
ID RET1_MOUSE Reviewed; 135 AA.
AC Q00915;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Retinol-binding protein 1;
DE AltName: Full=Cellular retinol-binding protein;
DE Short=CRBP;
DE AltName: Full=Cellular retinol-binding protein I;
DE Short=CRBP-I;
DE Short=mCRBPI;
GN Name=Rbp1; Synonyms=Crbpi, Rbp-1;
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].
RC TISSUE=Testis;
RX PubMed=1648481; DOI=10.1002/j.1460-2075.1991.tb07758.x;
RA Smith W.C., Nakshatri H., Leroy P., Rees J., Chambon P.;
RT "A retinoic acid response element is present in the mouse cellular retinol
RT binding protein I (mCRBPI) promoter.";
RL EMBO J. 10:2223-2230(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX PubMed=10487743; DOI=10.1093/emboj/18.18.4903;
RA Ghyselinck N.B., Baavik C., Sapin V., Mark M., Bonnier D., Hindelang C.,
RA Dierich A., Nilsson C.B., Haakansson H., Sauvant P., Azais-Braesco V.,
RA Frasson M., Picaud S., Chambon P.;
RT "Cellular retinol-binding protein I is essential for vitamin A
RT homeostasis.";
RL EMBO J. 18:4903-4914(1999).
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15632377; DOI=10.1093/jnci/dji004;
RA Farias E.F., Ong D.E., Ghyselinck N.B., Nakajo S., Kuppumbatti Y.S.,
RA Mira y Lopez R.;
RT "Cellular retinol-binding protein I, a regulator of breast epithelial
RT retinoic acid receptor activity, cell differentiation, and
RT tumorigenicity.";
RL J. Natl. Cancer Inst. 97:21-29(2005).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen, 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 [6]
RP FUNCTION.
RX PubMed=22665496; DOI=10.1128/mcb.00505-12;
RA Berry D.C., O'Byrne S.M., Vreeland A.C., Blaner W.S., Noy N.;
RT "Cross talk between signaling and vitamin A transport by the retinol-
RT binding protein receptor STRA6.";
RL Mol. Cell. Biol. 32:3164-3175(2012).
RN [7]
RP DISRUPTION PHENOTYPE.
RX PubMed=26030625; DOI=10.1371/journal.pgen.1005213;
RA Ruehl R., Krzyzosiak A., Niewiadomska-Cimicka A., Rochel N., Szeles L.,
RA Vaz B., Wietrzych-Schindler M., Alvarez S., Szklenar M., Nagy L.,
RA de Lera A.R., Krezel W.;
RT "9-cis-13,14-Dihydroretinoic Acid Is an Endogenous Retinoid Acting as RXR
RT Ligand in Mice.";
RL PLoS Genet. 11:E1005213-E1005213(2015).
CC -!- FUNCTION: Cytoplasmic retinol-binding protein. Accepts retinol from the
CC transport protein STRA6, and thereby contributes to retinol uptake,
CC storage and retinoid homeostasis. {ECO:0000269|PubMed:10487743,
CC ECO:0000269|PubMed:15632377, ECO:0000269|PubMed:22665496}.
CC -!- SUBUNIT: Interacts (only as retinol-free apoprotein) with STRA6.
CC {ECO:0000250|UniProtKB:P09455}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10487743}. Lipid
CC droplet {ECO:0000269|PubMed:15632377}.
CC -!- DOMAIN: Forms a beta-barrel structure that accommodates hydrophobic
CC ligands in its interior. {ECO:0000250|UniProtKB:P09455}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype when mice are kept on a
CC vitamin A-enriched diet. Still, mutant mice have impaired vitamin A
CC homeostasis. Four week old mice have reduced levels of retinoids in the
CC liver, due to more rapid vitamin A turnover. When mice are kept on a
CC vitamin A-deficient diet after weaning, they gain weight normally
CC during the first 5 weeks, and then stop gaining weight. Their hepatic
CC retinyl palmitate stores begin to decrease from the moment they are fed
CC a vitamin A-deficient diet and become undetectable after 14 weeks,
CC After this, serum retinol levels decrease rapidly and approach
CC undetectable levels after 24 weeks on a vitamin A-deficient diet. After
CC 23 weeks on a vitamin A-deficient diet, electroretinograms show
CC dramatically decreased amplitudes of the a and b waves in response to
CC light. At the same time, their eyes show impaired contact between the
CC retinal pigment epithelium and the outer segment photoreceptors.
CC Knockout mice exhibit memory deficits (PubMed:26030625).
CC {ECO:0000269|PubMed:10487743, ECO:0000269|PubMed:26030625}.
CC -!- SIMILARITY: Belongs to the calycin superfamily. Fatty-acid binding
CC protein (FABP) family. {ECO:0000305}.
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DR EMBL; X60367; CAA42919.1; -; mRNA.
DR EMBL; BC018254; AAH18254.1; -; mRNA.
DR CCDS; CCDS23424.1; -.
DR PIR; S16355; S16355.
DR RefSeq; NP_035384.1; NM_011254.5.
DR AlphaFoldDB; Q00915; -.
DR BMRB; Q00915; -.
DR SMR; Q00915; -.
DR BioGRID; 202827; 1.
DR CORUM; Q00915; -.
DR STRING; 10090.ENSMUSP00000059749; -.
DR iPTMnet; Q00915; -.
DR PhosphoSitePlus; Q00915; -.
DR REPRODUCTION-2DPAGE; Q00915; -.
DR PaxDb; Q00915; -.
DR PeptideAtlas; Q00915; -.
DR PRIDE; Q00915; -.
DR ProteomicsDB; 253214; -.
DR Antibodypedia; 17981; 497 antibodies from 36 providers.
DR DNASU; 19659; -.
DR Ensembl; ENSMUST00000052068; ENSMUSP00000059749; ENSMUSG00000046402.
DR GeneID; 19659; -.
DR KEGG; mmu:19659; -.
DR UCSC; uc009rdj.1; mouse.
DR CTD; 5947; -.
DR MGI; MGI:97876; Rbp1.
DR VEuPathDB; HostDB:ENSMUSG00000046402; -.
DR eggNOG; KOG4015; Eukaryota.
DR GeneTree; ENSGT00940000159675; -.
DR HOGENOM; CLU_113772_5_1_1; -.
DR InParanoid; Q00915; -.
DR OMA; CMTTINW; -.
DR OrthoDB; 1377380at2759; -.
DR PhylomeDB; Q00915; -.
DR TreeFam; TF316894; -.
DR Reactome; R-MMU-2453902; The canonical retinoid cycle in rods (twilight vision).
DR Reactome; R-MMU-975634; Retinoid metabolism and transport.
DR BioGRID-ORCS; 19659; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Rbp1; mouse.
DR PRO; PR:Q00915; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q00915; protein.
DR Bgee; ENSMUSG00000046402; Expressed in choroid plexus of fourth ventricle and 287 other tissues.
DR ExpressionAtlas; Q00915; baseline and differential.
DR Genevisible; Q00915; MM.
DR GO; GO:0044297; C:cell body; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005811; C:lipid droplet; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:1904768; F:all-trans-retinol binding; ISS:UniProtKB.
DR GO; GO:0005504; F:fatty acid binding; IBA:GO_Central.
DR GO; GO:0016918; F:retinal binding; IEA:UniProtKB-KW.
DR GO; GO:0005501; F:retinoid binding; TAS:MGI.
DR GO; GO:0019841; F:retinol binding; ISO:MGI.
DR GO; GO:0015908; P:fatty acid transport; IBA:GO_Central.
DR GO; GO:0055088; P:lipid homeostasis; ISS:UniProtKB.
DR GO; GO:0030852; P:regulation of granulocyte differentiation; IMP:MGI.
DR GO; GO:0033189; P:response to vitamin A; IMP:MGI.
DR GO; GO:0002138; P:retinoic acid biosynthetic process; IEA:Ensembl.
DR GO; GO:0042573; P:retinoic acid metabolic process; IMP:MGI.
DR GO; GO:0042572; P:retinol metabolic process; IMP:MGI.
DR GO; GO:0006776; P:vitamin A metabolic process; ISS:UniProtKB.
DR Gene3D; 2.40.128.20; -; 1.
DR InterPro; IPR012674; Calycin.
DR InterPro; IPR031264; CRBP1.
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:SF56; PTHR11955:SF56; 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 Cytoplasm; Lipid droplet; Reference proteome; Retinol-binding; Transport;
KW Vitamin A.
FT CHAIN 1..135
FT /note="Retinol-binding protein 1"
FT /id="PRO_0000067393"
FT REGION 22..32
FT /note="Important for interaction with STRA6"
FT /evidence="ECO:0000250|UniProtKB:P09455"
FT BINDING 41
FT /ligand="all-trans-retinol"
FT /ligand_id="ChEBI:CHEBI:17336"
FT /evidence="ECO:0000250|UniProtKB:P09455"
FT BINDING 63
FT /ligand="all-trans-retinol"
FT /ligand_id="ChEBI:CHEBI:17336"
FT /evidence="ECO:0000250|UniProtKB:P09455"
FT BINDING 109
FT /ligand="all-trans-retinol"
FT /ligand_id="ChEBI:CHEBI:17336"
FT /evidence="ECO:0000250|UniProtKB:P09455"
SQ SEQUENCE 135 AA; 15846 MW; 6816E73284BD28B7 CRC64;
MPVDFNGYWK MLSNENFEEY LRALDVNVAL RKIANLLKPD KEIVQDGDHM IIRTLSTFRN
YIMDFQVGKE FEEDLTGIDD RKCMTTVSWD GDKLQCVQKG EKEGRGWTQW IEGDELHLEM
RAEGVICKQV FKKVH
