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   24-JAN-2024, entry version 173.
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
RC   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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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   SwissPalm; Q00915; -.
DR   REPRODUCTION-2DPAGE; Q00915; -.
DR   PaxDb; 10090-ENSMUSP00000059749; -.
DR   PeptideAtlas; Q00915; -.
DR   ProteomicsDB; 253214; -.
DR   Pumba; Q00915; -.
DR   Antibodypedia; 17981; 533 antibodies from 36 providers.
DR   DNASU; 19659; -.
DR   Ensembl; ENSMUST00000052068.11; ENSMUSP00000059749.10; ENSMUSG00000046402.11.
DR   GeneID; 19659; -.
DR   KEGG; mmu:19659; -.
DR   UCSC; uc009rdj.1; mouse.
DR   AGR; MGI:97876; -.
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; 46617at2759; -.
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 79 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 289 other cell types or tissues.
DR   ExpressionAtlas; Q00915; baseline and differential.
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:0080021; P:response to benzoic acid; IEA:Ensembl.
DR   GO; GO:0032526; P:response to retinoic acid; IEA:Ensembl.
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   CDD; cd19462; CRBP1; 1.
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; FATTY ACID BINDING PROTEIN; 1.
DR   PANTHER; PTHR11955:SF56; RETINOL-BINDING PROTEIN 1; 1.
DR   Pfam; PF00061; Lipocalin; 1.
DR   PRINTS; PR00178; FATTYACIDBP.
DR   SUPFAM; SSF50814; Lipocalins; 1.
DR   PROSITE; PS00214; FABP; 1.
DR   Genevisible; Q00915; MM.
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
//