RET4_MOUSE
ID RET4_MOUSE Reviewed; 201 AA.
AC Q00724; P70357; Q566I5;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Retinol-binding protein 4;
DE AltName: Full=Plasma retinol-binding protein;
DE Short=PRBP;
DE Short=RBP;
DE Flags: Precursor;
GN Name=Rbp4;
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 STRAIN=C57BL/6 X CBA;
RX PubMed=9721191; DOI=10.1006/abbi.1998.0821;
RA Jessen K.A., Satre M.A.;
RT "Induction of mouse retinol binding protein gene expression by cyclic AMP
RT in Hepa 1-6 cells.";
RL Arch. Biochem. Biophys. 357:126-130(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Maekawa K., Kojima T., Fujiyama A., Hattori M., Sakaki Y.;
RT "Genomic sequence of mouse retinol binding protein 4 region, complete
RT sequence.";
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Stomach;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Liver;
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-179.
RX PubMed=1613076;
RA Dale B., Jones A.H., Presland R., Adler D.A., Disteche C.M.;
RT "Chromosomal localization of the retinol binding protein gene and its
RT elimination as a candidate gene for the repeated epilation (Er) mutation in
RT mice.";
RL J. Craniofac. Genet. Dev. Biol. 12:76-81(1992).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen,
RC 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 [7]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-139, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Retinol-binding protein that mediates retinol transport in
CC blood plasma. Delivers retinol from the liver stores to the peripheral
CC tissues. Transfers the bound all-trans retinol to STRA6, that then
CC facilitates retinol transport across the cell membrane.
CC {ECO:0000250|UniProtKB:P02753}.
CC -!- SUBUNIT: Interacts with TTR. Interaction with TTR prevents its loss by
CC filtration through the kidney glomeruli. Interacts with STRA6.
CC {ECO:0000250|UniProtKB:P02753}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02753}.
CC -!- SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.
CC {ECO:0000305}.
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DR EMBL; U63146; AAB06955.1; -; mRNA.
DR EMBL; AB124638; BAD16678.1; -; Genomic_DNA.
DR EMBL; AK008765; BAB25881.1; -; mRNA.
DR EMBL; BC031809; AAH31809.1; -; mRNA.
DR EMBL; BC093529; AAH93529.1; -; mRNA.
DR EMBL; M74527; AAA63395.1; -; mRNA.
DR CCDS; CCDS29784.1; -.
DR RefSeq; NP_001152959.1; NM_001159487.1.
DR RefSeq; NP_035385.1; NM_011255.3.
DR AlphaFoldDB; Q00724; -.
DR SMR; Q00724; -.
DR BioGRID; 202830; 3.
DR STRING; 10090.ENSMUSP00000025951; -.
DR iPTMnet; Q00724; -.
DR PhosphoSitePlus; Q00724; -.
DR SwissPalm; Q00724; -.
DR CPTAC; non-CPTAC-3736; -.
DR EPD; Q00724; -.
DR jPOST; Q00724; -.
DR MaxQB; Q00724; -.
DR PaxDb; Q00724; -.
DR PRIDE; Q00724; -.
DR ProteomicsDB; 255289; -.
DR Antibodypedia; 885; 1427 antibodies from 45 providers.
DR DNASU; 19662; -.
DR Ensembl; ENSMUST00000112335; ENSMUSP00000107954; ENSMUSG00000024990.
DR GeneID; 19662; -.
DR KEGG; mmu:19662; -.
DR UCSC; uc008hjd.2; mouse.
DR CTD; 5950; -.
DR MGI; MGI:97879; Rbp4.
DR VEuPathDB; HostDB:ENSMUSG00000024990; -.
DR eggNOG; ENOG502RXEW; Eukaryota.
DR GeneTree; ENSGT00510000047107; -.
DR HOGENOM; CLU_094618_0_0_1; -.
DR InParanoid; Q00724; -.
DR OMA; FATFEDT; -.
DR OrthoDB; 1631943at2759; -.
DR PhylomeDB; Q00724; -.
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; 19662; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Rbp4; mouse.
DR PRO; PR:Q00724; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q00724; protein.
DR Bgee; ENSMUSG00000024990; Expressed in left lobe of liver and 192 other tissues.
DR ExpressionAtlas; Q00724; baseline and differential.
DR Genevisible; Q00724; MM.
DR GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0016918; F:retinal binding; IEA:UniProtKB-KW.
DR GO; GO:0019841; F:retinol binding; IDA:MGI.
DR GO; GO:0034632; F:retinol transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0048738; P:cardiac muscle tissue development; IMP:BHF-UCL.
DR GO; GO:0050908; P:detection of light stimulus involved in visual perception; IMP:MGI.
DR GO; GO:0048562; P:embryonic organ morphogenesis; IMP:BHF-UCL.
DR GO; GO:0060059; P:embryonic retina morphogenesis in camera-type eye; IMP:BHF-UCL.
DR GO; GO:0048706; P:embryonic skeletal system development; IMP:BHF-UCL.
DR GO; GO:0001654; P:eye development; IMP:BHF-UCL.
DR GO; GO:0048807; P:female genitalia morphogenesis; IMP:BHF-UCL.
DR GO; GO:0006094; P:gluconeogenesis; IMP:BHF-UCL.
DR GO; GO:0042593; P:glucose homeostasis; ISO:MGI.
DR GO; GO:0007507; P:heart development; IMP:BHF-UCL.
DR GO; GO:0060347; P:heart trabecula formation; IMP:BHF-UCL.
DR GO; GO:0030324; P:lung development; IMP:BHF-UCL.
DR GO; GO:0030277; P:maintenance of gastrointestinal epithelium; ISO:MGI.
DR GO; GO:0008584; P:male gonad development; IMP:MGI.
DR GO; GO:0060044; P:negative regulation of cardiac muscle cell proliferation; IMP:BHF-UCL.
DR GO; GO:0002639; P:positive regulation of immunoglobulin production; IDA:BHF-UCL.
DR GO; GO:0032024; P:positive regulation of insulin secretion; ISO:MGI.
DR GO; GO:0032868; P:response to insulin; IMP:MGI.
DR GO; GO:0032526; P:response to retinoic acid; ISO:MGI.
DR GO; GO:0060041; P:retina development in camera-type eye; IMP:MGI.
DR GO; GO:0042574; P:retinal metabolic process; IMP:MGI.
DR GO; GO:0042572; P:retinol metabolic process; IGI:MGI.
DR GO; GO:0034633; P:retinol transport; IMP:MGI.
DR GO; GO:0007283; P:spermatogenesis; IMP:MGI.
DR GO; GO:0060157; P:urinary bladder development; IMP:BHF-UCL.
DR GO; GO:0060065; P:uterus development; IMP:BHF-UCL.
DR GO; GO:0060068; P:vagina development; IMP:BHF-UCL.
DR GO; GO:0071939; P:vitamin A import into cell; IMP:MGI.
DR Gene3D; 2.40.128.20; -; 1.
DR InterPro; IPR012674; Calycin.
DR InterPro; IPR022271; Lipocalin_ApoD.
DR InterPro; IPR022272; Lipocalin_CS.
DR InterPro; IPR000566; Lipocln_cytosolic_FA-bd_dom.
DR InterPro; IPR002449; Retinol-bd/Purpurin.
DR PANTHER; PTHR11873; PTHR11873; 1.
DR Pfam; PF00061; Lipocalin; 1.
DR PIRSF; PIRSF036893; Lipocalin_ApoD; 1.
DR PIRSF; PIRSF500204; RBP_purpurin; 1.
DR PRINTS; PR01174; RETINOLBNDNG.
DR SUPFAM; SSF50814; SSF50814; 1.
DR PROSITE; PS00213; LIPOCALIN; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Methylation; Reference proteome; Retinol-binding; Secreted;
KW Signal; Transport; Vitamin A.
FT SIGNAL 1..18
FT /evidence="ECO:0000250|UniProtKB:P02753"
FT CHAIN 19..201
FT /note="Retinol-binding protein 4"
FT /id="PRO_0000017966"
FT BINDING 116
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P27485"
FT MOD_RES 139
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT DISULFID 22..178
FT /evidence="ECO:0000250|UniProtKB:P02753"
FT DISULFID 88..192
FT /evidence="ECO:0000250|UniProtKB:P02753"
FT DISULFID 138..147
FT /evidence="ECO:0000250|UniProtKB:P02753"
FT CONFLICT 17
FT /note="S -> T (in Ref. 5; AAA63395)"
FT /evidence="ECO:0000305"
FT CONFLICT 20
FT /note="R -> P (in Ref. 5; AAA63395)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 201 AA; 23206 MW; 8D187E293B37A75B CRC64;
MEWVWALVLL AALGGGSAER DCRVSSFRVK ENFDKARFSG LWYAIAKKDP EGLFLQDNII
AEFSVDEKGH MSATAKGRVR LLSNWEVCAD MVGTFTDTED PAKFKMKYWG VASFLQRGND
DHWIIDTDYD TFALQYSCRL QNLDGTCADS YSFVFSRDPN GLSPETRRLV RQRQEELCLE
RQYRWIEHNG YCQSRPSRNS L
