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   21-SEP-2011, entry version 100.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6 X CBA;
RX   MEDLINE=98389586; 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
RT   AMP 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.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   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.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-179.
RX   MEDLINE=92308333; 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)
RT   mutation in mice.";
RL   J. Craniofac. Genet. Dev. Biol. 12:76-81(1992).
CC   -!- FUNCTION: Delivers retinol from the liver stores to the peripheral
CC       tissues. In plasma, the RBP-retinol complex interacts with
CC       transthyretin, this prevents its loss by filtration through the
CC       kidney glomeruli.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.
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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   IPI; IPI00122429; -.
DR   RefSeq; NP_001152959.1; NM_001159487.1.
DR   RefSeq; NP_035385.1; NM_011255.3.
DR   UniGene; Mm.2605; -.
DR   ProteinModelPortal; Q00724; -.
DR   SMR; Q00724; 19-192.
DR   STRING; Q00724; -.
DR   PRIDE; Q00724; -.
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   HOGENOM; HBG715497; -.
DR   HOVERGEN; HBG004493; -.
DR   InParanoid; Q00724; -.
DR   OMA; MEWVWAL; -.
DR   OrthoDB; EOG4T4CWM; -.
DR   PhylomeDB; Q00724; -.
DR   NextBio; 296954; -.
DR   ArrayExpress; Q00724; -.
DR   Bgee; Q00724; -.
DR   CleanEx; MM_RBP4; -.
DR   Genevestigator; Q00724; -.
DR   GermOnline; ENSMUSG00000024990; Mus musculus.
DR   GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
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 transporter activity; IMP:MGI.
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:0048807; P:female genitalia morphogenesis; IMP:BHF-UCL.
DR   GO; GO:0006094; P:gluconeogenesis; 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: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:0051024; P:positive regulation of immunoglobulin secretion; IDA:BHF-UCL.
DR   GO; GO:0032868; P:response to insulin stimulus; 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: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   InterPro; IPR012674; Calycin.
DR   InterPro; IPR011038; Calycin-like.
DR   InterPro; IPR002345; Lipocalin.
DR   InterPro; IPR022271; Lipocalin_ApoD.
DR   InterPro; IPR022272; Lipocalin_CS.
DR   InterPro; IPR000566; Lipocln_cytosolic_FA-bd_dom.
DR   InterPro; IPR002449; Retinol-bd.
DR   Gene3D; G3DSA:2.40.128.20; Calycin; 1.
DR   PANTHER; PTHR11873; Retinol_bd; 1.
DR   Pfam; PF00061; Lipocalin; 1.
DR   PIRSF; PIRSF036893; Lipocalin_ApoD; 1.
DR   PRINTS; PR00179; LIPOCALIN.
DR   PRINTS; PR01174; RETINOLBNDNG.
DR   SUPFAM; SSF50814; Calycin; 1.
DR   PROSITE; PS00213; LIPOCALIN; 1.
PE   2: Evidence at transcript level;
KW   Complete proteome; Disulfide bond; Reference proteome;
KW   Retinol-binding; Secreted; Signal; Transport; Vitamin A.
FT   SIGNAL        1     18       By similarity.
FT   CHAIN        19    201       Retinol-binding protein 4.
FT                                /FTId=PRO_0000017966.
FT   DISULFID     22    178       By similarity.
FT   DISULFID     88    192       By similarity.
FT   DISULFID    138    147       By similarity.
FT   CONFLICT     17     17       S -> T (in Ref. 5; AAA63395).
FT   CONFLICT     20     20       R -> P (in Ref. 5; AAA63395).
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
//