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UniProtKB/Swiss-Prot entry Q00724


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name RET4_MOUSE
Primary accession number Q00724
Secondary accession numbers P70357 Q566I5
Integrated into Swiss-Prot on April 1, 1993
Sequence was last modified on December 15, 1998 (Sequence version 2)
Annotations were last modified on    June 16, 2009 (Entry version 78)
Name and origin of the protein
Protein name Retinol-binding protein 4 [Precursor]
Synonyms Plasma retinol-binding protein
PRBP
RBP
Gene name
Name: Rbp4
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C57BL/6 X CBA;
DOI=10.1006/abbi.1998.0821; PubMed=9721191 [NCBI, ExPASy, EBI, Israel, Japan]
Jessen K.A., Satre M.A.;
"Induction of mouse retinol binding protein gene expression by cyclic AMP in Hepa 1-6 cells.";
Arch. Biochem. Biophys. 357:126-130(1998).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Maekawa K., Kojima T., Fujiyama A., Hattori M., Sakaki Y.;
"Genomic sequence of mouse retinol binding protein 4 region, complete sequence.";
Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J;
TISSUE=Stomach;
DOI=10.1126/science.1112014; PubMed=16141072 [NCBI, ExPASy, EBI, Israel, Japan]
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N;
TISSUE=Liver;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-179.
PubMed=1613076 [NCBI, ExPASy, EBI, Israel, Japan]
Dale B., Jones A.H., Presland R., Adler D.A., Disteche C.M.;
"Chromosomal localization of the retinol binding protein gene and its elimination as a candidate gene for the repeated epilation (Er) mutation in mice.";
J. Craniofac. Genet. Dev. Biol. 12:76-81(1992).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
U63146; AAB06955.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB124638; BAD16678.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK008765; BAB25881.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC031809; AAH31809.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC093529; AAH93529.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M74527; AAA63395.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00122429; -.
RefSeq NP_035385.1; -.
UniGene Mm.2605
3D structure databases
HSSP P27485; 1AQB. [HSSP ENTRY / PDB]
SMR Q00724; 19-192.
ModBase Q00724.
Organism-specific databases
MGI MGI:97879; Rbp4.
Gene expression databases
ArrayExpress Q00724; -.
Bgee Q00724; -.
CleanEx MM_RBP4; -.
GermOnline ENSMUSG00000024990; Mus musculus.
Ontologies
GO
GO:0005615; Cellular component: extracellular space (inferred from direct assay from UniProtKB).
GO:0016918; Molecular function: retinal binding (inferred from electronic annotation from UniProtKB-KW).
GO:0019841; Molecular function: retinol binding (inferred from direct assay from MGI).
GO:0034632; Molecular function: retinol transporter activity (inferred from mutant phenotype from MGI).
GO:0048738; Biological process: cardiac muscle tissue development (inferred from mutant phenotype from UniProtKB).
GO:0050908; Biological process: detection of light stimulus involved in visual perception (inferred from mutant phenotype from MGI).
GO:0048562; Biological process: embryonic organ morphogenesis (inferred from mutant phenotype from UniProtKB).
GO:0060059; Biological process: embryonic retina morphogenesis in camera-type eye (inferred from mutant phenotype from UniProtKB).
GO:0048706; Biological process: embryonic skeletal system development (inferred from mutant phenotype from UniProtKB).
GO:0048807; Biological process: female genitalia morphogenesis (inferred from mutant phenotype from UniProtKB).
GO:0006094; Biological process: gluconeogenesis (inferred from mutant phenotype from UniProtKB).
GO:0060347; Biological process: heart trabecula formation (inferred from mutant phenotype from UniProtKB).
GO:0030324; Biological process: lung development (inferred from mutant phenotype from UniProtKB).
GO:0008584; Biological process: male gonad development (inferred from mutant phenotype from MGI).
GO:0060044; Biological process: negative regulation of cardiac muscle cell proliferation (inferred from mutant phenotype from UniProtKB).
GO:0051024; Biological process: positive regulation of immunoglobulin secretion (inferred from direct assay from UniProtKB).
GO:0032868; Biological process: response to insulin stimulus (inferred from mutant phenotype from MGI).
GO:0042574; Biological process: retinal metabolic process (inferred from mutant phenotype from MGI).
GO:0042572; Biological process: retinol metabolic process (inferred from genetic interaction from MGI).
GO:0034633; Biological process: retinol transport (inferred from mutant phenotype from MGI).
GO:0007284; Biological process: spermatogonial cell division (inferred from mutant phenotype from MGI).
GO:0060157; Biological process: urinary bladder development (inferred from mutant phenotype from UniProtKB).
GO:0060065; Biological process: uterus development (inferred from mutant phenotype from UniProtKB).
GO:0060068; Biological process: vagina development (inferred from mutant phenotype from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR012674; Calycin.
IPR002345; Lipocalin.
IPR000566; Lipocln_cytFABP.
IPR002449; Retinol_bd.
Graphical view of domain structure.
Gene3D G3DSA:2.40.128.20; Calycin; 1.
PANTHER PTHR11873; Retinol_bd; 1.
Pfam PF00061; Lipocalin; 1.
Pfam graphical view of domain structure.
PRINTS PR00179; LIPOCALIN.
PR01174; RETINOLBNDNG.
PROSITE PS00213; LIPOCALIN; 1.
Genome annotation databases
Ensembl ENSMUSG00000024990; Mus musculus. [Contig view]
GeneID 19662; -.
KEGG mmu:19662; -.
Phylogenomic databases
HOGENOM Q00724; -.
HOVERGEN Q00724; -.
OMA Q00724; MEWVWAL.
Other
NextBio 296954; -.
SOURCE Rbp4; Mus musculus.
ProtoNet Q00724.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Disulfide bond; Retinol-binding; Secreted; Signal; Transport; Vitamin A.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
SIGNAL   1    18  18     By similarity. 
CHAIN   19   201  183     Retinol-binding protein 4. PRO_0000017966
DISULFID   22   178        By similarity. 
DISULFID   88   192        By similarity. 
DISULFID   138   147        By similarity. 
CONFLICT   17    17        S -> T (in Ref. 5; AAA63395). 
CONFLICT   20    20        R -> P (in Ref. 5; AAA63395). 
Sequence information
Length: 201 AA [This is the length of the unprocessed precursor] Molecular weight: 23206 Da [This is the MW of the unprocessed precursor] CRC64: 8D187E293B37A75B [This is a checksum on the sequence]
        10         20         30         40         50         60 
MEWVWALVLL AALGGGSAER DCRVSSFRVK ENFDKARFSG LWYAIAKKDP EGLFLQDNII 

        70         80         90        100        110        120 
AEFSVDEKGH MSATAKGRVR LLSNWEVCAD MVGTFTDTED PAKFKMKYWG VASFLQRGND 

       130        140        150        160        170        180 
DHWIIDTDYD TFALQYSCRL QNLDGTCADS YSFVFSRDPN GLSPETRRLV RQRQEELCLE 

       190        200 
RQYRWIEHNG YCQSRPSRNS L 

Q00724 in FASTA format

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