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Reviewed, UniProtKB/Swiss-Prot Q00724 (RET4_MOUSE)

Last modified June 16, 2009. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Retinol-binding protein 4
Alternative name(s):
    Plasma retinol-binding protein
      Short name=PRBP
      Short name=RBP
Gene names
Name: Rbp4
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length201 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

Delivers retinol from the liver stores to the peripheral tissues. In plasma, the RBP-retinol complex interacts with transthyretin, this prevents its loss by filtration through the kidney glomeruli.

Subcellular location

Secreted.

Sequence similarities

Belongs to the calycin superfamily. Lipocalin family.

Ontologies

Keywords
   Biological processTransport
   Cellular componentSecreted
   DomainSignal
   LigandRetinol-binding
Vitamin A
   PTMDisulfide bond
Gene Ontology (GO)
   Biological processcardiac muscle tissue development

Inferred from mutant phenotype. Source: UniProtKB

detection of light stimulus involved in visual perception

Inferred from mutant phenotype. Source: MGI

embryonic organ morphogenesis

Inferred from mutant phenotype. Source: UniProtKB

embryonic retina morphogenesis in camera-type eye

Inferred from mutant phenotype. Source: UniProtKB

embryonic skeletal system development

Inferred from mutant phenotype. Source: UniProtKB

female genitalia morphogenesis

Inferred from mutant phenotype. Source: UniProtKB

gluconeogenesis

Inferred from mutant phenotype. Source: UniProtKB

heart trabecula formation

Inferred from mutant phenotype. Source: UniProtKB

lung development

Inferred from mutant phenotype. Source: UniProtKB

male gonad development

Inferred from mutant phenotype. Source: MGI

negative regulation of cardiac muscle cell proliferation

Inferred from mutant phenotype. Source: UniProtKB

positive regulation of immunoglobulin secretion

Inferred from direct assay. Source: UniProtKB

response to insulin stimulus

Inferred from mutant phenotype. Source: MGI

retinal metabolic process

Inferred from mutant phenotype. Source: MGI

retinol metabolic process

Inferred from genetic interaction. Source: MGI

retinol transport

Inferred from mutant phenotype. Source: MGI

spermatogonial cell division

Inferred from mutant phenotype. Source: MGI

urinary bladder development

Inferred from mutant phenotype. Source: UniProtKB

uterus development

Inferred from mutant phenotype. Source: UniProtKB

vagina development

Inferred from mutant phenotype. Source: UniProtKB

   Cellular componentextracellular space

Inferred from direct assay. Source: UniProtKB

   Molecular functionretinal binding

Inferred from electronic annotation. Source: UniProtKB-KW

retinol binding

Inferred from direct assay. Source: MGI

retinol transporter activity

Inferred from mutant phenotype. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 By similarity
Chain19 – 201183Retinol-binding protein 4
PRO_0000017966

Amino acid modifications

Disulfide bond22 ↔ 178 By similarity
Disulfide bond88 ↔ 192 By similarity
Disulfide bond138 ↔ 147 By similarity

Experimental info

Sequence conflict171S → T in AAA63395. Ref.5
Sequence conflict201R → P in AAA63395. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Q00724-1 [UniParc].

Last modified December 15, 1998. Version 2.
Checksum: 8D187E293B37A75B

FASTA20123,206
        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 

« Hide

References

« Hide 'large scale' references
[1]"Induction of mouse retinol binding protein gene expression by cyclic AMP in Hepa 1-6 cells."
Jessen K.A., Satre M.A.
Arch. Biochem. Biophys. 357:126-130(1998) [PubMed: 9721191] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C57BL/6 X CBA.
[2]"Genomic sequence of mouse retinol binding protein 4 region, complete sequence."
Maekawa K., Kojima T., Fujiyama A., Hattori M., Sakaki Y.
Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"The transcriptional landscape of the mammalian genome."
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. expand/collapse author list , 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.
Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Stomach.
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Liver.
[5]"Chromosomal localization of the retinol binding protein gene and its elimination as a candidate gene for the repeated epilation (Er) mutation in mice."
Dale B., Jones A.H., Presland R., Adler D.A., Disteche C.M.
J. Craniofac. Genet. Dev. Biol. 12:76-81(1992) [PubMed: 1613076] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-179.
+Additional computationally mapped references.

Cross-references

Sequence databases

U63146 mRNA. Translation: AAB06955.1.
AB124638 Genomic DNA. Translation: BAD16678.1.
AK008765 mRNA. Translation: BAB25881.1.
BC031809 mRNA. Translation: AAH31809.1.
BC093529 mRNA. Translation: AAH93529.1.
M74527 mRNA. Translation: AAA63395.1.
IPIIPI00122429.
RefSeqNP_035385.1.
UniGeneMm.2605

3D structure databases

HSSPHSSP built from PDB template 1AQB based on UniProtKB P27485.
SMRQ00724. Positions 19-192.
ModBaseSearch...

Genome annotation databases

EnsemblENSMUSG00000024990. Mus musculus. [Contig view]
GeneID19662.
KEGGmmu:19662.

Organism-specific databases

MGIMGI:97879. Rbp4.

Phylogenomic databases

HOGENOMQ00724.
HOVERGENQ00724.
OMAQ00724. MEWVWAL.

Gene expression databases

ArrayExpressQ00724.
BgeeQ00724.
CleanExMM_RBP4.
GermOnlineENSMUSG00000024990. Mus musculus.

Family and domain databases

InterProIPR012674. Calycin.
IPR002345. Lipocalin.
IPR000566. Lipocln_cytFABP.
IPR002449. Retinol_bd.
[Graphical view]
Gene3DG3DSA:2.40.128.20. Calycin. 1 hit.
PANTHERPTHR11873. Retinol_bd. 1 hit.
PfamPF00061. Lipocalin. 1 hit.
[Graphical view]
PRINTSPR00179. LIPOCALIN.
PR01174. RETINOLBNDNG.
PROSITEPS00213. LIPOCALIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio296954.
SOURCESearch...

Entry information

Entry nameRET4_MOUSE
AccessionPrimary (citable) accession number: Q00724
Secondary accession number(s): P70357, Q566I5
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: December 15, 1998
Last modified: June 16, 2009
This is version 78 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents