Reviewed, UniProtKB/Swiss-Prot Q00724 (RET4_MOUSE)

Names and origin

Protein names

Recommended name:
    Retinol-binding protein 4
Alternative name(s):
    Plasma retinol-binding protein
      Short name=PRBP
      Short name=RBP

Gene names

Name:

Rbp4

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	201 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 process	Transport
Cellular component	Secreted
Domain	Signal
Ligand	Retinol-binding Vitamin A
Gene Ontology (GO)
Biological process	cardiac muscle development Inferred from mutant phenotype. Source: UniProtKB 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 lung development Inferred from mutant phenotype. Source: UniProtKB negative regulation of cardiac muscle cell proliferation Inferred from mutant phenotype. Source: UniProtKB positive regulation of immunoglobulin secretion Inferred from direct assay. Source: UniProtKB 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 component	extracellular space Inferred from direct assay. Source: UniProtKB
Molecular function	retinal binding Inferred from electronic annotation. Source: UniProtKB-KW retinol binding Inferred from electronic annotation. Source: UniProtKB-KW transporter activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 18	18	By similarity
	Chain	19 – 201	183	Retinol-binding protein 4		PRO_0000017966
Amino acid modifications
	Disulfide bond	22 ↔ 178		By similarity
	Disulfide bond	88 ↔ 192		By similarity
	Disulfide bond	138 ↔ 147		By similarity
Experimental info
	Sequence conflict	17	1	S → T in AAA63395. Ref.5
	Sequence conflict	20	1	R → P in AAA63395. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Q00724-1 [UniParc]. Last modified December 15, 1998. Version 2. Checksum: 8D187E293B37A75B	FASTA	201	23,206
	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

References

	« Hide 'large scale' referencesShow '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. , 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
EMBLGenBankDDBJ	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.
RefSeq	NP_035385.1.
UniGene	Mm.2605
3D structure databases
HSSP	HSSP built from PDB template 1AQB based on UniProtKB P27485.
SMR	Q00724. Positions 19-192.
ModBase	Search...
Genome annotation databases
Ensembl	ENSMUSG00000024990. Mus musculus. [Contig view]
GeneID	19662.
KEGG	mmu:19662.
Organism-specific databases
MGI	MGI:97879. Rbp4.
Phylogenomic databases
HOGENOM	Q00724.
HOVERGEN	Q00724.
Gene expression databases
ArrayExpress	Q00724.
CleanEx	MM_RBP4.
GermOnline	ENSMUSG00000024990. Mus musculus.
Family and domain databases
InterPro	IPR012674. Calycin. IPR002345. Lipocalin. IPR000566. Lipocln_cytFABP. IPR002449. Retinol_bd. [Graphical view]
Gene3D	G3DSA:2.40.128.20. Calycin. 1 hit.
PANTHER	PTHR11873. Retinol_bd. 1 hit.
Pfam	PF00061. Lipocalin. 1 hit. [Graphical view]
PRINTS	PR00179. LIPOCALIN. PR01174. RETINOLBNDNG.
PROSITE	PS00213. LIPOCALIN. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	296954.
SOURCE	Search...

Entry information

Entry name

RET4_MOUSE

Accession

Primary (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:	November 25, 2008
This is version 73 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)