Q08652 (RET2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Retinol-binding protein 2

Alternative name(s):
Cellular retinol-binding protein II
Short name=CRBP-II

Gene names

Name:	Rbp2
Synonyms:	Crbpii

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 › Mus

Protein attributes

Sequence length	134 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	Intracellular transport of retinol.
Subcellular location	Cytoplasm.
Tissue specificity	Expressed in prenatal liver, intestine and lung, and in adult intestine.
Domain	Forms a beta-barrel structure that accommodates hydrophobic ligands in its interior By similarity.
Sequence similarities	Belongs to the calycin superfamily. Fatty-acid binding protein (FABP) family.

Ontologies

Keywords
Biological process	Transport
Cellular component	Cytoplasm
Ligand	Retinol-binding Vitamin A
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	retinoid metabolic process Traceable author statement. Source: MGI
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
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
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 134	133	Retinol-binding protein 2		PRO_0000067396
Sites
	Binding site	41	1	Retinoic acid By similarity
	Binding site	109	1	Retinoic acid By similarity
Experimental info
	Sequence conflict	98	1	Q → H in BAB22708. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q08652 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 6B29171BA6A7AB63	FASTA	134	15,610
	10 20 30 40 50 60 MTKDQNGTWE MESNENFEGY MKALDIDFAT RKIAVRLTQT KIITQDGDNF KTKTNSTFRN 70 80 90 100 110 120 YDLDFTVGVE FDEHTKGLDG RHVKTLVTWE GNTLVCVQKG EKENRGWKQW VEGDKLYLEL 130 TCGDQVCRQV FKKK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The directly repeated RG(G/T)TCA motifs of the rat and mouse cellular retinol-binding protein II genes are promiscuous binding sites for RAR, RXR, HNF-4, and ARP-1 homo- and heterodimers." Nakshatri H., Chambon P. J. Biol. Chem. 269:890-902(1994) [PubMed: 8288643] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Intestine.
[2]	"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: Embryo.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X74154 mRNA. Translation: CAA52268.1. AK003312 mRNA. Translation: BAB22708.1.
IPI	IPI00222362.
PIR	S34717. I48311.
RefSeq	NP_033060.3. NM_009034.4.
UniGene	Mm.12825.
3D structure databases
ProteinModelPortal	Q08652.
SMR	Q08652. Positions 1-134.
ModBase	Search...
Protein-protein interaction databases
STRING	Q08652.
Proteomic databases
PRIDE	Q08652.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000035029; ENSMUSP00000035029; ENSMUSG00000032454.
GeneID	19660.
KEGG	mmu:19660.
Organism-specific databases
CTD	5948.
MGI	MGI:97877. Rbp2.
Phylogenomic databases
GeneTree	ENSGT00560000076799.
HOGENOM	HBG714759.
HOVERGEN	HBG005633.
InParanoid	Q08652.
OMA	WKQWVEG.
OrthoDB	EOG4WSWC0.
PhylomeDB	Q08652.
Gene expression databases
ArrayExpress	Q08652.
Bgee	Q08652.
CleanEx	MM_RBP2.
Genevestigator	Q08652.
GermOnline	ENSMUSG00000032454. Mus musculus.
Family and domain databases
InterPro	IPR012674. Calycin. IPR011038. Calycin-like. IPR000463. Fatty_acid-bd. IPR000566. Lipocln_cytosolic_FA-bd_dom. [Graphical view]
Gene3D	G3DSA:2.40.128.20. Calycin. 1 hit.
KO	K14622.
Pfam	PF00061. Lipocalin. 1 hit. [Graphical view]
PRINTS	PR00178. FATTYACIDBP.
SUPFAM	SSF50814. Calycin. 1 hit.
PROSITE	PS00214. FABP. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	296946.
SOURCE	Search...

Entry information

Entry name

RET2_MOUSE

Accession

Primary (citable) accession number: Q08652
Secondary accession number(s): Q9D1N1

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	January 23, 2007
Last modified:	November 16, 2011
This is version 96 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program