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Q08652

- RET2_MOUSE

UniProt

Q08652 - RET2_MOUSE

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Protein
Retinol-binding protein 2
Gene
Rbp2, Crbpii
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at transcript leveli

Functioni

Intracellular transport of retinol.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei41 – 411Retinoic acid By similarity
Binding sitei109 – 1091Retinoic acid By similarity

GO - Molecular functioni

  1. retinal binding Source: UniProtKB-KW
  2. retinoid binding Source: MGI
  3. retinol binding Source: UniProtKB-KW
  4. transporter activity Source: InterPro
Complete GO annotation...

GO - Biological processi

  1. retinoid metabolic process Source: MGI
Complete GO annotation...

Keywords - Biological processi

Transport

Keywords - Ligandi

Retinol-binding, Vitamin A

Enzyme and pathway databases

ReactomeiREACT_198569. Retinoid metabolism and transport.

Names & Taxonomyi

Protein namesi
Recommended name:
Retinol-binding protein 2
Alternative name(s):
Cellular retinol-binding protein II
Short name:
CRBP-II
Gene namesi
Name:Rbp2
Synonyms:Crbpii
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 9

Organism-specific databases

MGIiMGI:97877. Rbp2.

Subcellular locationi

GO - Cellular componenti

  1. Golgi apparatus Source: Ensembl
  2. cytosol Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 134133Retinol-binding protein 2
PRO_0000067396Add
BLAST

Proteomic databases

MaxQBiQ08652.
PRIDEiQ08652.

PTM databases

PhosphoSiteiQ08652.

Expressioni

Tissue specificityi

Expressed in prenatal liver, intestine and lung, and in adult intestine.

Gene expression databases

ArrayExpressiQ08652.
BgeeiQ08652.
CleanExiMM_RBP2.
GenevestigatoriQ08652.

Structurei

3D structure databases

ProteinModelPortaliQ08652.
SMRiQ08652. Positions 1-134.

Family & Domainsi

Domaini

Forms a beta-barrel structure that accommodates hydrophobic ligands in its interior By similarity.

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG284832.
GeneTreeiENSGT00750000117564.
HOGENOMiHOG000004831.
HOVERGENiHBG005633.
InParanoidiQ08652.
KOiK14622.
OMAiQTKIIDQ.
OrthoDBiEOG7NW6BZ.
PhylomeDBiQ08652.
TreeFamiTF316894.

Family and domain databases

Gene3Di2.40.128.20. 1 hit.
InterProiIPR012674. Calycin.
IPR011038. Calycin-like.
IPR000463. Fatty_acid-bd.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
[Graphical view]
PfamiPF00061. Lipocalin. 1 hit.
[Graphical view]
PRINTSiPR00178. FATTYACIDBP.
SUPFAMiSSF50814. SSF50814. 1 hit.
PROSITEiPS00214. FABP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q08652-1 [UniParc]FASTAAdd to Basket

« Hide

MTKDQNGTWE MESNENFEGY MKALDIDFAT RKIAVRLTQT KIITQDGDNF    50
KTKTNSTFRN YDLDFTVGVE FDEHTKGLDG RHVKTLVTWE GNTLVCVQKG 100
EKENRGWKQW VEGDKLYLEL TCGDQVCRQV FKKK 134
Length:134
Mass (Da):15,610
Last modified:January 23, 2007 - v2
Checksum:i6B29171BA6A7AB63
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti98 – 981Q → H in BAB22708. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X74154 mRNA. Translation: CAA52268.1.
AK003312 mRNA. Translation: BAB22708.1.
CCDSiCCDS23425.1.
PIRiI48311. S34717.
RefSeqiNP_033060.3. NM_009034.4.
UniGeneiMm.12825.

Genome annotation databases

EnsembliENSMUST00000035029; ENSMUSP00000035029; ENSMUSG00000032454.
GeneIDi19660.
KEGGimmu:19660.
UCSCiuc009rdk.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X74154 mRNA. Translation: CAA52268.1 .
AK003312 mRNA. Translation: BAB22708.1 .
CCDSi CCDS23425.1.
PIRi I48311. S34717.
RefSeqi NP_033060.3. NM_009034.4.
UniGenei Mm.12825.

3D structure databases

ProteinModelPortali Q08652.
SMRi Q08652. Positions 1-134.
ModBasei Search...

PTM databases

PhosphoSitei Q08652.

Proteomic databases

MaxQBi Q08652.
PRIDEi Q08652.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000035029 ; ENSMUSP00000035029 ; ENSMUSG00000032454 .
GeneIDi 19660.
KEGGi mmu:19660.
UCSCi uc009rdk.2. mouse.

Organism-specific databases

CTDi 5948.
MGIi MGI:97877. Rbp2.

Phylogenomic databases

eggNOGi NOG284832.
GeneTreei ENSGT00750000117564.
HOGENOMi HOG000004831.
HOVERGENi HBG005633.
InParanoidi Q08652.
KOi K14622.
OMAi QTKIIDQ.
OrthoDBi EOG7NW6BZ.
PhylomeDBi Q08652.
TreeFami TF316894.

Enzyme and pathway databases

Reactomei REACT_198569. Retinoid metabolism and transport.

Miscellaneous databases

NextBioi 296946.
PROi Q08652.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q08652.
Bgeei Q08652.
CleanExi MM_RBP2.
Genevestigatori Q08652.

Family and domain databases

Gene3Di 2.40.128.20. 1 hit.
InterProi IPR012674. Calycin.
IPR011038. Calycin-like.
IPR000463. Fatty_acid-bd.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
[Graphical view ]
Pfami PF00061. Lipocalin. 1 hit.
[Graphical view ]
PRINTSi PR00178. FATTYACIDBP.
SUPFAMi SSF50814. SSF50814. 1 hit.
PROSITEi PS00214. FABP. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Embryo.

Entry informationi

Entry nameiRET2_MOUSE
AccessioniPrimary (citable) accession number: Q08652
Secondary accession number(s): Q9D1N1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 114 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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