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Protein

Cellular retinoic acid-binding protein 2

Gene

Crabp2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Transports retinoic acid to the nucleus. Regulates the access of retinoic acid to the nuclear retinoic acid receptors (By similarity).By similarity

GO - Molecular functioni

  • lipid binding Source: RGD
  • retinal binding Source: UniProtKB-KW
  • retinoic acid binding Source: RGD
  • retinol binding Source: UniProtKB-KW
  • transporter activity Source: InterPro

GO - Biological processi

  • lipid transport Source: RGD
  • regulation of retinoic acid receptor signaling pathway Source: InterPro
  • retinoic acid biosynthetic process Source: RGD
  • retinoic acid metabolic process Source: RGD
Complete GO annotation...

Keywords - Biological processi

Transport

Keywords - Ligandi

Retinol-binding, Vitamin A

Enzyme and pathway databases

ReactomeiR-RNO-5362517. Signaling by Retinoic Acid.

Names & Taxonomyi

Protein namesi
Recommended name:
Cellular retinoic acid-binding protein 2
Alternative name(s):
Cellular retinoic acid-binding protein II
Short name:
CRABP-II
Gene namesi
Name:Crabp2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 2

Organism-specific databases

RGDi62070. Crabp2.

Subcellular locationi

  • Cytoplasm
  • Endoplasmic reticulum By similarity
  • Nucleus By similarity

  • Note: Upon ligand binding, a conformation change exposes a nuclear localization motif and the protein is transported into the nucleus.By similarity

GO - Cellular componenti

  • cytoplasm Source: RGD
  • cytosol Source: RGD
  • endoplasmic reticulum Source: UniProtKB-SubCell
  • nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Nucleus

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL4345.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000674171 – 139Cellular retinoic acid-binding protein 2Add BLAST139

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki103Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity

Post-translational modificationi

Sumoylated in response to retinoic acid binding, sumoylation is critical for dissociation from ER and subsequent nuclear translocation.

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Proteomic databases

PaxDbiP51673.
PRIDEiP51673.

PTM databases

PhosphoSitePlusiP51673.

Expressioni

Gene expression databases

BgeeiENSRNOG00000022101.
GenevisibleiP51673. RN.

Interactioni

Subunit structurei

Interacts with importin alpha, RXR and RARA.By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000015134.

Structurei

3D structure databases

ProteinModelPortaliP51673.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni134 – 136Retinoic acid bindingBy similarity3

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi21 – 31Nuclear localization signalBy similarityAdd BLAST11

Domaini

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG4015. Eukaryota.
ENOG4111US8. LUCA.
GeneTreeiENSGT00760000118898.
HOGENOMiHOG000004831.
HOVERGENiHBG005633.
InParanoidiP51673.
KOiK17289.
OMAiFPKWETD.
OrthoDBiEOG091G0QSV.
PhylomeDBiP51673.
TreeFamiTF316894.

Family and domain databases

Gene3Di2.40.128.20. 1 hit.
InterProiIPR012674. Calycin.
IPR011038. Calycin-like.
IPR031281. CRABP2.
IPR000463. Fatty_acid-bd.
IPR031259. iLBP.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
[Graphical view]
PANTHERiPTHR11955. PTHR11955. 1 hit.
PTHR11955:SF60. PTHR11955:SF60. 1 hit.
PfamiPF00061. Lipocalin. 1 hit.
[Graphical view]
PRINTSiPR00178. FATTYACIDBP.
SUPFAMiSSF50814. SSF50814. 1 hit.
PROSITEiPS00214. FABP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P51673-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPNFSGNWKI IRSENFEEML KALGVNMMMR KIAVAAASKP AVEIKQENDD
60 70 80 90 100
TFYIKTSTTV RTTEINFKIG EEFEEQTVDG RPCKSLVKWE SENKMVCEQR
110 120 130
LLKGEGPKTS WSRELTNDGE LILTMTADDV VCTRVYVRE
Length:139
Mass (Da):15,933
Last modified:January 23, 2007 - v2
Checksum:iC32B812D6DC57841
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U23407 mRNA. Translation: AAA80225.1.
PIRiI53298.
RefSeqiNP_058940.1. NM_017244.1.
UniGeneiRn.11333.

Genome annotation databases

EnsembliENSRNOT00000025183; ENSRNOP00000015134; ENSRNOG00000022101.
GeneIDi29563.
KEGGirno:100911902.
rno:29563.
UCSCiRGD:62070. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U23407 mRNA. Translation: AAA80225.1.
PIRiI53298.
RefSeqiNP_058940.1. NM_017244.1.
UniGeneiRn.11333.

3D structure databases

ProteinModelPortaliP51673.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000015134.

Chemistry databases

ChEMBLiCHEMBL4345.

PTM databases

PhosphoSitePlusiP51673.

Proteomic databases

PaxDbiP51673.
PRIDEiP51673.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000025183; ENSRNOP00000015134; ENSRNOG00000022101.
GeneIDi29563.
KEGGirno:100911902.
rno:29563.
UCSCiRGD:62070. rat.

Organism-specific databases

CTDi1382.
RGDi62070. Crabp2.

Phylogenomic databases

eggNOGiKOG4015. Eukaryota.
ENOG4111US8. LUCA.
GeneTreeiENSGT00760000118898.
HOGENOMiHOG000004831.
HOVERGENiHBG005633.
InParanoidiP51673.
KOiK17289.
OMAiFPKWETD.
OrthoDBiEOG091G0QSV.
PhylomeDBiP51673.
TreeFamiTF316894.

Enzyme and pathway databases

ReactomeiR-RNO-5362517. Signaling by Retinoic Acid.

Miscellaneous databases

PROiP51673.

Gene expression databases

BgeeiENSRNOG00000022101.
GenevisibleiP51673. RN.

Family and domain databases

Gene3Di2.40.128.20. 1 hit.
InterProiIPR012674. Calycin.
IPR011038. Calycin-like.
IPR031281. CRABP2.
IPR000463. Fatty_acid-bd.
IPR031259. iLBP.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
[Graphical view]
PANTHERiPTHR11955. PTHR11955. 1 hit.
PTHR11955:SF60. PTHR11955:SF60. 1 hit.
PfamiPF00061. Lipocalin. 1 hit.
[Graphical view]
PRINTSiPR00178. FATTYACIDBP.
SUPFAMiSSF50814. SSF50814. 1 hit.
PROSITEiPS00214. FABP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRABP2_RAT
AccessioniPrimary (citable) accession number: P51673
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: November 30, 2016
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. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.