Retinol-binding protein 2 - Rattus norvegicus (Rat)

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P06768 (RET2_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 107. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

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

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 protein level

General annotation (Comments)

Function	Intracellular transport of retinol.
Subcellular location	Cytoplasm.
Domain	Forms a beta-barrel structure that accommodates hydrophobic ligands in its interior.
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	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	retinol metabolic process Traceable author statement Ref.1. Source: RGD
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	retinal binding Inferred from electronic annotation. Source: UniProtKB-KW retinol binding Traceable author statement Ref.1. Source: RGD 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

Removed Ref.3

Chain

2 – 134

133

Retinol-binding protein 2

PRO_0000067398

Sites

Binding site

Retinoic acid By similarity

Binding site

109

Retinoic acid

Secondary structure

134

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P06768 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 68491539A0115208
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FASTA

134

15,585

        10         20         30         40         50         60 
MTKDQNGTWE MESNENFEGY MKALDIDFAT RKIAVRLTQT KIIVQDGDNF KTKTNSTFRN 

        70         80         90        100        110        120 
YDLDFTVGVE FDEHTKGLDG RNVKTLVTWE GNTLVCVQKG EKENRGWKQW VEGDKLYLEL 

       130 
TCGDQVCRQV FKKK

« Hide

References

[1]	"The cellular retinol binding protein II gene. Sequence analysis of the rat gene, chromosomal localization in mice and humans, and documentation of its close linkage to the cellular retinol binding protein gene." Demmer L.A., Birkenmeier E.H., Sweetser D.A., Levin M.S., Zollman S., Sparkes R.S., Mohandas T., Lusis A.J., Gordon J.I. J. Biol. Chem. 262:2458-2467(1987) [PubMed: 3029082] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Rat cellular retinol-binding protein II: use of a cloned cDNA to define its primary structure, tissue-specific expression, and developmental regulation." Li E., Demmer L.A., Sweetser D.A., Ong D.E., Gordon J.I. Proc. Natl. Acad. Sci. U.S.A. 83:5779-5783(1986) [PubMed: 3461459] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Purification, primary structure characterization, and cellular distribution of two forms of cellular retinol-binding protein, type II from adult rat small intestine." Schaefer W.H., Kakkad B., Crow J.A., Blair I.A., Ong D.E. J. Biol. Chem. 264:4212-4221(1989) [PubMed: 2645288] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-134.
[4]	"Crystal structures of holo and apo-cellular retinol-binding protein II." Winter N.S., Bratt J.M., Banaszak L.J. J. Mol. Biol. 230:1247-1259(1993) [PubMed: 8487303] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH RETINOL.
[5]	"The structure and dynamics of rat apo-cellular retinol-binding protein II in solution: comparison with the X-ray structure." Lu J., Lin C.L., Tang C., Ponder J.W., Kao J.L., Cistola D.P., Li E. J. Mol. Biol. 286:1179-1195(1999) [PubMed: 10047490] [Abstract] Cited for: STRUCTURE BY NMR.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M13949 mRNA. Translation: AAA42022.1.
M16402, M16400, M16401 Genomic DNA. Translation: AAA40963.1. Sequence problems.

IPI

IPI00206644.

PIR

A29065. A92626.

RefSeq

NP_036772.2. NM_012640.2.

UniGene

Rn.9828.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1B4M	NMR	-	A	1-134	[»]
1EII	NMR	-	A	1-134	[»]
1OPA	X-ray	1.90	A/B	1-134	[»]
1OPB	X-ray	1.90	A/B/C/D	1-134	[»]

ProteinModelPortal

P06768.

SMR

P06768. Positions 1-134.

ModBase

Search...

Protein-protein interaction databases

STRING

P06768.

Proteomic databases

PRIDE

P06768.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSRNOT00000018755; ENSRNOP00000018755; ENSRNOG00000013932.

GeneID

24710.

KEGG

rno:24710.

UCSC

NM_012640. rat.

Organism-specific databases

CTD

5948.

RGD

3544. Rbp2.

Phylogenomic databases

eggNOG

roNOG16009.

GeneTree

ENSGT00560000076799.

HOVERGEN

HBG005633.

InParanoid

P06768.

OMA

WKQWVEG.

OrthoDB

EOG4WSWC0.

PhylomeDB

P06768.

Gene expression databases

ArrayExpress

P06768.

Genevestigator

P06768.

GermOnline

ENSRNOG00000013932. Rattus norvegicus.

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.

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

604193.

Entry information

Entry name

RET2_RAT

Accession

Primary (citable) accession number: P06768

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1988
Last sequence update:	January 23, 2007
Last modified:	November 16, 2011
This is version 107 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents