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Reviewed, UniProtKB/Swiss-Prot P02696 (RET1_RAT)

Last modified March 2, 2010. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
Retinol-binding protein 1
Alternative name(s):
Cellular retinol-binding protein I
Short name=CRBP-I
Cellular retinol-binding protein
Short name=CRBP
Gene names
Name:Rbp1
Synonyms:Rbp-1
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

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Protein attributes

Sequence length135 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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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.

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Ontologies

Keywords
   Biological processTransport
   Cellular componentCytoplasm
   LigandRetinol-binding
Vitamin A
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological processtransport

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionretinal 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...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.3 Ref.4 Ref.5
Chain2 – 135134Retinol-binding protein 1
PRO_0000067394

Sites

Binding site1091Retinoic acid

Secondary structure

1 ........................... 135
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P02696-1 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 680CCE3284BD28B7

FASTA13515,834
        10         20         30         40         50         60 
MPVDFNGYWK MLSNENFEEY LRALDVNVAL RKIANLLKPD KEIVQDGDHM IIRTLSTFRN 

        70         80         90        100        110        120 
YIMDFQVGKE FEEDLTGIDD RKCMTTVSWD GDKLQCVQKG EKEGRGWTQW IEGDELHLEM 

       130 
RAEGVTCKQV FKKVH

« Hide

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References

[1]"Rat cellular retinol-binding protein: cDNA sequence and rapid retinol-dependent accumulation of mRNA."
Sherman D.R., Lloyd R.S., Chytil F.
Proc. Natl. Acad. Sci. U.S.A. 84:3209-3213(1987) [PubMed: 3472205] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Comparison of the tissue-specific expression and developmental regulation of two closely linked rodent genes encoding cytosolic retinol-binding proteins."
Levin M.S., Li E., Ong D.E., Gordon J.I.
J. Biol. Chem. 262:7118-7124(1987) [PubMed: 3584109] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"The primary structure of rat liver cellular retinol-binding protein."
Sundelin J., Anundi H., Traegaardh L., Eriksson U., Lind P., Ronne H., Peterson P.A., Rask L.
J. Biol. Chem. 260:6488-6493(1985) [PubMed: 4039728] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-135.
Tissue: Liver.
[4]"Cellular retinol-binding protein. Quantitation and distribution."
Eriksson U., Das K., Busch C., Nordlinder H., Rask L., Sundelin J., Sallstrom J., Peterson P.A.
J. Biol. Chem. 259:13464-13470(1984) [PubMed: 6541654] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-51.
Tissue: Testis.
[5]"Structural and functional studies of vitamin A-binding proteins."
Rask L., Anundi H., Boehme J., Eriksson U., Ronne H., Sege K., Peterson P.A.
Ann. N. Y. Acad. Sci. 359:79-90(1981) [PubMed: 6942701] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-35.
Tissue: Liver.
[6]"Crystallographic studies on a family of cellular lipophilic transport proteins. Refinement of P2 myelin protein and the structure determination and refinement of cellular retinol-binding protein in complex with all-trans-retinol."
Cowan S.W., Newcomer M.E., Jones T.A.
J. Mol. Biol. 230:1225-1246(1993) [PubMed: 7683727] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH ALL-TRANS-RETINOL.
+Additional computationally mapped references.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M16459 mRNA. Translation: AAA42021.1.
M19257 mRNA. Translation: AAA40962.1.
IPIIPI00231825.
PIRRJRTO. A29570.
RefSeqNP_036865.1.
UniGeneRn.902

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1CRBX-ray2.10A2-135[»]
1JBHNMR-A1-135[»]
1KGLNMR-A1-135[»]
1MX7NMR-A2-135[»]
1MX8NMR-A2-135[»]
ModBaseSearch...

Protein-protein interaction databases

STRINGP02696.

Proteomic databases

PRIDEP02696.

Genome annotation databases

EnsemblENSRNOT00000018622; ENSRNOP00000018622; ENSRNOG00000013794; Rattus norvegicus. [Genome view]
GeneID25056.
KEGGrno:25056.
UCSCNM_012733. rat.

Organism-specific databases

CTD25056.
RGD3543. Rbp1.

Phylogenomic databases

eggNOGroNOG11637.
HOVERGENHBG005633.
InParanoidP02696.
OMAGVICKQV.
OrthoDBEOG9MSGHP.
PhylomeDBP02696.

Gene expression databases

ArrayExpressP02696.
GenevestigatorP02696.
GermOnlineENSRNOG00000013794. Rattus norvegicus.

Family and domain databases

InterProIPR012674. Calycin.
IPR011038. Calycin-like.
IPR000463. Fatty_acid_bd.
IPR000566. Lipocln_cytosolic_FA_bd.
[Graphical view]
Gene3DG3DSA:2.40.128.20. Calycin. 1 hit.
PANTHERPTHR11955. Fatty_acid_bd. 1 hit.
PfamPF00061. Lipocalin. 1 hit.
[Graphical view]
PRINTSPR00178. FATTYACIDBP.
SUPFAMSSF50814. Calycin. 1 hit.
PROSITEPS00214. FABP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio605266.

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Entry information

Entry nameRET1_RAT
AccessionPrimary (citable) accession number: P02696
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: March 2, 2010
This is version 95 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents