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Protein

Retinol-binding protein 1

Gene

Rbp1

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

Functioni

Intracellular transport of retinol.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei109 – 1091Retinoic acid

GO - Molecular functioni

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

GO - Biological processi

  • regulation of granulocyte differentiation Source: Ensembl
  • response to vitamin A Source: Ensembl
  • retinoic acid biosynthetic process Source: RGD
  • retinol metabolic process Source: RGD
  • vitamin A metabolic process Source: InterPro
Complete GO annotation...

Keywords - Biological processi

Transport

Keywords - Ligandi

Retinol-binding, Vitamin A

Enzyme and pathway databases

ReactomeiR-RNO-2453902. The canonical retinoid cycle in rods (twilight vision).
R-RNO-975634. Retinoid metabolism and transport.

Names & Taxonomyi

Protein namesi
Recommended name:
Retinol-binding protein 1
Alternative name(s):
Cellular retinol-binding protein
Short name:
CRBP
Cellular retinol-binding protein I
Short name:
CRBP-I
Gene namesi
Name:Rbp1
Synonyms:Rbp-1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 8

Organism-specific databases

RGDi3543. Rbp1.

Subcellular locationi

GO - Cellular componenti

  • cell body Source: RGD
  • cytosol Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved3 Publications
Chaini2 – 135134Retinol-binding protein 1PRO_0000067394Add
BLAST

Proteomic databases

PaxDbiP02696.
PRIDEiP02696.

PTM databases

iPTMnetiP02696.

Expressioni

Gene expression databases

GenevisibleiP02696. RN.

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000018622.

Structurei

Secondary structure

1
135
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 1610Combined sources
Helixi17 – 226Combined sources
Turni23 – 253Combined sources
Helixi28 – 369Combined sources
Beta strandi40 – 467Combined sources
Beta strandi49 – 557Combined sources
Beta strandi57 – 593Combined sources
Beta strandi61 – 666Combined sources
Beta strandi71 – 744Combined sources
Turni76 – 794Combined sources
Beta strandi82 – 909Combined sources
Beta strandi93 – 10210Combined sources
Beta strandi106 – 1127Combined sources
Beta strandi115 – 1228Combined sources
Beta strandi125 – 1339Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CRBX-ray2.10A2-135[»]
1JBHNMR-A1-135[»]
1KGLNMR-A1-135[»]
1MX7NMR-A2-135[»]
1MX8NMR-A2-135[»]
ProteinModelPortaliP02696.
SMRiP02696. Positions 1-135.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02696.

Family & Domainsi

Domaini

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG4015. Eukaryota.
ENOG4111US8. LUCA.
GeneTreeiENSGT00760000118898.
HOGENOMiHOG000004831.
HOVERGENiHBG005633.
InParanoidiP02696.
OMAiHLEMRAE.
OrthoDBiEOG7NW6BZ.
PhylomeDBiP02696.
TreeFamiTF316894.

Family and domain databases

Gene3Di2.40.128.20. 1 hit.
InterProiIPR012674. Calycin.
IPR011038. Calycin-like.
IPR031264. CRBP1.
IPR000463. Fatty_acid-bd.
IPR031259. iLBP.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
[Graphical view]
PANTHERiPTHR11955. PTHR11955. 1 hit.
PTHR11955:SF56. PTHR11955:SF56. 1 hit.
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.

P02696-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPVDFNGYWK MLSNENFEEY LRALDVNVAL RKIANLLKPD KEIVQDGDHM
60 70 80 90 100
IIRTLSTFRN YIMDFQVGKE FEEDLTGIDD RKCMTTVSWD GDKLQCVQKG
110 120 130
EKEGRGWTQW IEGDELHLEM RAEGVTCKQV FKKVH
Length:135
Mass (Da):15,834
Last modified:January 23, 2007 - v2
Checksum:i680CCE3284BD28B7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M16459 mRNA. Translation: AAA42021.1.
M19257 mRNA. Translation: AAA40962.1.
PIRiA29570. RJRTO.
RefSeqiNP_036865.1. NM_012733.4.
UniGeneiRn.902.

Genome annotation databases

EnsembliENSRNOT00000018622; ENSRNOP00000018622; ENSRNOG00000013794.
GeneIDi25056.
KEGGirno:25056.
UCSCiRGD:3543. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M16459 mRNA. Translation: AAA42021.1.
M19257 mRNA. Translation: AAA40962.1.
PIRiA29570. RJRTO.
RefSeqiNP_036865.1. NM_012733.4.
UniGeneiRn.902.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CRBX-ray2.10A2-135[»]
1JBHNMR-A1-135[»]
1KGLNMR-A1-135[»]
1MX7NMR-A2-135[»]
1MX8NMR-A2-135[»]
ProteinModelPortaliP02696.
SMRiP02696. Positions 1-135.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000018622.

PTM databases

iPTMnetiP02696.

Proteomic databases

PaxDbiP02696.
PRIDEiP02696.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000018622; ENSRNOP00000018622; ENSRNOG00000013794.
GeneIDi25056.
KEGGirno:25056.
UCSCiRGD:3543. rat.

Organism-specific databases

CTDi5947.
RGDi3543. Rbp1.

Phylogenomic databases

eggNOGiKOG4015. Eukaryota.
ENOG4111US8. LUCA.
GeneTreeiENSGT00760000118898.
HOGENOMiHOG000004831.
HOVERGENiHBG005633.
InParanoidiP02696.
OMAiHLEMRAE.
OrthoDBiEOG7NW6BZ.
PhylomeDBiP02696.
TreeFamiTF316894.

Enzyme and pathway databases

ReactomeiR-RNO-2453902. The canonical retinoid cycle in rods (twilight vision).
R-RNO-975634. Retinoid metabolism and transport.

Miscellaneous databases

EvolutionaryTraceiP02696.
NextBioi605266.
PROiP02696.

Gene expression databases

GenevisibleiP02696. RN.

Family and domain databases

Gene3Di2.40.128.20. 1 hit.
InterProiIPR012674. Calycin.
IPR011038. Calycin-like.
IPR031264. CRBP1.
IPR000463. Fatty_acid-bd.
IPR031259. iLBP.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
[Graphical view]
PANTHERiPTHR11955. PTHR11955. 1 hit.
PTHR11955:SF56. PTHR11955:SF56. 1 hit.
PfamiPF00061. Lipocalin. 1 hit.
[Graphical view]
PRINTSiPR00178. FATTYACIDBP.
SUPFAMiSSF50814. SSF50814. 1 hit.
PROSITEiPS00214. FABP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH ALL-TRANS-RETINOL.

Entry informationi

Entry nameiRET1_RAT
AccessioniPrimary (citable) accession number: P02696
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: January 20, 2016
This is version 134 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.