Rab proteins geranylgeranyltransferase component A 1

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P37727 (RAE1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 92. History...

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

Documents (2) |

Third-party data

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

Names and origin

Protein names

Recommended name:
Rab proteins geranylgeranyltransferase component A 1

Alternative name(s):
Choroideremia protein homolog
Rab escort protein 1
Short name=REP-1

Gene names

Name:	Chm
Synonyms:	Rep1

Organism

Rattus norvegicus (Rat) [Reference proteome]

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	650 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Binds unprenylated Rab proteins, presents it to the catalytic Rab GGTase dimer, and remains bound to it after the geranylgeranyl transfer reaction. The component A is thought to be regenerated by transferring its prenylated Rab back to the donor membrane. Also a pre-formed complex consisting of CHM and the Rab GGTase dimer (RGGT or component B) can bind to and prenylate Rab proteins; this alternative pathway is proposed to be the predominant pathway for Rab protein geranylgeranylation.
Subunit structure	Monomer. Can associate with the Rab GGTase dimer (RGGT or component B) prior to Rab protein binding; the association is stabilized by geranylgeranyl pyrophosphate (GGpp). The CHM:RGGT:Rab complex is destabilized by GGpp. Interacts with RAB1B; the interaction is required for RAB1B prenylation. Interacts with RABGGTA. Ref.3 Ref.4
Tissue specificity	Most abundant in the heart, brain, and spleen. Lower levels seen in the lung, liver, muscle and kidney. Extremely low levels seen in the testis.
Sequence similarities	Belongs to the Rab GDI family.

Ontologies

Keywords
Molecular function	GTPase activation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	intracellular protein transport Inferred from electronic annotation. Source: InterPro positive regulation of GTPase activity Inferred from electronic annotation. Source: GOC
Cellular_component	Rab-protein geranylgeranyltransferase complex Inferred from electronic annotation. Source: InterPro
Molecular_function	GTPase activator activity Inferred from electronic annotation. Source: UniProtKB-KW Rab GTPase binding Inferred from direct assay Ref.1. Source: RGD Rab geranylgeranyltransferase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Rab7a	P09527	2	EBI-1039231,EBI-916225

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 650

650

Rab proteins geranylgeranyltransferase component A 1

PRO_0000056688

Experimental info

Mutagenesis

279

F → A: Abolishes association with RGGT. Ref.5

Secondary structure

650

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P37727 [UniParc].

Last modified October 1, 1994. Version 1.
Checksum: 5BF42B445E546282
Show »

FASTA

650

72,480

        10         20         30         40         50         60 
MADNLPSDFD VIVIGTGLPE SIIAAACSRS GQRVLHVDSR SYYGGNWASF SFSGLLSWLK 

        70         80         90        100        110        120 
EYQENNDVVT ENSMWQEQIL ENEEAIPLSS KDKTIQHVEV FCYASQDLHK DVEEAGALQK 

       130        140        150        160        170        180 
NHASVTSAQS AEAAEAAETS CLPTAVEPLS MGSCEIPAEQ SQCPGPESSP EVNDAEATGK 

       190        200        210        220        230        240 
KENSDAKSST EEPSENVPKV QDNTETPKKN RITYSQIIKE GRRFNIDLVS QLLYSRGLLI 

       250        260        270        280        290        300 
DLLIKSNVSR YAEFKNITRI LAFREGTVEQ VPCSRADVFN SKQLTMVEKR MLMKFLTFCV 

       310        320        330        340        350        360 
EYEEHPDEYR AYEGTTFSEY LKTQKLTPNL QYFVLHSIAM TSETTSCTVD GLKATKKFLQ 

       370        380        390        400        410        420 
CLGRYGNTPF LFPLYGQGEL PQCFCRMCAV FGGIYCLRHS VQCLVVDKES RKCKAVIDQF 

       430        440        450        460        470        480 
GQRIISKHFI IEDSYLSENT CSRVQYRQIS RAVLITDGSV LKTDADQQVS ILAVPAEEPG 

       490        500        510        520        530        540 
SFGVRVIELC SSTMTCMKGT YLVHLTCMSS KTAREDLERV VQKLFTPYTE IEAENEQVEK 

       550        560        570        580        590        600 
PRLLWALYFN MRDSSDISRD CYNDLPSNVY VCSGPDSGLG NDNAVKQAET LFQQICPNED 

       610        620        630        640        650 
FCPAPPNPED IVLDGDSSQQ EVPESSVTPE TNSETPKEST VLGNPEEPSE

« Hide

References

[1]	"cDNA cloning of component A of Rab geranylgeranyl transferase and demonstration of its role as a Rab escort protein." Andres D.A., Seabra M.C., Brown M.S., Armstrong S.A., Smeland T.E., Cremers F.P.M., Goldstein J.L. Cell 73:1091-1099(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain.
[2]	"Purification of component A of Rab geranylgeranyl transferase: possible identity with the choroideremia gene product." Saebra M.C., Brown M.S., Slaughter C.A., Suedhof T.C., Goldstein J.L. Cell 70:1049-1057(1992) [PubMed] [Europe PMC] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE. Tissue: Brain.
[3]	"Membrane targeting of a Rab GTPase that fails to associate with Rab escort protein (REP) or guanine nucleotide dissociation inhibitor (GDI)." Overmeyer J.H., Wilson A.L., Maltese W.A. J. Biol. Chem. 276:20379-20386(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH RAB1B.
[4]	"Phosphoisoprenoids modulate association of Rab geranylgeranyltransferase with REP-1." Thoma N.H., Iakovenko A., Goody R.S., Alexandrov K. J. Biol. Chem. 276:48637-48643(2001) [PubMed] [Europe PMC] [Abstract] Cited for: SUBUNIT.
[5]	"Structure of Rab escort protein-1 in complex with Rab geranylgeranyltransferase." Pylypenko O., Rak A., Reents R., Niculae A., Sidorovitch V., Cioaca M.D., Bessolitsyna E., Thomae N.H., Waldmann H., Schlichting I., Goody R.S., Alexandrov K. Mol. Cell 11:483-494(2003) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN COMPLEX WITH RABGGTA AND RABGGTB, MUTAGENESIS OF PHE-279.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L13722 mRNA. Translation: AAA87626.1.

IPI

IPI00209504.

PIR

A40686.

RefSeq

NP_058763.1. NM_017067.1.

UniGene

Rn.10191.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1LTX	X-ray	2.70	R	1-650	[»]
1VG0	X-ray	2.20	A	1-650	[»]
1VG9	X-ray	2.50	A/C/E/G	1-650	[»]

DisProt

DP00458.

ProteinModelPortal

P37727.

SMR

P37727. Positions 2-614.

ModBase

Search...

Protein-protein interaction databases

IntAct

P37727. 1 interaction.

STRING

10116.ENSRNOP00000000174.

PTM databases

PhosphoSite

P37727.

Proteomic databases

PaxDb

P37727.

PRIDE

P37727.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

24942.

KEGG

rno:24942.

UCSC

RGD:2340. rat.

Organism-specific databases

CTD

1121.

RGD

2340. Chm.

Phylogenomic databases

eggNOG

COG5044.

HOGENOM

HOG000231282.

HOVERGEN

HBG004961.

InParanoid

P37727.

OrthoDB

EOG441QBB.

Gene expression databases

ArrayExpress

P37727.

Genevestigator

P37727.

GermOnline

ENSRNOG00000000161. Rattus norvegicus.

Family and domain databases

InterPro

IPR018203. GDP_dissociation_inhibitor.
IPR001738. Rab_escort.
IPR016664. Rab_geranylTrfase_A_euk.
[Graphical view]

Pfam

PF00996. GDI. 2 hits.
[Graphical view]

PIRSF

PIRSF016550. Rab_ger_ger_transf_A_euk. 1 hit.

PRINTS

PR00893. RABESCORT.
PR00891. RABGDIREP.

ProtoNet

Search...

Other

EvolutionaryTrace

P37727.

NextBio

604935.

Entry information

Entry name

RAE1_RAT

Accession

Primary (citable) accession number: P37727

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	October 1, 1994
Last modified:	April 3, 2013
This is version 92 of the entry and version 1 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·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM 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