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Protein

Rab proteins geranylgeranyltransferase component A 1

Gene

Chm

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

Functioni

Substrate-binding subunit of the Rab geranylgeranyltransferase (GGTase) complex. Binds unprenylated Rab proteins and presents the substrate peptide to the catalytic component B composed of RABGGTA and RABGGTB, 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. Besides, 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.5 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

GTPase activation

Names & Taxonomyi

Protein namesi
Recommended name:
Rab proteins geranylgeranyltransferase component A 1
Alternative name(s):
Choroideremia protein homolog
Rab escort protein 1
Short name:
REP-1
Gene namesi
Name:Chm
Synonyms:Rep1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2340. Chm.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: UniProtKB
  • Rab-protein geranylgeranyltransferase complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi279 – 2791F → A: Abolishes association with RGGT. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 650650Rab proteins geranylgeranyltransferase component A 1PRO_0000056688Add
BLAST

Proteomic databases

PaxDbiP37727.
PRIDEiP37727.

PTM databases

iPTMnetiP37727.
PhosphoSiteiP37727.

Expressioni

Tissue specificityi

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.

Interactioni

Subunit structurei

Monomer. Heterotrimer composed of RABGGTA, RABGGTB and CHM; within this trimer, RABGGTA and RABGGTB form the catalytic component B, while CHM (component A) mediates Rab protein binding. 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 RAB1A, RAB1B, RAB7A and RAB27A and mediates their prenylation.7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Rab7aP095272EBI-1039231,EBI-916225

GO - Molecular functioni

  • Rab GTPase binding Source: UniProtKB

Protein-protein interaction databases

IntActiP37727. 1 interaction.
STRINGi10116.ENSRNOP00000000174.

Structurei

Secondary structure

1
650
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi10 – 145Combined sources
Helixi18 – 2912Combined sources
Beta strandi34 – 374Combined sources
Beta strandi39 – 435Combined sources
Helixi45 – 473Combined sources
Helixi52 – 6110Combined sources
Helixi75 – 784Combined sources
Beta strandi83 – 886Combined sources
Beta strandi95 – 1028Combined sources
Helixi214 – 2196Combined sources
Helixi221 – 2233Combined sources
Beta strandi226 – 2294Combined sources
Beta strandi233 – 2375Combined sources
Helixi238 – 2469Combined sources
Helixi248 – 2514Combined sources
Beta strandi254 – 2563Combined sources
Beta strandi259 – 27012Combined sources
Helixi275 – 2806Combined sources
Beta strandi282 – 2843Combined sources
Helixi286 – 30015Combined sources
Helixi301 – 3044Combined sources
Helixi306 – 3105Combined sources
Turni311 – 3144Combined sources
Helixi317 – 3215Combined sources
Beta strandi324 – 3263Combined sources
Helixi328 – 33710Combined sources
Beta strandi343 – 3453Combined sources
Helixi348 – 36114Combined sources
Beta strandi364 – 37310Combined sources
Helixi379 – 39012Combined sources
Beta strandi394 – 3985Combined sources
Beta strandi401 – 4077Combined sources
Turni408 – 4103Combined sources
Beta strandi413 – 4186Combined sources
Beta strandi423 – 4253Combined sources
Beta strandi427 – 4326Combined sources
Helixi433 – 4353Combined sources
Turni438 – 4436Combined sources
Beta strandi447 – 45812Combined sources
Beta strandi470 – 4745Combined sources
Beta strandi478 – 4803Combined sources
Beta strandi484 – 4896Combined sources
Helixi491 – 4933Combined sources
Beta strandi494 – 4963Combined sources
Beta strandi501 – 5088Combined sources
Helixi513 – 52412Combined sources
Beta strandi542 – 55312Combined sources
Helixi559 – 5613Combined sources
Beta strandi562 – 5643Combined sources
Beta strandi569 – 5724Combined sources
Beta strandi577 – 5815Combined sources
Helixi582 – 59514Combined sources
Beta strandi596 – 5983Combined sources
Beta strandi610 – 6134Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LTXX-ray2.70R1-650[»]
1VG0X-ray2.20A1-650[»]
1VG9X-ray2.50A/C/E/G1-650[»]
DisProtiDP00458.
ProteinModelPortaliP37727.
SMRiP37727. Positions 2-614.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP37727.

Family & Domainsi

Sequence similaritiesi

Belongs to the Rab GDI family.Curated

Phylogenomic databases

eggNOGiKOG4405. Eukaryota.
COG5044. LUCA.
HOGENOMiHOG000231282.
HOVERGENiHBG004961.
InParanoidiP37727.
PhylomeDBiP37727.

Family and domain databases

Gene3Di3.50.50.60. 2 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR018203. GDP_dissociation_inhibitor.
IPR001738. Rab_escort.
[Graphical view]
PfamiPF00996. GDI. 2 hits.
[Graphical view]
PIRSFiPIRSF016550. Rab_ger_ger_transf_A_euk. 1 hit.
PRINTSiPR00893. RABESCORT.
PR00891. RABGDIREP.
SUPFAMiSSF51905. SSF51905. 2 hits.

Sequencei

Sequence statusi: Complete.

P37727-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADNLPSDFD VIVIGTGLPE SIIAAACSRS GQRVLHVDSR SYYGGNWASF
60 70 80 90 100
SFSGLLSWLK EYQENNDVVT ENSMWQEQIL ENEEAIPLSS KDKTIQHVEV
110 120 130 140 150
FCYASQDLHK DVEEAGALQK NHASVTSAQS AEAAEAAETS CLPTAVEPLS
160 170 180 190 200
MGSCEIPAEQ SQCPGPESSP EVNDAEATGK KENSDAKSST EEPSENVPKV
210 220 230 240 250
QDNTETPKKN RITYSQIIKE GRRFNIDLVS QLLYSRGLLI DLLIKSNVSR
260 270 280 290 300
YAEFKNITRI LAFREGTVEQ VPCSRADVFN SKQLTMVEKR MLMKFLTFCV
310 320 330 340 350
EYEEHPDEYR AYEGTTFSEY LKTQKLTPNL QYFVLHSIAM TSETTSCTVD
360 370 380 390 400
GLKATKKFLQ CLGRYGNTPF LFPLYGQGEL PQCFCRMCAV FGGIYCLRHS
410 420 430 440 450
VQCLVVDKES RKCKAVIDQF GQRIISKHFI IEDSYLSENT CSRVQYRQIS
460 470 480 490 500
RAVLITDGSV LKTDADQQVS ILAVPAEEPG SFGVRVIELC SSTMTCMKGT
510 520 530 540 550
YLVHLTCMSS KTAREDLERV VQKLFTPYTE IEAENEQVEK PRLLWALYFN
560 570 580 590 600
MRDSSDISRD CYNDLPSNVY VCSGPDSGLG NDNAVKQAET LFQQICPNED
610 620 630 640 650
FCPAPPNPED IVLDGDSSQQ EVPESSVTPE TNSETPKEST VLGNPEEPSE
Length:650
Mass (Da):72,480
Last modified:October 1, 1994 - v1
Checksum:i5BF42B445E546282
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L13722 mRNA. Translation: AAA87626.1.
PIRiA40686.
RefSeqiNP_058763.1. NM_017067.1.
UniGeneiRn.10191.

Genome annotation databases

GeneIDi24942.
KEGGirno:24942.
UCSCiRGD:2340. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L13722 mRNA. Translation: AAA87626.1.
PIRiA40686.
RefSeqiNP_058763.1. NM_017067.1.
UniGeneiRn.10191.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LTXX-ray2.70R1-650[»]
1VG0X-ray2.20A1-650[»]
1VG9X-ray2.50A/C/E/G1-650[»]
DisProtiDP00458.
ProteinModelPortaliP37727.
SMRiP37727. Positions 2-614.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP37727. 1 interaction.
STRINGi10116.ENSRNOP00000000174.

PTM databases

iPTMnetiP37727.
PhosphoSiteiP37727.

Proteomic databases

PaxDbiP37727.
PRIDEiP37727.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi24942.
KEGGirno:24942.
UCSCiRGD:2340. rat.

Organism-specific databases

CTDi1121.
RGDi2340. Chm.

Phylogenomic databases

eggNOGiKOG4405. Eukaryota.
COG5044. LUCA.
HOGENOMiHOG000231282.
HOVERGENiHBG004961.
InParanoidiP37727.
PhylomeDBiP37727.

Miscellaneous databases

EvolutionaryTraceiP37727.
PROiP37727.

Family and domain databases

Gene3Di3.50.50.60. 2 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR018203. GDP_dissociation_inhibitor.
IPR001738. Rab_escort.
[Graphical view]
PfamiPF00996. GDI. 2 hits.
[Graphical view]
PIRSFiPIRSF016550. Rab_ger_ger_transf_A_euk. 1 hit.
PRINTSiPR00893. RABESCORT.
PR00891. RABGDIREP.
SUPFAMiSSF51905. SSF51905. 2 hits.
ProtoNetiSearch...

Entry informationi

Entry nameiRAE1_RAT
AccessioniPrimary (citable) accession number: P37727
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: July 6, 2016
This is version 115 of the entry and version 1 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.