RAE1_MOUSE
ID RAE1_MOUSE Reviewed; 665 AA.
AC Q9QXG2; Q80UV8;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 123.
DE RecName: Full=Rab proteins geranylgeranyltransferase component A 1;
DE AltName: Full=Choroideremia protein homolog;
DE AltName: Full=Rab escort protein 1;
DE Short=REP-1;
GN Name=Chm; Synonyms=Rep1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ;
RA van den Hurk J.A., Huber I., van de Pol T.J., Cremers F.P.;
RT "Cloning and sequencing of the mouse choroideremia gene.";
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Liver, Lung, Pancreas, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Substrate-binding subunit of the Rab
CC geranylgeranyltransferase (GGTase) complex. Binds unprenylated Rab
CC proteins and presents the substrate peptide to the catalytic component
CC B composed of RABGGTA and RABGGTB, and remains bound to it after the
CC geranylgeranyl transfer reaction. The component A is thought to be
CC regenerated by transferring its prenylated Rab back to the donor
CC membrane. Besides, a pre-formed complex consisting of CHM and the Rab
CC GGTase dimer (RGGT or component B) can bind to and prenylate Rab
CC proteins; this alternative pathway is proposed to be the predominant
CC pathway for Rab protein geranylgeranylation (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Monomer (By similarity). Heterotrimer composed of RABGGTA,
CC RABGGTB and CHM; within this trimer, RABGGTA and RABGGTB form the
CC catalytic component B, while CHM (component A) mediates Rab protein
CC binding (By similarity). Can associate with the Rab GGTase dimer (RGGT
CC or component B) prior to Rab protein binding; the association is
CC stabilized by geranylgeranyl pyrophosphate (GGpp). The CHM:RGGT:Rab
CC complex is destabilized by GGpp (By similarity). Interacts with RAB1A,
CC RAB1B, RAB5A, RAB7A and RAB27A and mediates their prenylation (By
CC similarity). Interacts with the non-phosphorylated forms of RAB3A,
CC RAB3B, RAB3C, RAB3D, RAB5B, RAB5C RAB8A, RAB8B, RAB10, RAB12, RAB35,
CC and RAB43 (By similarity). {ECO:0000250|UniProtKB:P24386,
CC ECO:0000250|UniProtKB:P37727}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the Rab GDI family. {ECO:0000305}.
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DR EMBL; AF218084; AAF25478.1; -; mRNA.
DR EMBL; BC047461; AAH47461.1; -; mRNA.
DR AlphaFoldDB; Q9QXG2; -.
DR SMR; Q9QXG2; -.
DR STRING; 10090.ENSMUSP00000026607; -.
DR iPTMnet; Q9QXG2; -.
DR PhosphoSitePlus; Q9QXG2; -.
DR EPD; Q9QXG2; -.
DR MaxQB; Q9QXG2; -.
DR PaxDb; Q9QXG2; -.
DR PeptideAtlas; Q9QXG2; -.
DR PRIDE; Q9QXG2; -.
DR ProteomicsDB; 255031; -.
DR MGI; MGI:892979; Chm.
DR eggNOG; KOG4405; Eukaryota.
DR InParanoid; Q9QXG2; -.
DR PhylomeDB; Q9QXG2; -.
DR Reactome; R-MMU-6803205; TP53 regulates transcription of several additional cell death genes whose specific roles in p53-dependent apoptosis remain uncertain.
DR Reactome; R-MMU-8873719; RAB geranylgeranylation.
DR Reactome; R-MMU-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR ChiTaRS; Chm; mouse.
DR PRO; PR:Q9QXG2; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9QXG2; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005968; C:Rab-protein geranylgeranyltransferase complex; ISS:UniProtKB.
DR GO; GO:0005092; F:GDP-dissociation inhibitor activity; IEA:InterPro.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0031267; F:small GTPase binding; ISS:UniProtKB.
DR GO; GO:0001568; P:blood vessel development; IMP:MGI.
DR GO; GO:0018344; P:protein geranylgeranylation; ISS:UniProtKB.
DR GO; GO:0006612; P:protein targeting to membrane; ISS:UniProtKB.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR Gene3D; 3.50.50.60; -; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR018203; GDP_dissociation_inhibitor.
DR InterPro; IPR001738; Rab_escort.
DR PANTHER; PTHR11787; PTHR11787; 1.
DR Pfam; PF00996; GDI; 2.
DR PIRSF; PIRSF016550; Rab_ger_ger_transf_A_euk; 1.
DR PRINTS; PR00893; RABESCORT.
DR PRINTS; PR00891; RABGDIREP.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; GTPase activation; Reference proteome.
FT CHAIN 1..665
FT /note="Rab proteins geranylgeranyltransferase component A
FT 1"
FT /id="PRO_0000056687"
FT REGION 167..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 620..665
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..184
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..219
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 628..654
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 203
FT /note="S -> C (in Ref. 2; AAH47461)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 665 AA; 73977 MW; FF71A74AD3FBDE0A CRC64;
MADNLPSDFD VIVIGTGLPE SIIAAACSRS GQRVLHVDSR SYYGGNWASF SFSGLLSWLK
EYQENSDVVT ENSMWQEQIL ENEEAILLSS KDKTIQHVEV FCYASQDLHK DVEEAGALQK
NPASVMSAQA TEAAEAAEAA EATEAAEAAE AAEAACLPTA EESLSTRSCE LPAEQSQCMG
PESSPQVNDA EVGEKETQSD AKSSTEQSSE ILPKVQDNTE TPKRNVITYS QIIKEGRRFN
IDLVSKLLYS RGLLIDLLIK SNVSRYAEFK NITRILAFRE GTVEQVPCSR ADVFNSKQLT
MVEKRMLMKF LTFCVEYEDH PDEYKAYEET TFSEYLKTQK LTPNLQYFVL HSIAMTSETT
SSTVDGLKAT KKFLQCLGRY GNTPFLFPLY GQGELPQCFC RMCAVFGGIY CLRHSVQCLV
VDKESRKCKA IVDQFGQRII SKHFVIEDSY LSENTCSGVQ YRQISRAVLI TDGSVLKPDS
DQQVSILTVP AEESGSFAVR VIELCSSTMT CMKGTYLVHL TCMSSKTARE DLERVVQKLF
TPYTEIEAEN EQVEKPRILW ALYFNMRDSS DISRDCYNDL PSNVYVCSGP DCNLGNDNAV
QQAEIVFQKI CPNEDFCPAP PNPEDIILDG DSSQQEVSES SVIPETNSET PKESTVLGDS
EEPSE
