RAE2_MOUSE
ID RAE2_MOUSE Reviewed; 621 AA.
AC Q9QZD5; Q0VF88; Q8CH16;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 2.
DT 25-MAY-2022, entry version 127.
DE RecName: Full=Rab proteins geranylgeranyltransferase component A 2;
DE AltName: Full=Choroideremia-like protein;
DE AltName: Full=Rab escort protein 2;
DE Short=REP-2;
GN Name=Chml; Synonyms=Rep2;
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 [GENOMIC DNA].
RC STRAIN=129/SvJ;
RA Gegg M., Tolmachova T., Seabra M.C.;
RT "Cloning and sequencing of the mouse REP2 gene.";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=12242008; DOI=10.1016/s0378-1119(02)00799-0;
RA Kasper G., Taudien S., Staub E., Mennerich D., Rieder M., Hinzmann B.,
RA Dahl E., Schwidetzky U., Rosenthal A., Rump A.;
RT "Different structural organization of the encephalopsin gene in man and
RT mouse.";
RL Gene 295:27-32(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
CC -!- FUNCTION: Substrate-binding subunit (component A) of the Rab
CC geranylgeranyltransferase (GGTase) complex. Binds unprenylated Rab
CC proteins and presents the substrate peptide to the catalytic component
CC B. The component A is thought to be regenerated by transferring its
CC prenylated Rab back to the donor membrane. Less effective than CHM in
CC supporting prenylation of Rab3 family (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Monomer. Heterotrimer composed of RABGGTA, RABGGTB and CHML;
CC within this trimer, RABGGTA and RABGGTB form the catalytic component B,
CC while CHML (component A) mediates Rab protein binding. Interacts with
CC RAB1A, RAB7A and RAB27A, but has much lower affinity for RAB1A, RAB7A
CC and RAB27A than CHM (By similarity). Interacts with the non-
CC phosphorylated forms of RAB3A, RAB3B, RAB3C, RAB3D, RAB5B, RAB5C,
CC RAB8A, RAB8B, RAB10, RAB12, RAB35, and RAB43 (By similarity).
CC {ECO:0000250|UniProtKB:P26374}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the Rab GDI family. {ECO:0000305}.
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DR EMBL; AF189156; AAF01059.1; -; Genomic_DNA.
DR EMBL; AF482427; AAO15718.1; -; Genomic_DNA.
DR EMBL; BC118932; AAI18933.1; -; mRNA.
DR CCDS; CCDS35796.1; -.
DR RefSeq; NP_067325.2; NM_021350.2.
DR AlphaFoldDB; Q9QZD5; -.
DR SMR; Q9QZD5; -.
DR STRING; 10090.ENSMUSP00000100600; -.
DR iPTMnet; Q9QZD5; -.
DR PhosphoSitePlus; Q9QZD5; -.
DR MaxQB; Q9QZD5; -.
DR PaxDb; Q9QZD5; -.
DR PeptideAtlas; Q9QZD5; -.
DR PRIDE; Q9QZD5; -.
DR ProteomicsDB; 300347; -.
DR DNASU; 12663; -.
DR GeneID; 12663; -.
DR KEGG; mmu:12663; -.
DR UCSC; uc007dtr.2; mouse.
DR CTD; 1122; -.
DR MGI; MGI:101913; Chml.
DR eggNOG; KOG4405; Eukaryota.
DR InParanoid; Q9QZD5; -.
DR OrthoDB; 1017439at2759; -.
DR PhylomeDB; Q9QZD5; -.
DR TreeFam; TF320813; -.
DR Reactome; R-MMU-8873719; RAB geranylgeranylation.
DR Reactome; R-MMU-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR BioGRID-ORCS; 12663; 2 hits in 75 CRISPR screens.
DR PRO; PR:Q9QZD5; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9QZD5; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
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:0031267; F:small GTPase binding; ISS:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0018344; P:protein geranylgeranylation; 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 2: Evidence at transcript level;
KW Cytoplasm; GTPase activation; Reference proteome.
FT CHAIN 1..621
FT /note="Rab proteins geranylgeranyltransferase component A
FT 2"
FT /id="PRO_0000056690"
FT REGION 113..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..155
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..171
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 351
FT /note="T -> P (in Ref. 1; AAF01059)"
FT /evidence="ECO:0000305"
FT CONFLICT 361
FT /note="N -> T (in Ref. 2; AAO15718)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 621 AA; 70010 MW; F198A7489F9D5D6E CRC64;
MAEKLPTEFD VVIIGTGLPE SILAAACSRS GQRVLHVDSR SYYGGNWASF SFTGLQSWLK
DYQQNHDSEE GVTATWQDLI HETEEAISLR KKDETIQHTE VFCYASQDVE DSVQDTETLQ
RSSPLEASAT PADSLDSASL PKERQSAYST SYEVPSRHTE ESDRELSLPS ANVEDSLEKE
KYCGDKTDMH TVSGEDKGEH KLVVQDSIEQ PKRNRITYSQ MVKESRRFNI DLVSKPLYSQ
GSLIDLLIKS NVSRYAEFKN VTRILAFWEG KVEQVPCSRA DVFNSKELSM VEKRMLMKFL
TFCLDYEQHS DEYQDFKQCS FSDYLKTKKL TPNLQHFILH SIAMTSESSC TTLDGLQATK
NFLQCLGRFG NTPFIFPLYG HGEIPQCFCR MCAVFGGVYC LRHKVQCLVV DKDSGRCKGI
IDAFGQRISA NYFIVEDSYL PKETCSNVQY KQISRAVLIT DQSILKTDSD QQISILVVPP
LEPGTTSVRV MELCSSTMTC MKDSYLVHLT CSSSKTARED LEPVVKQLFI PEAEAEAGKD
ELRKPRLLWA LYFNMRDSSG VSRSSYCGLP SNVYICSGPD WGLGSEHAVK QAETLFQEIF
PSEEFCPPPP NPEDIIFEAE G
