REP1_CAEEL
ID REP1_CAEEL Reviewed; 510 AA.
AC Q9BKQ5;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Rab proteins geranylgeranyltransferase component A 1 {ECO:0000250|UniProtKB:P24386};
DE AltName: Full=Rab escort protein 1 {ECO:0000312|WormBase:Y67D2.1};
DE AltName: Full=TCD protein {ECO:0000250|UniProtKB:P24386};
GN Name=rep-1 {ECO:0000312|WormBase:Y67D2.1};
GN ORFNames=Y67D2.1 {ECO:0000312|WormBase:Y67D2.1};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP FUNCTION, INTERACTION WITH RAB-5; RAB-7 AND RAB-11, TISSUE SPECIFICITY,
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF GLU-107.
RX PubMed=19090809; DOI=10.1111/j.1365-2443.2008.01232.x;
RA Tanaka D., Kameyama K., Okamoto H., Doi M.;
RT "Caenorhabditis elegans Rab escort protein (REP-1) differently regulates
RT each Rab protein function and localization in a tissue-dependent manner.";
RL Genes Cells 13:1141-1157(2008).
CC -!- FUNCTION: Substrate-binding subunit of the Rab
CC geranylgeranyltransferase (GGTase) complex (By similarity). Binds
CC unprenylated Rab proteins and presents the substrate peptide to the
CC catalytic component B and remains bound to it after the geranylgeranyl
CC transfer reaction (By similarity). The component A is thought to be
CC regenerated by transferring its prenylated Rab back to the donor
CC membrane (By similarity). Plays a role in neurotransmitter release from
CC presynaptic terminals at neuromuscular junctions (PubMed:19090809).
CC Positively regulates the function of rab-27 in synaptic transmission
CC most likely through mediating rab-27 prenylation (PubMed:19090809).
CC {ECO:0000250|UniProtKB:P24386, ECO:0000269|PubMed:19090809}.
CC -!- SUBUNIT: May interact with rab-5, rab-7 and rab-11 (PubMed:19090809).
CC Does not interact with rab-3, rab-27 and rab-10 (PubMed:19090809).
CC {ECO:0000269|PubMed:19090809}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|RuleBase:RU363124}.
CC -!- TISSUE SPECIFICITY: Expressed in several neurons including head
CC neurons, motor neurons located in the ventral nerve cord, HSN and CAN
CC neurons, and tail neurons, and in muscles such as body-wall,
CC pharyngeal, intestinal and anal sphincter (PubMed:19090809). Also
CC expressed in seam cells, the hypodermis and the intestine
CC (PubMed:19090809). {ECO:0000269|PubMed:19090809}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in mild
CC defecation defects (PubMed:19090809). RNAi-mediated knockdown increases
CC the levels of unprenylated rab-27 (PubMed:19090809). RNAi-mediated
CC knockdown disrupts the localization of rab-5 and rab-7
CC (PubMed:19090809). {ECO:0000269|PubMed:19090809}.
CC -!- SIMILARITY: Belongs to the Rab GDI family.
CC {ECO:0000255|RuleBase:RU363124}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BX284603; CCD73025.1; -; Genomic_DNA.
DR RefSeq; NP_001022928.1; NM_001027757.3.
DR AlphaFoldDB; Q9BKQ5; -.
DR SMR; Q9BKQ5; -.
DR STRING; 6239.Y67D2.1a.1; -.
DR EPD; Q9BKQ5; -.
DR PaxDb; Q9BKQ5; -.
DR PeptideAtlas; Q9BKQ5; -.
DR EnsemblMetazoa; Y67D2.1.1; Y67D2.1.1; WBGene00022051.
DR EnsemblMetazoa; Y67D2.1.2; Y67D2.1.2; WBGene00022051.
DR GeneID; 175311; -.
DR KEGG; cel:CELE_Y67D2.1; -.
DR UCSC; Y67D2.1b.1; c. elegans.
DR CTD; 175311; -.
DR WormBase; Y67D2.1; CE27306; WBGene00022051; rep-1.
DR eggNOG; KOG4405; Eukaryota.
DR GeneTree; ENSGT00950000182994; -.
DR HOGENOM; CLU_021695_4_1_1; -.
DR InParanoid; Q9BKQ5; -.
DR OMA; IKSNICR; -.
DR OrthoDB; 1017439at2759; -.
DR PhylomeDB; Q9BKQ5; -.
DR Reactome; R-CEL-6803205; TP53 regulates transcription of several additional cell death genes whose specific roles in p53-dependent apoptosis remain uncertain.
DR Reactome; R-CEL-8873719; RAB geranylgeranylation.
DR Reactome; R-CEL-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00022051; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005968; C:Rab-protein geranylgeranyltransferase complex; IBA:GO_Central.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0005093; F:Rab GDP-dissociation inhibitor activity; IEA:InterPro.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0018344; P:protein geranylgeranylation; IBA:GO_Central.
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; -; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR018203; GDP_dissociation_inhibitor.
DR InterPro; IPR001738; Rab_escort.
DR InterPro; IPR000806; RabGDI.
DR PANTHER; PTHR11787; PTHR11787; 1.
DR Pfam; PF00996; GDI; 2.
DR PIRSF; PIRSF016550; Rab_ger_ger_transf_A_euk; 1.
DR PRINTS; PR00892; RABGDI.
DR PRINTS; PR00891; RABGDIREP.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; GTPase activation; Reference proteome.
FT CHAIN 1..510
FT /note="Rab proteins geranylgeranyltransferase component A
FT 1"
FT /id="PRO_0000454726"
FT MUTAGEN 107
FT /note="E->K: In ta208; embryonic lethality in some animals
FT and reduces brood size. Some animals have abnormal germ-
FT line development and gonad morphology. In severely affected
FT animals, either gonads fail to develop or small traces of
FT gonads are located around the vulva. Mild defecation
FT defects. Disrupts the localization of rab-5, rab-7 and rab-
FT 27. Reduces the number of body bends in response to
FT exogenous melatonin. Mild resistance to the
FT acetylcholinesterase inhibitor aldicarb. However, induces
FT paralysis in response to aldicarb in some animals."
FT /evidence="ECO:0000269|PubMed:19090809"
SQ SEQUENCE 510 AA; 56838 MW; 5037C7772C618620 CRC64;
MDEKLPESVD VVVLGTGLPE AILASACARA GLSVLHLDRN EYYGGDWSSF TMSMVHEVTE
NQVKKLDSSE ISKLSELLTE NEQLIELGNR EIVENIEMTW IPRGKDEEKP MKTQLEEASQ
MRRFSIDLVP KILLSKGAMV QTLCDSQVSH YAEFKLVNRQ LCPTETPEAG ITLNPVPCSK
GEIFQSNALS ILEKRALMKF ITFCTQWSTK DTEEGRKLLA EHADRPFSEF LEQMGVGKTL
QSFIINTIGI LQQRPTAMTG MLASCQFMDS VGHFGPSPFL FPLYGCGELS QCFCRLAAVF
GSLYCLGRPV QAIVKKDGKI TAVIANGDRV NCRYIVMSPR FVPETVPASS TLKIERIVYA
TDKSIKEAEK EQLTLLNLAS LRPDAAVSRL VEVGFEACTA PKGHFLVHAT GTQEGETSVK
TIAEKIFEKN EVEPYWKMSF TANSMKFDTA GAENVVVAPP VDANLHYASV VEECRQLFCT
TWPELDFLPR AMKKEEEEEE EPETEEIAEN
