RME6_CAEEL
ID RME6_CAEEL Reviewed; 1093 AA.
AC Q9GYH7; Q4VQC9; Q8MNR6;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Receptor-mediated endocytosis protein 6;
GN Name=rme-6; ORFNames=F49E7.1;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, SUBCELLULAR LOCATION,
RP INTERACTION WITH RAB5 AND ALPHA-ADAPTIN, AND MUTAGENESIS OF VAL-65;
RP CYS-1017 AND TRP-1079.
RX PubMed=15895077; DOI=10.1038/ncb1261;
RA Sato M., Sato K., Fonarev P., Huang C.-J., Liou W., Grant B.D.;
RT "Caenorhabditis elegans RME-6 is a novel regulator of RAB-5 at the
RT clathrin-coated pit.";
RL Nat. Cell Biol. 7:559-569(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Bristol N2;
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).
CC -!- FUNCTION: Acts both as a GTPase-activating protein (GAP) and a guanine
CC nucleotide exchange factor (GEF), and participates in endocytosis. Acts
CC by regulating the activation of rab-5 by exchanging bound GDP for free
CC GTP at clathrin coated pits. {ECO:0000269|PubMed:15895077}.
CC -!- SUBUNIT: Interacts with GDP-bound rab-5. Interacts with alpha-adaptin.
CC {ECO:0000269|PubMed:15895077}.
CC -!- INTERACTION:
CC Q9GYH7; Q22601: apa-2; NbExp=3; IntAct=EBI-320814, EBI-5323248;
CC Q9GYH7; P91857: rab-5; NbExp=2; IntAct=EBI-320814, EBI-2655330;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:15895077};
CC Peripheral membrane protein {ECO:0000269|PubMed:15895077}. Cytoplasmic
CC vesicle, clathrin-coated vesicle {ECO:0000269|PubMed:15895077}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a;
CC IsoId=Q9GYH7-1; Sequence=Displayed;
CC Name=b;
CC IsoId=Q9GYH7-2; Sequence=VSP_032369;
CC -!- SIMILARITY: Belongs to the GAPVD1 family. {ECO:0000305}.
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DR EMBL; AY750054; AAW73253.1; -; mRNA.
DR EMBL; FO080361; CCD63167.1; -; Genomic_DNA.
DR EMBL; FO080361; CCD63168.1; -; Genomic_DNA.
DR PIR; T25788; T25788.
DR PIR; T31057; T31057.
DR RefSeq; NP_001294826.1; NM_001307897.1.
DR RefSeq; NP_508208.2; NM_075807.3. [Q9GYH7-1]
DR AlphaFoldDB; Q9GYH7; -.
DR SMR; Q9GYH7; -.
DR BioGRID; 45416; 3.
DR DIP; DIP-25631N; -.
DR IntAct; Q9GYH7; 2.
DR STRING; 6239.F49E7.1a; -.
DR EPD; Q9GYH7; -.
DR PaxDb; Q9GYH7; -.
DR PeptideAtlas; Q9GYH7; -.
DR PRIDE; Q9GYH7; -.
DR EnsemblMetazoa; F49E7.1a.1; F49E7.1a.1; WBGene00004377. [Q9GYH7-1]
DR EnsemblMetazoa; F49E7.1b.1; F49E7.1b.1; WBGene00004377. [Q9GYH7-2]
DR EnsemblMetazoa; F49E7.1b.2; F49E7.1b.2; WBGene00004377. [Q9GYH7-2]
DR EnsemblMetazoa; F49E7.1b.3; F49E7.1b.3; WBGene00004377. [Q9GYH7-2]
DR GeneID; 180463; -.
DR KEGG; cel:CELE_F49E7.1; -.
DR UCSC; F49E7.1a; c. elegans. [Q9GYH7-1]
DR CTD; 180463; -.
DR WormBase; F49E7.1a; CE38712; WBGene00004377; rme-6. [Q9GYH7-1]
DR WormBase; F49E7.1b; CE26468; WBGene00004377; rme-6. [Q9GYH7-2]
DR eggNOG; KOG2319; Eukaryota.
DR GeneTree; ENSGT00940000156611; -.
DR HOGENOM; CLU_012490_0_0_1; -.
DR InParanoid; Q9GYH7; -.
DR OMA; SCFLGKK; -.
DR OrthoDB; 944088at2759; -.
DR PhylomeDB; Q9GYH7; -.
DR Reactome; R-CEL-8856828; Clathrin-mediated endocytosis.
DR PRO; PR:Q9GYH7; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00004377; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR GO; GO:0045334; C:clathrin-coated endocytic vesicle; IDA:WormBase.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005769; C:early endosome; IDA:WormBase.
DR GO; GO:0030139; C:endocytic vesicle; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:WormBase.
DR GO; GO:0032794; F:GTPase activating protein binding; ISS:UniProtKB.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISS:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; IPI:WormBase.
DR GO; GO:0006897; P:endocytosis; IMP:WormBase.
DR GO; GO:0018996; P:molting cycle, collagen and cuticulin-based cuticle; IGI:WormBase.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IGI:WormBase.
DR GO; GO:2000369; P:regulation of clathrin-dependent endocytosis; IMP:WormBase.
DR GO; GO:0051223; P:regulation of protein transport; ISS:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 1.10.506.10; -; 1.
DR Gene3D; 1.20.1050.80; -; 1.
DR InterPro; IPR001936; RasGAP_dom.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR003123; VPS9.
DR InterPro; IPR045046; Vps9-like.
DR InterPro; IPR037191; VPS9_dom_sf.
DR PANTHER; PTHR23101; PTHR23101; 1.
DR Pfam; PF00616; RasGAP; 1.
DR Pfam; PF02204; VPS9; 1.
DR SMART; SM00167; VPS9; 1.
DR SUPFAM; SSF109993; SSF109993; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR PROSITE; PS50018; RAS_GTPASE_ACTIV_2; 1.
DR PROSITE; PS51205; VPS9; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasmic vesicle; Endocytosis; GTPase activation;
KW Guanine-nucleotide releasing factor; Membrane; Reference proteome.
FT CHAIN 1..1093
FT /note="Receptor-mediated endocytosis protein 6"
FT /id="PRO_0000324775"
FT DOMAIN 140..355
FT /note="Ras-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00167"
FT DOMAIN 955..1093
FT /note="VPS9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00550"
FT REGION 547..610
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 643..669
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..601
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 651..666
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..999
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_032369"
FT MUTAGEN 65
FT /note="V->D: In ar483; shows endocytic defects."
FT /evidence="ECO:0000269|PubMed:15895077"
FT MUTAGEN 1017
FT /note="C->Y: In ar507; shows endocytic defects."
FT /evidence="ECO:0000269|PubMed:15895077"
FT MUTAGEN 1079
FT /note="W->R: In b1015; shows endocytic defects."
FT /evidence="ECO:0000269|PubMed:15895077"
SQ SEQUENCE 1093 AA; 124005 MW; 8C50161C988EF4B2 CRC64;
MADIIERIRS QDEYREFYEL ATKIRNQKLL TDAELHSLNR HQQEVSDNEI KLLTEAWRSS
YWNNVGRQLK NQALEPTIAC RLLKEISETE ALPAYKHVGH HFSTLDQLLT ILYNEPQSVA
ELLNSIDRND ITSNDSTIQV LFHLVYSCAL YPEDELKIAQ VVCNLLKLQL YRSGSEMRTI
LRKETSISTR FYKHFVELIH PTMVYLTKAL RKGVLDVIQL GSFWLDIDAK QSTARFLRDN
KQNEDRLPEY RALVVSKLVD FVDTFLENIS KALPMLPPNL NWIIRDIFCS LYEVVDDVSA
IELSHACKDM IVSNLICPAI ISPQKFGVVD NDVRVGTIVN HNLVQIAMII QMISLREFES
PPEEYKEFLS QCRNTHLISE MMDALLVEKL APDVEITSLI ANGTAESDMA TKSSFVGTVA
DVNVLIKIIR NAPSTSDAKL SRILSVCDKL PATISSTTQK SHFDNLEASP KISTLRNIHR
KVQHSFKRTG DSFNDINELG AKQGEALAFG KENFDLFYLE YSPKNYKDVA EADRLKKKAE
ERRQLADLEK LLEPTPAPKE TPVENNLIDF SSGSAETNSE HLSDSTSVSP EPLTSTEELQ
IGDQGVGGEQ RGKLAKLKSL SDRMKKGITQ SNTLSDIREH LRRSGSFVKP PPSGIPTSSS
EQNLPDVATG PRDDILAKYA SISSIKEQKP ALGNLIDGTA SASSTPRKEP LEPYYSSENL
VGCRAFQDTL RKMITVLGNI SYLPRIGYRN ETKQNEWDKK VLLGRFLDGV LVETEHRREY
GLAAQLREVK RCIELFEHAG VEILMDHLKL NEAEQDKIVN GMREERASLM RKSNDISSLE
QRVLLNRRLT EQILVDFLMR TFLETGFNNK HTVGKTQEVT AVLKFYDEFK YLRAQDERAE
FLKNLLTFLR DRLMQNVDWN FATDTMMSRA MTTIERYVIF AVYDNAFYPN RDADHHRDKL
LRGTIAKVSD VVTPVNDFLK IPEHLHGEAP WPSAQAELSM LDIYVTAQDK LNCVVRCCDV
INNLVALSSK NAVASADDLT PVLVFVIIKA NPRALLSNVQ FVETFAGDRI ESGRDAYYWV
NFKSAVEYIK TIL
