RME6_CAEBR
ID RME6_CAEBR Reviewed; 1104 AA.
AC A8WVM4;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Receptor-mediated endocytosis protein 6;
GN Name=rme-6; ORFNames=CBG04130;
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16;
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with GDP-bound rab-5. Interacts with alpha-adaptin
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein.
CC Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the GAPVD1 family. {ECO:0000305}.
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DR EMBL; HE600974; CAP24535.3; -; Genomic_DNA.
DR RefSeq; XP_002643315.1; XM_002643269.1.
DR AlphaFoldDB; A8WVM4; -.
DR SMR; A8WVM4; -.
DR STRING; 6238.CBG04130; -.
DR GeneID; 8585309; -.
DR KEGG; cbr:CBG_04130; -.
DR CTD; 8585309; -.
DR WormBase; CBG04130; CBP46353; WBGene00026865; Cbr-rme-6.
DR eggNOG; KOG2319; Eukaryota.
DR HOGENOM; CLU_012490_0_0_1; -.
DR InParanoid; A8WVM4; -.
DR OMA; SCFLGKK; -.
DR OrthoDB; 944088at2759; -.
DR Proteomes; UP000008549; Chromosome X.
DR GO; GO:0030136; C:clathrin-coated vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0030139; C:endocytic vesicle; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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; IBA:GO_Central.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0043087; P:regulation of GTPase activity; IEA:InterPro.
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 3: Inferred from homology;
KW Cytoplasmic vesicle; Endocytosis; GTPase activation;
KW Guanine-nucleotide releasing factor; Membrane; Reference proteome.
FT CHAIN 1..1104
FT /note="Receptor-mediated endocytosis protein 6"
FT /id="PRO_0000324774"
FT DOMAIN 140..355
FT /note="Ras-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00167"
FT DOMAIN 966..1104
FT /note="VPS9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00550"
FT REGION 663..682
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 664..682
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1104 AA; 125815 MW; B3FB1E9AEAE5D3F3 CRC64;
MSEAVEKIRS HDKYRQFYEL ATKIRNQKLL ADAESASLHR HKQEVADLEV KLLTEAWRSS
YWTNVSRQLK SQSLDPSYAC RLLKEISDTE ALAAYKHFGH HYSTLNQLLT VLYMEPTSVA
ELLNMWDQND VTTNDNLIQT FFHLVYSCGL YPDDELKIAQ VVCYLLKLQL VKSGSQMRTM
LRKETSISTR FYKYFVEQMH PTMVYLTKAL RKSVLNVIQL GNFWLDVDMK QSSSRFLSDG
RQNSERLPEY RALVVSKLVD FVDNFLENIS LALSMLPPNL NWIVRDIFCS LYEIVDDMSA
IELSHACKDM IVSNLLCPAI ISPQKFGVVD NDVRIGSIVN HNLAQIAMII QMISLREFES
PPEEYREFLS QCRNTHLISE MMDSLLVENM APDVEITSLI ASGKSESDLE TKSNFVGSLA
DANKLIKMIR ETPPTTDLKI SRIVSVCQKM PESFASTVEK LHVENSEDSP KLSALRNIHR
KVQKSFKRTG DSFYDPNELH MKTENYGGVF EKENFDRKLR EASEVERRKQ EARKQKQLKE
TELLIMDNIS SDSAPITIKA SAATNAPIAN NNFTENKDLI DFSTLYTTTD DVISIPSEPS
KEEKSVEKPN VNNVSVDAPV EALQIGESRG GLAKLKNFSD RMKKGITQSN TLSDIRDHLR
RSSSLAKQPS GMVSSASAQN IPDTEKGDSI LAKYASNSSI KIEKSTFTKL TDTKSMPKNT
EMSEPYYSPE NLTSCRAFKD TLRKMITVLG NVSYLPKIGC RSEMKEMSKK VRLDSFLDGV
LVETEHRREY GQAAQLREVK RCIELFENEG VEILMDHLVG NEVEQDFLVR QMREERAILM
RKSNDISSME QRVLLNRRLT EQILVDNLIQ TFLETGFQNS KLASGKTPEV VAVGKFYSEF
KFLQAHDERA EFLQNLLTYL RERLMQNYDW NFATESMIAR AMTTMERFVM FAVYEIAFWP
NREMDQKKDK LLQSVIGKAS SSVTPVHEAL KIPEHLLGEA PWPSAQAELS MLDNYVTAQE
KLNCLVRCCD VINNLVALSS KNAVASADDL TPVLVFVIIK ANPRSLLSNL QFIETFAGDQ
IESGRDAYYW VNFKSAVEYI KTIL
