ID   E3M9Y7_CAERE            Unreviewed;      1088 AA.
AC   E3M9Y7;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   24-JAN-2024, entry version 58.
DE   SubName: Full=CRE-RME-6 protein {ECO:0000313|EMBL:EFO96743.1};
GN   Name=Cre-rme-6 {ECO:0000313|EMBL:EFO96743.1};
GN   ORFNames=CRE_17064 {ECO:0000313|EMBL:EFO96743.1};
OS   Caenorhabditis remanei (Caenorhabditis vulgaris).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=31234 {ECO:0000313|Proteomes:UP000008281};
RN   [1] {ECO:0000313|Proteomes:UP000008281}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PB4641 {ECO:0000313|Proteomes:UP000008281};
RG   Caenorhabditis remanei Sequencing Consortium;
RA   Wilson R.K.;
RT   "PCAP assembly of the Caenorhabditis remanei genome.";
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004170};
CC       Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}.
CC   -!- SIMILARITY: Belongs to the GAPVD1 family.
CC       {ECO:0000256|ARBA:ARBA00008489}.
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DR   EMBL; DS268431; EFO96743.1; -; Genomic_DNA.
DR   RefSeq; XP_003106903.1; XM_003106855.1.
DR   AlphaFoldDB; E3M9Y7; -.
DR   STRING; 31234.E3M9Y7; -.
DR   EnsemblMetazoa; CRE17064.1; CRE17064.1; WBGene00060153.
DR   eggNOG; KOG2319; Eukaryota.
DR   HOGENOM; CLU_012490_0_0_1; -.
DR   InParanoid; E3M9Y7; -.
DR   OMA; ELSHACK; -.
DR   OrthoDB; 20678at2759; -.
DR   Proteomes; UP000008281; Unassembled WGS sequence.
DR   GO; GO:0045334; C:clathrin-coated endocytic vesicle; IEA:EnsemblMetazoa.
DR   GO; GO:0005769; C:early endosome; IEA:EnsemblMetazoa.
DR   GO; GO:0005886; C:plasma membrane; IEA:EnsemblMetazoa.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0031267; F:small GTPase binding; IEA:EnsemblMetazoa.
DR   GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR   GO; GO:0018996; P:molting cycle, collagen and cuticulin-based cuticle; IEA:EnsemblMetazoa.
DR   GO; GO:0043547; P:positive regulation of GTPase activity; IEA:EnsemblMetazoa.
DR   GO; GO:2000369; P:regulation of clathrin-dependent endocytosis; IEA:EnsemblMetazoa.
DR   Gene3D; 1.20.1050.80; VPS9 domain; 1.
DR   InterPro; IPR041545; DUF5601.
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:SF25; GTPASE-ACTIVATING PROTEIN AND VPS9 DOMAIN-CONTAINING PROTEIN 1; 1.
DR   PANTHER; PTHR23101; RAB GDP/GTP EXCHANGE FACTOR; 1.
DR   Pfam; PF18151; DUF5601; 1.
DR   Pfam; PF00616; RasGAP; 1.
DR   Pfam; PF02204; VPS9; 1.
DR   SMART; SM00167; VPS9; 1.
DR   SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR   SUPFAM; SSF109993; VPS9 domain; 1.
DR   PROSITE; PS50018; RAS_GTPASE_ACTIV_2; 1.
DR   PROSITE; PS51205; VPS9; 1.
PE   3: Inferred from homology;
KW   Endocytosis {ECO:0000256|ARBA:ARBA00022583};
KW   Guanine-nucleotide releasing factor {ECO:0000256|ARBA:ARBA00022658};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008281}.
FT   DOMAIN          101..355
FT                   /note="Ras-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50018"
FT   DOMAIN          950..1088
FT                   /note="VPS9"
FT                   /evidence="ECO:0000259|PROSITE:PS51205"
FT   REGION          525..622
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        525..551
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1088 AA;  123769 MW;  4A42CDA1115BCA8C CRC64;
     MSEAIERIRS QDEYRQFYEL ATKIRNQKLL ADAELNSLNR HKQEVADIEI KLLTEAWRSS
     YWNNVGRQLK NQSLEPNIAC RLLKEINDTE AQPAYKHVGH HFSTLDQLLT VLYKEPSTVA
     ELLNNFDQND VSSNDAIIQV FFHLVYSCGL YPEDELKIAQ VVCYLLKLQL LKSGTHMRTM
     LRKETSMSTR FYKHFVELMH PTMVYLTKAL RKGVLDVIQL GSFWLDIDVK QSTTRFIRDG
     KQDQNRFPEY RAMVVSKLVY FVDTFLEQIY LALPMLPPNL NWIIREIFCS LYELVDDISA
     IELSHACKDM IVSNLICPAI ISPQKCGVVD NDVRIGNIVN HNLVQIAMII QMISLREFES
     PPEEYKEFLS QCRNTHLISE MMDALLIEKL APDVEITSLI ANGLAVSDMQ TKSSFVGSVA
     DVNVLTKMIR STPATTNNNI ERIVAICEKL PETLASTIQK SNVENAEESP KVSTLRNIHR
     KVQQSLKRTG DSFYDAMEVK NEEGGVFGKE NFDLFFLDYS SENYMEASEM ERRKNEAKER
     RRREETERLL LDTPTTSEPA PAAQPPATKE DLIDFSASTV TDDPTSISPE PAADESKGVE
     TSPESTQATE AGGRLAKLKS LSDRMKKGIT QSNTLSDIRG HLRRSGSLIK PGMVTSASDQ
     NLPDAANVPR DDILAKYASI SSIKQEKPPL TKLISDNKSS ARSEVTEPYY SPENLVSCRA
     FKDTLRKMVT VLGNVSYLPR IGYRNETKDT SVGRKELLNK FLDGVLVETE HRREYGQAAQ
     LREVKRCIEL FENAGVEILI EHLKLNEIEQ ADVVNVMREE RATLMRKSND IVSLEQRVLL
     NRRLTEQNLV DFLMRTFLET GFHTKHAVAK TPEVAAVLKF YDEFKYLQAN DERAEFLKNL
     LAYLKDRLMQ NVDWNYATDT MLDRAMTTIE RYVMFAVYDT AFHPNKEAET HRDKLLKNTI
     AKVANVVTPV NDFLKIPEHL HGEAPWPSAQ AELSMLDIYV TAQDKLNCVV RCCDVINNLV
     ALSSKNAVAS ADDLTPVLVF VIIKANPRAL LSNLQFIETF AGDRIESGRD AYYWVNFKSA
     VEYIKTIL
//