ID A0A3P9P3Z2_POERE Unreviewed; 1474 AA.
AC A0A3P9P3Z2;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=GTPase activating protein and VPS9 domains 1 {ECO:0000313|Ensembl:ENSPREP00000016552.1};
OS Poecilia reticulata (Guppy) (Acanthophacelus reticulatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=8081 {ECO:0000313|Ensembl:ENSPREP00000016552.1, ECO:0000313|Proteomes:UP000242638};
RN [1] {ECO:0000313|Proteomes:UP000242638}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Guanapo {ECO:0000313|Proteomes:UP000242638};
RA Kuenstner A., Dreyer C.;
RT "The genomic landscape of the Guanapo guppy.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPREP00000016552.1}
RP IDENTIFICATION.
RC STRAIN=Guanapo {ECO:0000313|Ensembl:ENSPREP00000016552.1};
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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 RefSeq; XP_017162306.1; XM_017306817.1.
DR Ensembl; ENSPRET00000016732.1; ENSPREP00000016552.1; ENSPREG00000011087.1.
DR GeneID; 103470617; -.
DR CTD; 26130; -.
DR GeneTree; ENSGT00940000156611; -.
DR OrthoDB; 20678at2759; -.
DR Proteomes; UP000242638; Unassembled WGS sequence.
DR Bgee; ENSPREG00000011087; Expressed in caudal fin and 1 other cell type or tissue.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR CDD; cd05129; RasGAP_RAP6; 1.
DR Gene3D; 1.10.246.120; -; 1.
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:UP000242638}.
FT DOMAIN 144..352
FT /note="Ras-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50018"
FT DOMAIN 1334..1474
FT /note="VPS9"
FT /evidence="ECO:0000259|PROSITE:PS51205"
FT REGION 450..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 563..585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 598..632
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 760..891
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 909..1088
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 598..616
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 763..799
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 873..887
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 970..994
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1007..1026
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1474 AA; 163828 MW; 20F024A9EFC91A2E CRC64;
MVKPDIHTLA HHLKQERLYV ASEKQLIQRL NSDVLKTAER LYRAAWIAKQ QRINLDRLIL
TSVEASPAEC CQHAKMLEDT QFIDGYKTLG FQETIYGEFL ARLRENPRLV ASCLVAGERL
NQEHTQGVIH NVFTSLYGNC IMQEDESYLL QVLRYLVEFE LKENDNPRRL LRRGTCAFSI
LFKLFSEGLY SAKLFLTATL HEPIMQLLVE DEDHLETDPA KVTERLTPAQ QERFGEKGSE
DYKQRVQAAV EANEAKLVAL VNKFIGYLKQ NTYCFPHSLR WIVSQMYKTL SCVEQLEVGE
VRTMCTDLLL TCFICPAIVN PEQYGIISDA PINEVARFNL MQVGQLLQQL AMADDDIDPR
RKSSLSKFDK SCVAAFLDVV IGGRAVETPP MSSMNLLEGL SRTAVYITHS QLLALVDFVR
SVMAGDHLRE EEHMALETLL ANVPHSRTVK SNSLELTPSN TPQLSPATTP ANKKNRLPIG
QHLAAITSWD PSTTTLSAHI PLVTPFAARS RSRTNIAQEG EAEASSQESL QELMPEEVLV
ISLGTGPQTV PGMMSENEVL NLQMSDGPQG DGPADDTKLH GKPDKTLRFS LCSDNLEGIS
EGPSNRSNSV SSLDLEGESV SELGAGPSGS NGVEALQLLE HEQATTQDNL DDKLRKFEIR
DMMGLTDDRD ISETVSETWS TDVLGSDFDP NMDEDRLQEI AGAAAENMLG SLLCLPGSSS
VLLDPYGSTM SETTSEAWSV EVLPSDSEAP DLKQEERLQE LESCSGVGST SDDTEVREVS
SRPSTPGLSV VSGISATSED IPNKIEDLRS ECSSDFGGKD SVTSPDGEES GQGAHHLTSP
PSQADSLLAM FDPLSTGEGS STGTIVRPKV HYARPTHPPP DPPIPEASAM GPDIRHSICT
AQCLAQAELE QSKQRHSFPD RLVRSRSSDI VCPGRRPTSD PGLNRRVAVE ERDPPGAFAA
GPSSSPSKDS LKGEVEDRKD SDDEKSDRNR PWWKKRFVSA IPKAPMTAFR KKDKHEKEDA
AQDRVPQDDP VPRQNTQVQA AEDILDKYRN IKRTSPSDGA TGGASYDGSG ELCVEDNVND
PPREDALQNI SADDLPDSAS QTAQQHDSKF SFSDAKKKLR LALCSADSVA LPIMAPTTTR
NGLPDHMDPE DNEIVCFLKV QLAEAINLQD KNQMAQIQET TRCVSRFDAR TCRKLLAAIA
EDYRKRAPYI AYLTRCRQGL QTSQAHLERL LQRVLRDKEV ANRYFTTVCV RLLLEHMETK
MLEFIKAFQG CTAADDKTAA VEDFLRYLYG AMARDAIWQY ASEDQLQDAQ MAIERSVMNR
IFKLAFYPNQ DGDILRDQLF HEHIQRLSKV VTANHKALQI PEVYLKEAPW PSAQAEIRTI
NAYKTPRDKV QCILRMCSTI MNLLSLANED SVPGADDFVP VLVFVLIRAN PPCLLSTVQY
INNFYASRLS GEECYWWMQF TAAVEFIKTI DDRK
//
