ID A0A3Q1GJF3_9TELE Unreviewed; 1459 AA.
AC A0A3Q1GJF3;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=GTPase activating protein and VPS9 domains 1 {ECO:0000313|Ensembl:ENSAPOP00000017530.1};
OS Acanthochromis polyacanthus (spiny chromis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Acanthochromis.
OX NCBI_TaxID=80966 {ECO:0000313|Ensembl:ENSAPOP00000017530.1, ECO:0000313|Proteomes:UP000257200};
RN [1] {ECO:0000313|Ensembl:ENSAPOP00000017530.1}
RP IDENTIFICATION.
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 Ensembl; ENSAPOT00000026828.1; ENSAPOP00000017530.1; ENSAPOG00000020869.1.
DR GeneTree; ENSGT00940000156611; -.
DR Proteomes; UP000257200; Unplaced.
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:UP000257200}.
FT DOMAIN 144..352
FT /note="Ras-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50018"
FT DOMAIN 1319..1459
FT /note="VPS9"
FT /evidence="ECO:0000259|PROSITE:PS51205"
FT REGION 450..504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 572..606
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 734..869
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 882..966
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 989..1095
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 450..472
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 485..504
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 572..590
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 737..773
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 846..861
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 882..897
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 944..966
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 991..1011
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1014..1028
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1058..1072
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1073..1094
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1459 AA; 162275 MW; 0718607E85B7E01D CRC64;
MVKPDIHTLA HHLKQERLYV GSEKQLIQRL NSDVLKTAER LYRAAWIAKQ QRINLDRLIL
TSAEASPAEC CQHAKMLEDT QFIDGYKTLG FQETIYGEFL ARLRENPRLV ASCLVAGERL
NQEHTPGVIH TVFTSLYGNC IMQEDESYLL QVLRYLVEFE LKESDNPRRL LRRGTCAFSI
LFKLFSEGLY SAKLFLTATL HEPIMQLLVE DEDHLETDPA KVTERLTPAQ QERFGEKGSE
GYKQRVQAAV EANEAKLVAL VNKFIGYLKQ NTYCFPHSLR WIVSQMYKTL SCVERLEVGE
VRTMCTDLLL TCFICPAIVN PEQYGIISDA PINEVARFNL MQVGQLLQQL AMADDDADPR
RKSSLSKFDK SCVAAFLDVV IGGRAVETPP MSSMNLLEGL SRTVVYITHN QLLALVDFVR
SVMAGDHLRE EEHMALETLL ANVPQSRTVK SNSLELTPSN TPQLSPATTP ANKKNRLPIA
AARSRSRTNI AQEGEAEASS QESLQELMPE EVLVISLGTG PQTVPGMMSE NEVLNLQMAD
GAQGDGHADD TKLHGKPDKT LRFSLCSDNL EGISEGPSNR SNSVSSLDLE GESVSELGAG
PSGSNGVEAL QLLEHEQATT QDNLDDKLRK FEIRDMMGLT DDRDISETVS ETWSTDVLGS
DFDPNMDEDR LQEIAGAAAE NMLGSLLCLP GSGSVLLDPY GSTISETTSE AWSVEVLPSD
SEAPDLKQEE RLQELESCSG VGSTSDDTEV REVSSRPSTP GLSVVSGISA TSEDIPNKIE
DLRSECSSDF GGKDSVTSPD GEESGHGAHH LTSPPSQADS LLAMFDPLSS GEGSSTGTIV
RPKVHYARPP HPPPDPPIPE ASALGPETRH SLFTPHCLAQ AELEHTKQRH SFPDRLVRSR
SSDIVCPGRR PTSDPGLNRR VAVEERDPAG AFALGPSSSP SKDSLKGEVE DRKDSDDEKS
DRNRPWWKKR FVSAIPKVLY WTAESDVPAP IAAFRKRDKP EKDDIAQERI PQDDPLPRQS
SQTQAAEDIL DKYRNIKRTS PSDGATAGAS YDGTGDLCVE DSVHDSPRED TLQNISTDDL
PDSASQTAQQ HDSKFSFSDA KKKLRLALCS ADSVALPIMA PVATRNGLPD HMDPEDNEIV
CFLKVQLAEA INLQDKNQMA QIQETTRCVS RFDPRTCRKL LAAIAEDYRK RAPYIAYLTR
CRQGLQTSQA HLERLLQRVL RDKEVANRYF TTVCVRLLLE HMESKMLDFI KAFQVCTAAD
DKTAAVEDFL RYLYGAMARD AIWQYASEDQ LQDAQMAIER SVMNRIFKLA FYPNQDGDIL
RDQLFHEHIQ RLSKVVTANH KALQIPEVYL KEAPWPSAQS EIRTINAYKT PRDKVQCILR
MCSTIMNLLS LANEDSVPGA DDFVPVLVFV LIRANPPCLL STVQYINNFY ASRLSGEECY
WWMQFTAAVE FIKTIDDRK
//