ID A0A3B4XLE3_SERLL Unreviewed; 1475 AA.
AC A0A3B4XLE3;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=GTPase activating protein and VPS9 domains 1 {ECO:0000313|Ensembl:ENSSLDP00000016530.1};
OS Seriola lalandi dorsalis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Carangidae; Seriola.
OX NCBI_TaxID=1841481 {ECO:0000313|Ensembl:ENSSLDP00000016530.1, ECO:0000313|Proteomes:UP000261360};
RN [1] {ECO:0000313|Ensembl:ENSSLDP00000016530.1}
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR STRING; 1841481.ENSSLDP00000016491; -.
DR Ensembl; ENSSLDT00000017088.1; ENSSLDP00000016491.1; ENSSLDG00000013003.1.
DR Ensembl; ENSSLDT00000017127.1; ENSSLDP00000016530.1; ENSSLDG00000013003.1.
DR GeneTree; ENSGT00940000156611; -.
DR Proteomes; UP000261360; 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}.
FT DOMAIN 144..352
FT /note="Ras-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50018"
FT DOMAIN 1335..1475
FT /note="VPS9"
FT /evidence="ECO:0000259|PROSITE:PS51205"
FT REGION 453..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 599..633
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 761..892
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 911..1039
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1051..1111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 599..617
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 764..800
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 971..995
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1008..1031
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1074..1088
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1089..1110
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1475 AA; 163831 MW; DA9575674AB57854 CRC64;
MVKPDIHTLA HHLKQERLYV ASEKQLIQRL NSDVLKTAER LYRAAWIAKQ QRINLDRLIL
TSAEASPAEC CQHAKMLEDT QFIDGYKTLG FQETIYGEFL ARLRENPRLV ASCLVAGERL
NQEHTQGVIH 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 SRTAVYITHN QLLALVDFVR
SVTAGDHLRE EEHMALENLL ANVPQSRTVK SNSLELTPSN TPQLSPATTP ANKKNRLPIG
QHLAAITSWD PTTTTLSAHI PLVTPFAAAR SRSRTNIAQE GEAEASSQES LQELMPEEVL
VISLGTGPQT VPGMMSENEV LNLQMADGAQ GDGHADDTKL HGKPDKTLRF SLCSDNLEGI
SEGPSNRSNS VSSLDLEGES VSELGAGPSG SNGVEALQLL EHEQATTQDN LDDKLRKFEI
RDMMGLTDDR DISETVSETW STDVLGSDFD PNMDEDRLQE IAGAAAENML GSLLCLPGSG
SVLLDPYGST ISETTSEAWS VEVLPSDSEA PDLKQEERLQ ELESCSGVGS TSDDTEVREV
SSRPSTPGLS VVSGISATSE DIPNKIEDLR SECSSDFGGK DSVTSPDGEE SGHGAHHLTS
PPSQADSLLA MFDPLSSGEG SSTGTIVRPK VHYARPPHPP PDPPIPEASA LGQEMRHSLF
TPHCLAQAEL EHTKQRHSFP DRLVRSRSSD IVCPGRRPTS DPGLNRRVAV EERDPAGAFA
LGPSSSPSKD SLKGEAEDRK DSDDEKSDRN RPWWKKRFVS AIPKAPIAAF RKRDKQEKDD
ISQERIPQED PLPRHSSQAQ AAEDILDKYR NIKRPSPSDG AAAGASYDGT GDLCVEDSVH
DSPREDTLQN ISTDDLPDSA SQTAQQHDSK FSFSDAKKKL RLALCSADSV ALPIMAPATT
RNGLPDHMDP EDNEIVCFLK VQLAEAINLQ DKNQMAQIQE TTRCVSRFDA RTCRKLLAAI
AEDYRKRAPY IAYLTRCRQG LQTSQAHLER LLQRVLRDKE VANRYFTTVC VRLLLEHMES
KMLDFIKAFQ GCTAADDKTA AVEDFLRYLY GAMARDAIWQ YASEDQLQDA QMAIERSVMN
RIFKLAFYPN QDGDILRDQL FHEHIQRLSK VVTATHKALQ IPEVYLKEAP WPSAQSEIRT
INAYKTPRDK VQCILRMCST IMNLLSLANE DSVPGADDFV PVLVFVLIRA NPPCLLSTVQ
YINNFYASRL SGEECYWWMQ FTAAVEFIKT IDDRK
//