ID A0A1V4J715_PATFA Unreviewed; 1448 AA.
AC A0A1V4J715;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 08-NOV-2023, entry version 20.
DE SubName: Full=GTPase-activating protein and VPS9 domain-containing protein 1 isoform C {ECO:0000313|EMBL:OPJ67587.1};
GN Name=GAPVD1 {ECO:0000313|EMBL:OPJ67587.1};
GN ORFNames=AV530_001869 {ECO:0000313|EMBL:OPJ67587.1};
OS Patagioenas fasciata monilis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Patagioenas.
OX NCBI_TaxID=372326 {ECO:0000313|EMBL:OPJ67587.1, ECO:0000313|Proteomes:UP000190648};
RN [1] {ECO:0000313|EMBL:OPJ67587.1, ECO:0000313|Proteomes:UP000190648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BTP2013 {ECO:0000313|EMBL:OPJ67587.1};
RC TISSUE=Blood {ECO:0000313|EMBL:OPJ67587.1};
RA Soares A.E., Novak B.J., Rice E.S., O'Connell B., Chang D., Weber S.,
RA Shapiro B.;
RT "Band-tailed pigeon sequencing and assembly.";
RL Submitted (FEB-2016) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OPJ67587.1}.
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DR EMBL; LSYS01008925; OPJ67587.1; -; Genomic_DNA.
DR Proteomes; UP000190648; Unassembled WGS sequence.
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:UP000190648}.
FT DOMAIN 188..397
FT /note="Ras-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50018"
FT DOMAIN 1308..1448
FT /note="VPS9"
FT /evidence="ECO:0000259|PROSITE:PS51205"
FT REGION 488..549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 585..606
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 618..652
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 756..842
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 863..1012
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1047..1082
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 489..533
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 618..636
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 758..794
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 823..842
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 928..942
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 943..967
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 979..999
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1048..1062
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1068..1082
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1448 AA; 161232 MW; C71403C5C012B40F CRC64;
MARRGRGDVL EVSMVTGPER AWPGAAAGTG ALAGGRCGTR SLPKMVKLDI HTLAHHLKQE
RLYVNSEKQL IQRLNADVLK TAEKLYRTAW ISKQQRINLD RLIITSAEAS PAECCQHAKV
LEDTQFVDGY KQLGFQETAY GEFLNRLREN PRLIASCLVA GEKLNQDNTQ SVIHTVFTSI
YGNCIMQEDE SYLLQVLRYL IEFELKESDN PRRLLRRGTC AFSILFKLFS EGLFSAKLFL
TATLHEPIMQ LLVEDEDHLE TDPNKLIERF SPVQQEKLFG EKGTEKFRQR VQEMVDSNEA
KLVTLVNKFI GYLKQNTYCF PHSLRWIVSQ MYKTLSCVDR LEVGEVRAMC TDLLLACFIC
PAIVNPEQYG IISDAPINEV ARFNLMQVGR LLQQLAMTGS EEGDPRTKGS LAKFDKSCVA
AFLDVVIDGR AVETPPMSPV NLLEGLSRTV VYVTHSQLTA LVGFMRNVMS SDQLKEDRMA
LENLLANLPQ NKPGKSSSLE MTPYNTPQLS PATTPANKKN RLPIATRSRS RSNIQMDQHG
EHEGCSQEPV PAAQAEEVLV ISLGTAPQVT PGMMSENEVL NMQLADGGQG DVPVDENKLH
GKPDKTLRFS LCSDNLEGIS EGPSNRSNSV SSLDLEGESV SELGAGPSGS NGVEALQLLE
HEQATTQDNL DDKLRKFEIR DMMGLTDDRD ISETVSETWS TDVLGSDFDP NIDEDRLQEI
AGSTISETTS EAWSVEVLPS DSEAPDLKQE ERLQELESCS GLGSTSDDTE VREVSSRPST
PGLSVVSGIS ATSEDIPNKI EDLRSECSSD FGGKDSVTSP DMDETAHGAS QLTSPPSQTD
SLLALFDPLS SNEGVSAVVR PKVHYARPSH PPPDPPILEG AMGERLVRSR SSDIVSSVRR
PMSDPGWNRR PGNEERELPM PSAGAAVLAA ASQSSSSSPS KDSSRGETED RKDSDDEKSD
RNKPWWRKRF VSAMPKAPIP FRKKEKQEKD KDDMVPDRYP ALQDDPSPRV SAQAQAAEDI
LDKYRNAIKR TSPSEGAIAN YDSAEALGDG ESVHDSPRDE ALQNMSADDL PDSASQVAQP
QSSAFSYRDA KKKLRLALCS ADSVAFPMLT HSTRNGLPDH TDPEDNEIVC FLKVQLAEAI
NLQDKNLMAQ LQETMRCVSR FDNRTCRKLL ASIAEDYRKR APYIAYLTRC RQGLQTTQAH
LERLLQRVLR DKEVANRYFT TVCVRLLLES KEKKIREFIQ DFQKLTAADD KTAQVEDFLQ
FLYGAMAQDA IWQNASEEQL QDAQLAIERS VMNRIFKLAF YPNQDGDILR DQVLHEHIQR
LSKVVTANHK ALQIPEVYLR EAPWPSAQSE IRTISAYKTP RDKVQCILRM CSTIMNLLSL
ANEDSVPGAD DFVPVLVFVL IKANPPCLLS TVQYISSFYA NCLSGEESYW WMQFTAAVEF
IKTIDDRK
//
