GAPD1_XENLA
ID GAPD1_XENLA Reviewed; 1452 AA.
AC A2RV61;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=GTPase-activating protein and VPS9 domain-containing protein 1;
GN Name=gapvd1;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acts both as a GTPase-activating protein (GAP) and a guanine
CC nucleotide exchange factor (GEF), and participates in various processes
CC such as endocytosis, insulin receptor internalization or LC2A4/GLUT4
CC trafficking. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}. Endosome {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the GAPVD1 family. {ECO:0000305}.
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DR EMBL; BC133191; AAI33192.1; -; mRNA.
DR RefSeq; NP_001091308.1; NM_001097839.1.
DR AlphaFoldDB; A2RV61; -.
DR SMR; A2RV61; -.
DR BioGRID; 674411; 1.
DR IntAct; A2RV61; 1.
DR GeneID; 100037133; -.
DR KEGG; xla:100037133; -.
DR CTD; 100037133; -.
DR Xenbase; XB-GENE-997392; gapvd1.S.
DR OrthoDB; 944088at2759; -.
DR Proteomes; UP000186698; Chromosome 8S.
DR Bgee; 100037133; Expressed in egg cell and 19 other tissues.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032794; F:GTPase activating protein binding; ISS:UniProtKB.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISS:UniProtKB.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0043087; P:regulation of GTPase activity; IEA:InterPro.
DR GO; GO:0051223; P:regulation of protein transport; ISS:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 1.10.506.10; -; 1.
DR Gene3D; 1.20.1050.80; -; 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; PTHR23101; 1.
DR Pfam; PF18151; DUF5601; 1.
DR Pfam; PF00616; RasGAP; 1.
DR Pfam; PF02204; VPS9; 1.
DR SMART; SM00167; VPS9; 1.
DR SUPFAM; SSF109993; SSF109993; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR PROSITE; PS50018; RAS_GTPASE_ACTIV_2; 1.
DR PROSITE; PS51205; VPS9; 1.
PE 2: Evidence at transcript level;
KW Endocytosis; Endosome; GTPase activation;
KW Guanine-nucleotide releasing factor; Membrane; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..1452
FT /note="GTPase-activating protein and VPS9 domain-containing
FT protein 1"
FT /id="PRO_0000324773"
FT DOMAIN 131..353
FT /note="Ras-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00167"
FT DOMAIN 1312..1452
FT /note="VPS9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00550"
FT REGION 445..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 571..611
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 735..816
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 885..912
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 929..974
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1037..1063
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 446..470
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 576..595
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 738..775
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 931..947
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 948..972
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1452 AA; 162630 MW; ECA144B5AB494711 CRC64;
MVKPDIHTLA HHLKQERLYV NSEKQLIQRL NADLLKTAER LYRTSWIAKQ QRINLDRLIL
TSAEASPAEC CQHAKVLEDT QFVDGYKQLG FQETAYGEFL NLLRENPRLI ASCLVTGEKL
NQENAQSVIH TVFTSLYGNC IMQEDESYLL QVLRYLIEFE LKESDNPRRL LRKGTCAFSI
IFKLFSEGLF SAKLFLTATL HEPIMQLLVE DEDHLETDPA KLIERFSPAQ QEKLFGGKGT
EAFRQRVQAM VETNEAKLVA LVNKFIGYLK QNTYCFPHSL RWIVSQMFKT LSCVEGLEVS
EVRSMCTDLL LTCFICPAIV NPEQYGIISD APINEVARFN LMQVGRLLQQ LALTGFEERD
SRNKSNLNKF DKSCVAAFLD VVIGGRAVET PPLSSVNLLE GLSRTVVYMT YSQLMSLLGF
MRTVISSEQL QEEDRMALEN LLATVPQTKP GKSNNDTPYS TPQLSPATTP ACKKNRLPIV
TRSRSKTNLM ETENECSPQE VTPNQPEEVL VISLGTGPQL TPGMMSENEV LNMQLVDGGQ
GDVPVDESKL HGKPDKTLRF SLCSDNLEGI SEEEENPCST GPSNRSNSVS SLDLEGESVS
ELGGGPSGSN GVEALQLLEH EQATTQDNLD DKLRKFEIRD MMGLTDDRDI SETVSETWST
DVLGSDFDPN IDEDRLQEIA GAAAENMLGS LLCLPGSLLL DPCTISETTS EAWSVEVLPS
DSAPDLKQEE RLHELESCSG LGSTSDDTEV REVSSRPSTP GLSVVSGISA TSEDIPNKTE
DLRSECSSDF GGKDSVTSPE AEESVHGPHH ITTPPTQSES LLAMFDPLAP ASSEVVRPKV
HYARPSHPPP DPPVLEGASG GNEARLPMFC SHVFIHTDSE AYRQRHSCPE RLVRSRSSDI
ASSIRRPISD PGWVRRGINE DRELLTGTAV NALINPPQSS SFSPSKDSSR GEPDEKKDSD
DERSDRNKPW WKKRFVSAMP KAPIPFRKKE KQEKEREDFV QDRFYVAVDS TSQLGPHSQA
AEDILAKYRN AIKRTIPNEG STMPYEGADP VGDGESLHES PRDEALQNMT SDDLLDSANQ
VAHPQESAFS YRDAKKKLRL ALCSADSVAF PVLSHSTRNG LPDHTDPEDN EIVCFLKVQL
AEAINLQDKN LMAQIQETMR CVSRFDSRSC SKILSSLAED YRKRASYIAY LTRCRQGLQS
TQAHLDRLLQ RVLRDKEVST RYFTTVCVRL LLESKENEIH EFIQDFQKLT AADDKTAQVE
EFLQSLYGAM AQDVIWQNAS EEQLQDAQIA IERSIMNRIF KLAFNPNQDA DILRDQVLHE
HIKRLSKVVT ANHRALQIPE VYLREAPWPS AQTEIRTISA YKTPRDKVQC ILRMCSTIMN
LLSLANEYSV PGADDFVPVL VFVLIKANPT YLLSTVQYIS SFYSNRLIGE ESYWWMQFTA
AVEFIKTIDD RK
