GAPD1_BOVIN
ID GAPD1_BOVIN Reviewed; 1413 AA.
AC A5D794;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=GTPase-activating protein and VPS9 domain-containing protein 1;
GN Name=GAPVD1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Ascending colon;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (APR-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. Acts as a GEF for the Ras-related protein RAB31 by
CC exchanging bound GDP for free GTP, leading to regulate LC2A4/GLUT4
CC trafficking. In the absence of insulin, it maintains RAB31 in an active
CC state and promotes a futile cycle between LC2A4/GLUT4 storage vesicles
CC and early endosomes, retaining LC2A4/GLUT4 inside the cells. Upon
CC insulin stimulation, it is translocated to the plasma membrane,
CC releasing LC2A4/GLUT4 from intracellular storage vesicles. Also
CC involved in EGFR trafficking and degradation, possibly by promoting
CC EGFR ubiquitination and subsequent degradation by the proteasome. Has
CC GEF activity for Rab5 and GAP activity for Ras (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with TRIP10/CIP4. Interacts with RAB5A (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}. Endosome {ECO:0000250}. Note=Recruited to the
CC plasma membrane by TRIP10/CIP4 in response to insulin. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the GAPVD1 family. {ECO:0000305}.
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DR EMBL; BC140474; AAI40475.1; -; mRNA.
DR RefSeq; NP_001095990.1; NM_001102520.1.
DR AlphaFoldDB; A5D794; -.
DR SMR; A5D794; -.
DR STRING; 9913.ENSBTAP00000015341; -.
DR PaxDb; A5D794; -.
DR PRIDE; A5D794; -.
DR Ensembl; ENSBTAT00000015341; ENSBTAP00000015341; ENSBTAG00000011544.
DR GeneID; 539646; -.
DR KEGG; bta:539646; -.
DR CTD; 26130; -.
DR VEuPathDB; HostDB:ENSBTAG00000011544; -.
DR VGNC; VGNC:29250; GAPVD1.
DR eggNOG; KOG2319; Eukaryota.
DR GeneTree; ENSGT00940000156611; -.
DR HOGENOM; CLU_002165_1_0_1; -.
DR InParanoid; A5D794; -.
DR OrthoDB; 944088at2759; -.
DR TreeFam; TF105908; -.
DR Proteomes; UP000009136; Chromosome 11.
DR Bgee; ENSBTAG00000011544; Expressed in neutrophil and 112 other tissues.
DR ExpressionAtlas; A5D794; baseline and differential.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0030139; C:endocytic vesicle; IBA:GO_Central.
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:0031267; F:small GTPase binding; IBA:GO_Central.
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..1413
FT /note="GTPase-activating protein and VPS9 domain-containing
FT protein 1"
FT /id="PRO_0000324770"
FT DOMAIN 131..353
FT /note="Ras-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00167"
FT DOMAIN 1273..1413
FT /note="VPS9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00550"
FT REGION 448..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 540..587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 718..799
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 826..852
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 871..957
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1011..1049
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..571
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 719..755
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 935..957
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1013..1027
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1031..1047
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 227
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14C86"
FT MOD_RES 390
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14C86"
FT MOD_RES 458
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14C86"
FT MOD_RES 466
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14C86"
FT MOD_RES 470
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14C86"
FT MOD_RES 721
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PAR5"
FT MOD_RES 725
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14C86"
FT MOD_RES 736
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14C86"
FT MOD_RES 741
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14C86"
FT MOD_RES 745
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14C86"
FT MOD_RES 856
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14C86"
FT MOD_RES 882
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14C86"
FT MOD_RES 883
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14C86"
FT MOD_RES 888
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PAR5"
FT MOD_RES 946
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14C86"
FT MOD_RES 972
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14C86"
FT MOD_RES 999
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PAR5"
FT MOD_RES 1031
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14C86"
SQ SEQUENCE 1413 AA; 157375 MW; 364CC73149F88C28 CRC64;
MVKLDIHTLA HHLKQERLYV NSEKQLIQRL NADVLKTAEK LYRTAWIAKQ QRINLDRLII
TSAEASPAEC CQHAKILEDT QFVDGYKQLG FQETAYGEFL SRLRENPRLI ASSLVAGEKL
NQENTQSVIY TVFTSLYGNC IMQEDESYLL QVLRYLIEFE LKESDNPRRL LRRGTCAFSI
LFKLFSEGLF SAKLFLTATL HEPIMQLLVE DEDHLETDPN KLIERFSPAQ QEKLFGEKGS
DRFRQKVQEM VDSNEAKLVA LVNKFIGYLK QNTYCFPHSL RWIVSQMYKT LSCVDRLEVG
EVRAMCTDLL LACFICPAVV NPEQYGIISD APINEVARFN LMQVGRLLQQ LAMTGSEEGD
PRTKSSLGKF DKSCVAAFLD VVIGGRAVET PPMSSVNLLE GLSRTVVYIT YSQLITLVNF
MKSVMSGDQL REDRMALDNL LANLPQAKPG KSSSLEMTPY STPQLSPAAT PANKKNRLPI
ATRSRSRTNV LMDLHMDHEG SAQETIQEVQ PEEVLVISLG TGPQLTPGMM SENEVLNMQL
SDGGQGDVPV DENKLHGPSN RSNSVSSLDL EGESVSELGA GPSGSNGVEA LQLLEHEQAT
TQDNLDDKLR KFEIRDMMGL TDDRDISETV SETWSTDVLG SDFDPNIDED RLQEIAGAAA
ENMLGSLLCL PGSGSVLLDP CTGSTISETT SEAWSVEVLP SDSEAPDLKQ EERLQELESC
SGLGSTSDDT DVREVSSRPS TPGLSVVSGI SATSEDIPNK IEDLRSECSS DFGGKDSVTS
PDMDEVTHGA HQLTSPPSQS ESLLAMFDPL SSHEGGASAV VRPKVHYARP SHPPPDPPIL
EGAVGGNEAR LPTFGSHILT PAEMEAFKQR HSYPERLVRS RSSDVVSSVR RPMSDPSWNR
RPGNEERELP PAAAIGATSL VAAPHSSSSS PSKDSSRGET EERKDSDDEK SDRNRPWWRK
RFVSAMPKDD PSPRLSAQAQ VAEDILDKYR NAIKRTSPSE GALANYESAE VMGDGESAHD
SPRDETLQNI SADDLPDSAS QAAHPQDSAF SYRDAKKKLR LALCSADSVA FPVLTHSTRN
GLPDHTDPED NEIVCFLKVQ IAEAINLQDK NLMAQLQETM RCVCRFDNRT CRKLLASIAE
DYRKRAPYIA YLTRCRQGLQ TTQAHLERLL QRVLRDKEVA NRYFTTVCVR LLLESKEKKI
REFIQDFQKL TAADDKTAQV EDFLQFLYGA MAQDVIWQNA SEEQLQDAQL AIERSVMNRI
FKLAFYPNQD GDILRDQVLH EHIQRLSKVV TANHRALQIP EVYLKEAPWP SAQSEIRTIS
AYKTPRDKVQ CILRMCSTIM NLLSLANEDS VPGADDFVPV LVFVLIKANP PCLLSTVQYI
SSFYASCLSG EESYWWMQFT AAVEFIKTID DRK
