ID A0A3R7Q2D9_PENVA Unreviewed; 1211 AA.
AC A0A3R7Q2D9;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE SubName: Full=Rho GTPase-activating protein {ECO:0000313|EMBL:ROT66713.1};
GN ORFNames=C7M84_015263 {ECO:0000313|EMBL:ROT66713.1};
OS Penaeus vannamei (Whiteleg shrimp) (Litopenaeus vannamei).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC Malacostraca; Eumalacostraca; Eucarida; Decapoda; Dendrobranchiata;
OC Penaeoidea; Penaeidae; Penaeus.
OX NCBI_TaxID=6689 {ECO:0000313|EMBL:ROT66713.1, ECO:0000313|Proteomes:UP000283509};
RN [1] {ECO:0000313|EMBL:ROT66713.1, ECO:0000313|Proteomes:UP000283509}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Muscle {ECO:0000313|EMBL:ROT66713.1};
RA Zhang X., Yuan J., Li F., Xiang J.;
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ROT66713.1, ECO:0000313|Proteomes:UP000283509}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Muscle {ECO:0000313|EMBL:ROT66713.1};
RA Sun Y., Gao Y., Yu Y.;
RT "The decoding of complex shrimp genome reveals the adaptation for benthos
RT swimmer, frequently molting mechanism and breeding impact on genome.";
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
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:ROT66713.1}.
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DR EMBL; QCYY01002901; ROT66713.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3R7Q2D9; -.
DR Proteomes; UP000283509; Unassembled WGS sequence.
DR GO; GO:0005543; F:phospholipid binding; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR041681; PH_9.
DR InterPro; IPR001605; PH_dom-spectrin-type.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR PANTHER; PTHR23175; PDZ DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR23175:SF23; PDZ DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF15410; PH_9; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR PRINTS; PR00683; SPECTRINPH.
DR SMART; SM00233; PH; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000283509}.
FT DOMAIN 54..162
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 259..451
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 169..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 461..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 593..666
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 764..786
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 866..1106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..226
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 464..485
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 593..619
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 640..666
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 871..892
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 894..909
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 910..951
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 952..1058
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1059..1092
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1211 AA; 134073 MW; B52CCAE3EDF08383 CRC64;
MSSAYDIMVN GSRGEGLEGV VADGGVVSRV GTPVTPGGPL CVGDLPSPAS LQSAILRQGS
LHVKLTMVDG KRAGDRSWKT VWAVVQGHAL IFYKDRQHAL QTPLGVEDQI SLRGAEVEVA
SDYTKRRNVL RLATPGGSQL LLQADTPPEM LAWLSTLQNN CAIQEGEACS KTPMNNNNVS
PQTSNKAMRK LTSSLRTRSP TGQSPSTKTR KPSSVESNSS PKSKTWRGNL VRPFMKKIQG
GSPAITPTTP HPEGATIGVC LEDCPQSEEN EFVPLLVALC VSVVETRGLQ TQGIYRIPGN
KAAVTHLTEM INKGPKAIDY SDPRWSDVNV ISSMLKQFFQ KLPDPLFTCD LYPLFIEASK
IEDPNQRLME LRRLVQELPD HHYETLRFLM LHLSHIVSNS ESNKMDVRNL AIVFGPTLVR
SGDDNMITMV TDMSHQCKIV ETLIGQAAWF FNDDDGEEVI PPSLSPSVLQ SSASDSLSPT
MEPETPSSQA LLLHNIQKVE GAKGDLKKDI VSSIISAANR KVHKVKYKKP VDDKPVDDIK
YSDKEGGFEE RDIDKEAELR KQRLLAKQIE SMVELPDPKP MSERKISNMS LMSVHGHPSS
MSSLTQSSER TSASEQGKHS LPEQDGRLFC VIKKDALSSS TPPPPGSSSV IAPSCQQSSQ
LTTPETSSLF GDEVAIRSYA GLSASTQERI RRFEMETRAM LHRDLTKHRR ETERRDVERR
RLEELWQRAK QDMESEDILD QLADNPTEVV RKISDYSWRL QGLSESMGGD QGSLTSQSSS
TSSQTGLISA ALSHHPLSNT SLTPTTNATT QVINGPEMGM PRCGSLDSLR DGSHIPHDDG
SDLLSAITAT FEEKMRSLQE SPLGLVTPLS EDATPSPSTS PEAGQPNDCT TRGKSECRLY
RDPSLHRRRT NPRNPSANTS TNSTAVNTTP TTTISQVEDA SPSVKLSEGS NKLNEDVTRE
VKVKRSDSLT KSEKTENNLK EKTEKRAREL KRTDTQESLN EKKPKEMKRS DGQDGLGRSR
DLPRKSESRE NSTASARRSS DVRSRRHNVK ELKEKFEQNT DSQPSSNPMK SSNSNHYNNI
SSSSNKTSKS SMRRSGYRGH IKRRHTVGGT KDLAKWAWLH SGEMSRSSPR STRLSAWERL
QPLVADERLN TDRSLEAWLA RERIRTSSPD LSRPQQLVLP CDMDDKENLH RRLSVQEAVL
NPLYPVLESH V
//
