ID A0A8B8AHI7_CRAVI Unreviewed; 1433 AA.
AC A0A8B8AHI7;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 10-JUN-2026, entry version 19.
DE SubName: Full=Rho GTPase-activating protein 20-like isoform X6 {ECO:0000313|RefSeq:XP_022290756.1};
GN Name=LOC111102361 {ECO:0000313|RefSeq:XP_022290756.1};
OS Crassostrea virginica (Eastern oyster).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC Autobranchia; Pteriomorphia; Ostreida; Ostreoidea; Ostreidae; Crassostrea.
OX NCBI_TaxID=6565 {ECO:0000313|Proteomes:UP000694844, ECO:0000313|RefSeq:XP_022290756.1};
RN [1] {ECO:0000313|RefSeq:XP_022290756.1}
RP IDENTIFICATION.
RC TISSUE=Whole sample {ECO:0000313|RefSeq:XP_022290756.1};
RG RefSeq;
RL Submitted (JAN-2026) to UniProtKB.
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DR RefSeq; XP_022290756.1; XM_022435048.1.
DR GeneID; 111102361; -.
DR OrthoDB; 9994905at2759; -.
DR Proteomes; UP000694844; Chromosome 7.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd13319; PH_RARhoGAP; 1.
DR CDD; cd17115; RA_RHG20; 1.
DR FunFam; 2.30.29.30:FF:000217; Rho GTPase activating protein 20; 1.
DR Gene3D; 1.20.900.10; Dbl homology (DH) domain; 1.
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; IPR047887; ARHGAP20_PH.
DR InterPro; IPR047888; ARHGAP20_RA.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH_dom.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR000159; RA_dom.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR PANTHER; PTHR23179:SF3; RHO GTPASE-ACTIVATING PROTEIN 20; 1.
DR PANTHER; PTHR23179; T-CELL ACTIVATION RHO GTPASE ACTIVATING PROTEIN-RELATED; 1.
DR Pfam; PF00788; RA; 1.
DR Pfam; PF22286; RHG20_PH; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50200; RA; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 4: Predicted;
KW GTPase activation {ECO:0000256|ARBA:ARBA00022468, ECO:0000256|PROSITE-
KW ProRule:PRU00172}; Reference proteome {ECO:0000313|Proteomes:UP000694844}.
FT DOMAIN 16..60
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 255..364
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT DOMAIN 410..596
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 76..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 365..410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 664..696
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 723..765
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 830..851
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 955..999
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1037..1297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1347..1433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 674..687
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 755..765
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 970..982
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 984..995
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1049..1058
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1067..1090
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1091..1108
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1138..1162
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1201..1218
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1245..1254
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1255..1267
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1271..1281
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1288..1297
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1365..1377
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1386..1395
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1433 AA; 161726 MW; F897312664445A2C CRC64;
MVDIFNYPEN VQLLSVQRIP DYEKYLSDLL EATDPQHPDY EDLSKAANRA KTMVKEHEDE
LGTNNDQIKM DRIQQRFPND DLQLRENTPP SSRSLSARRK SAPGAVLFKS LGKTRSSSNL
WSNSSMGKKE MDLVNPLRHG GNSQRQFILE GHVEFAQGMQ TQDRYLFLFN DLLLVAKQKS
STTFKLKHRI RVCEIWLATC IYDVSEATLP PDKSFVLGWP VTNVVATFKS VELKELWLNK
LNETIELERM KEANKTVKVK VHSRDLDQTC TLQIDNHTTA KDLLSQCVGK FHITESEASE
CQLWVKTGKE ESPYPLIGHE LPHSIKFSQL RDFAKTDDPM VSLDGMDPEG EGKSAEFILQ
NRLKGSKKQS FDESNKGNKS KSKKSPFNFF KRGKDDKNNN TTPPGKLFGH PLQDVMQEGH
LPKPVLELMK LVITNGPYTK GVFRKSCNVK LAKEIHQKLD EGLDCVNGDT PTLVVGHLLK
EYLRSLPHCL LYEDLYEEWI SLSEEENTPQ KLEKVRSLLN KLPEGHLELL KHLLCVLYHI
DKNNKENMMT SYNLSVCIAP SILWAKQGDD PMRALAMAKS PQQIVEYLIV NCVELFGEDV
IYLFGDLLEH KIRQDSSTDS DSMHSVLSMG DSAIGSFVAF PGGSIIRHDD SSVESLERMY
FDDSSPNLAK SHISPSSLSR DSGLYSSQEN LDNGAKSRVN TTLVKSRSGC HLYFEDEPVS
YPTEINGPIT RINRDRDHRL QRQKSVAEST PPTSPHSKLS YSSLDSSLTD SMSSYLNRQY
SKDTDNSDQW FTAEESFRDS FDSTRECKDD SSINFQRSNS LSATIPKSIQ NIQHLVSPPV
SPRSKRKSSS MDLHLNLSQT KSYPLPRTCF SQEKLSDPTS ARYGQSAMDL SSSNPFKQLS
KYSTPGLGTS PPPHIVLQQH KSVQKPSPNT PMRASYDSAI ISQFEKKDTF KTEMHVTKHV
PTPKSENESD MTLTNNSESP SVSRPEKPPS YDEAVRRKKR IDKGLPLEIL TEQDIQEEKE
KQRRAKSLYI DSINKFEQDT RDESTSSESE SESTEEDVYV SLKNPKKIFE ESLKMYEEQS
SQRRPPHYDN KNVSNVSATN IQRSSSDSAD YMNKVSMVAK HREPSPNYRV PPHHREPSPS
TTRLSHSSSS VSNSSSETVT DSRQSSPNQR ERSESSPVVP RHHFQKTSPM KFKANYAPLD
SAQSSSSIHK EQTVNNPALS RDSRTTKSTP TEVSKSVPKP ELSVHNPSSY STPQTREKRV
VKSHDFVDSP VVSSPRTISQ ESPRKNLTVL SKSRDSTVIS NHRDLYARSS TARNRISASL
ELCNRDSEKS PRKQDLPWSV KSLKQIYDKE GALPSSDNVK DTGVRPPPPP YQPPPPFRRP
DFSRLSQSSQ SSVGSGNTGR STPPIKGLPT HRRSGGPQTF SYRKDQDPDI SYV
//
