ID A0A8C7CG30_ONCKI Unreviewed; 1138 AA.
AC A0A8C7CG30;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 10-JUN-2026, entry version 19.
DE RecName: Full=Rho GTPase-activating protein 20 {ECO:0000256|ARBA:ARBA00070254};
DE AltName: Full=Rho-type GTPase-activating protein 20 {ECO:0000256|ARBA:ARBA00083374};
GN Name=LOC109869449 {ECO:0000313|Ensembl:ENSOKIP00005003920.1};
OS Oncorhynchus kisutch (Coho salmon) (Salmo kisutch).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Oncorhynchus.
OX NCBI_TaxID=8019 {ECO:0000313|Ensembl:ENSOKIP00005003920.1, ECO:0000313|Proteomes:UP000694557};
RN [1] {ECO:0000313|Ensembl:ENSOKIP00005003920.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSOKIP00005003920.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
CC -!- FUNCTION: GTPase activator for the Rho-type GTPases by converting them
CC to an inactive GDP-bound state. {ECO:0000256|ARBA:ARBA00055252}.
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DR RefSeq; XP_031655130.1; XM_031799270.1.
DR AlphaFoldDB; A0A8C7CG30; -.
DR Ensembl; ENSOKIT00005004106.1; ENSOKIP00005003920.1; ENSOKIG00005001770.1.
DR GeneID; 109869449; -.
DR GeneTree; ENSGT00940000154633; -.
DR Proteomes; UP000694557; Unassembled WGS sequence.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0035023; P:regulation of Rho protein signal transduction; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd13319; PH_RARhoGAP; 1.
DR CDD; cd17115; RA_RHG20; 1.
DR CDD; cd04402; RhoGAP_ARHGAP20; 1.
DR FunFam; 2.30.29.30:FF:000217; Rho GTPase activating protein 20; 1.
DR FunFam; 1.10.555.10:FF:000025; Rho GTPase-activating protein 20; 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; IPR047886; ARHGAP20-like_RhoGAP.
DR InterPro; IPR047887; ARHGAP20_PH.
DR InterPro; IPR047888; ARHGAP20_RA.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR000159; RA_dom.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR23179:SF28; 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; SM00324; RhoGAP; 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 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}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000694557}.
FT DOMAIN 190..286
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT DOMAIN 368..557
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 349..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 568..722
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 759..789
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 829..871
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 888..924
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1030..1072
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 572..583
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 584..593
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 594..603
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 611..624
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 657..669
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 711..722
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 767..789
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 829..838
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 852..864
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1138 AA; 126538 MW; 92C664A85D659357 CRC64;
MELLLGDGNL EDHKRDRSGS CVEFYQVKQM KTLAHRRQSA PSLVISKALT KSRSMSRENC
LSPVCPEKCP LVQAFLSPWR VFLAHAHTQL QTGLQTQERH LFLFTDTLLI AKAKSSTHFK
LKAQVRMCEM WTAGCMEDVC EGTTSPERSF VMGWPTFNCV ATFSSVEHKE KWLSLIKSRI
NEEKEKDDPK TIPLKIFAKD IGNCAYAKTL AVSNSDSTTD VIRMALQLFG ISGCVKDHQL
WMSSYKDDSP YPLIGHEFPF SIKMSHIRNV GAGGDGGKDA IPPPPPEADQ GTMLLDQCLP
PDTQCQFILK PSRVDLRQAP LIEPGQKSVK RKRLLINWAF WRGSSSQLDG VPLSPTSPSP
TPGRLFGRSL SSVCRPDHTL PKPVMDMLVF LYQEGPYTRG IFRRSAGAKA CRELRDRLDN
GTEDTHSLTH ESVFVTAAVF KDFLRNVPGS LLCVDLYEQW IGVMEREEEE EKWLAIHRLV
HLLPSENLLL LRHVVAVLHC IQGNAEDNQM NAFNLSVCIA PSMLWTPAPC SPRGEGEATK
KVCELVRLLI ENCRKVLGDD VTSLFGAFPQ KSNSSDHGSD VSSFQMNDSS YDSLENELNE
DPESPFQESL PLRDKAMPDS HSRDSVITLS DCDPDPDPEA DLLHLPPLPR PRKFTSAVRQ
PQPRQSFVQS HGPRRLRRSS EPALGHTPGA LIVQSDKHSL ASRKASYDAA MEGEEEEGEE
GEDEVFLKQG LRVLQLKDIV VTGGERGGVG TLERRMLKHA PPPPLRLDAS CSSLSSPATS
PTGSSLSSLD SAFSQYSTDY VTSAGFHFAE PSPHSPLSPR FPLSHLFPLS PRLPRSPQGS
PPKRDTVDWI QSHPPHSSRT PSTHHSLHPN TWFKRDRRLS LRQPDNGHLE EEVGEGEGVS
LPKSPEVKGV EVTTKRRSSS PPSYQQAILQ LQGSRSPFYR GTEKPLTVRE LRLLHDQSCK
VTHRPPTGSE VTQPPQGVFY GQSSSTLTLQ RHKSHSLTPA MDASRKVLTM PRRASEPSCL
TDAASSLTLE RPRVKSRTHR VKDQQLPESG LRVSDVEPQR NGAGPNSEPG ICLSPSTTRA
VRDYFSSQGR VDADACLGRS QEVALALVQG KREWQSRKCS DPCVDDFDQM FFAEESYV
//
