ID A0A667X269_9TELE Unreviewed; 1186 AA.
AC A0A667X269;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 10-JUN-2026, entry version 24.
DE SubName: Full=Rho GTPase-activating protein 20-like {ECO:0000313|Ensembl:ENSMMDP00005008073.1};
GN Name=LOC115369635 {ECO:0000313|Ensembl:ENSMMDP00005008073.1};
OS Myripristis murdjan (pinecone soldierfish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Holocentriformes; Holocentridae; Myripristis.
OX NCBI_TaxID=586833 {ECO:0000313|Ensembl:ENSMMDP00005008073.1, ECO:0000313|Proteomes:UP000472263};
RN [1] {ECO:0000313|Ensembl:ENSMMDP00005008073.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Wellcome Sanger Institute Data Sharing;
RL Submitted (JUN-2019) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSMMDP00005008073.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JAN-2026) to UniProtKB.
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DR RefSeq; XP_029922142.1; XM_030066282.1.
DR AlphaFoldDB; A0A667X269; -.
DR Ensembl; ENSMMDT00005008313.1; ENSMMDP00005008073.1; ENSMMDG00005004478.1.
DR GeneID; 115369635; -.
DR GeneTree; ENSGT00940000154633; -.
DR InParanoid; A0A667X269; -.
DR OrthoDB; 9994905at2759; -.
DR Proteomes; UP000472263; Chromosome 2.
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 Gene3D; 3.10.20.90; Phosphatidylinositol 3-kinase Catalytic Subunit, Chain A, domain 1; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW GTPase activation {ECO:0000256|ARBA:ARBA00022468, ECO:0000256|PROSITE-
KW ProRule:PRU00172}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000472263}.
FT DOMAIN 187..307
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT DOMAIN 359..548
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 655..700
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 712..803
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 815..1033
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 443..473
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..13
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..34
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 655..665
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 716..725
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 736..748
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 758..778
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 779..801
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 815..828
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 848..859
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 915..927
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 932..943
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 995..1021
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1186 AA; 130974 MW; ADCEE111EFFD956A CRC64;
MDSMSPQQQQ DNFSRGGGQQ ENKRRIKSVS HRRQSAPSLV ITKALTRSRT LSRESFLLPL
CPETCPLVQS YLACPGRSFL LHAHAQLKTG LQTQDRHLFL FSDIMVIAKA KSANHFKLKA
QACVCEMWTA GCMEEVCEGS TNPDRGFVMG WPTCNCVATF SSAEQKERWL SLLKSRIKEE
KEREEPKTIP LKVYGKGINT YAVTKTLPVS NSDSTNEVIR LALQQFGIPG NVKDYQLWVI
SKRDNTPYPL IGHEFPFSIQ MSHVRDVLSQ AGSSWDTVSS PDRQRALQAE QLQADKRCQF
ILKPRPIATT QHVFAESSQK PFKRRRSLIN WAFWRGSSSQ LNELSMSLSQ AAPGCLFGHP
LSSVCVEDTL PKPVMDMLVF LYHEGSWTRG IFRRPAGTRA VRELRESLDA GLFQLPLTRD
HVFIIAGVFK DFLRSIPGSL LCSEMYEEWM DVLEEEEEEE EEQVQDIKRL IGRLPKENAL
LLRYLIAMLH GIQGNAHDNL MTSLNLSVCI AHSMLWPPGP CSPEVEGAGA KKVCELVKFM
IEHCQQIIGE DPSSLFGGPP QRLDTDEMAS DSWHYSLTDS SYDSLENELD DHSSGTSPAL
HARKVCLKVK PLQGSLDSIL TLSDCDQDTD PDTHHACGKP VKTNCVMLHP FGRTTGRTQG
PNSSLACPKK EAPMVGSSST LDSLALDGRR RQRRRSEPAI AYMTEFRACL SGSNDDLTDE
EEDNDKELSK GPSGHTRTHT HSRAQNRRGG RESGFDLLGG RSLGLKTSTS SLSSDATSPV
PTRTSLDSLD SLGDQTGQTR QGGFCSAKAC LPTSSSSLAI SPPSGSGPTS PPFTPSGLGS
VLDPGGDPDQ RSCPKDSTPK ETLPWGTLKS SGGLHPNSWL KKARRLSLTQ QDNLENEEDT
TGGRSIDKSL CPGKLDPENG RPGEKGRGKQ MFTEQTKAKP STRPTKERGG GQVRARPGQE
PAKSLFPKHD SSSIPAHHRS TGNLQYPKSP CLRPSDSSLQ LTKASQQQAD TGSDVTSQGQ
AAGSDVNEFK QPSEAVFHRQ SGPMLSLFRR QKRHSGVAGL EEECKARLSQ RRASEPGRLV
MDRTSTLYLD GLYRQNVRRR LPSDPGLKVS EVDSQGGTSE PRFCLSPHAT KAVREYFSSH
PRSNPQSGQQ VALALVESHR EWLKRCHDPT AESDFDQLLF AEESYV
//
