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Database: UniProt
Entry: A0A8C7XDG0_9TELE
LinkDB: A0A8C7XDG0_9TELE
Original site: A0A8C7XDG0_9TELE 
ID   A0A8C7XDG0_9TELE        Unreviewed;      1128 AA.
AC   A0A8C7XDG0;
DT   19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2022, sequence version 1.
DT   10-JUN-2026, entry version 21.
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};
OS   Oryzias sinensis (Chinese medaka).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC   Oryzias.
OX   NCBI_TaxID=183150 {ECO:0000313|Ensembl:ENSOSIP00000011925.1, ECO:0000313|Proteomes:UP000694383};
RN   [1] {ECO:0000313|Ensembl:ENSOSIP00000011925.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JAN-2026) 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   AlphaFoldDB; A0A8C7XDG0; -.
DR   Ensembl; ENSOSIT00000012647.1; ENSOSIP00000011925.1; ENSOSIG00000006934.1.
DR   GeneTree; ENSGT00940000154633; -.
DR   Proteomes; UP000694383; Unplaced.
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:UP000694383}.
FT   DOMAIN          195..317
FT                   /note="Ras-associating"
FT                   /evidence="ECO:0000259|PROSITE:PS50200"
FT   DOMAIN          371..559
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50238"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          574..675
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          731..793
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          807..906
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1009..1028
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..21
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        574..584
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        585..594
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        595..604
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        612..623
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        658..668
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        731..749
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        769..793
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        827..841
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        866..906
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1128 AA;  124491 MW;  033000C3A024D43E CRC64;
     METMTPLQGT MGQQRSESLT GENKYLPENK KKMKTLAQRR QSAPSLVISK ALTRSRSTSR
     ETCSMPVSPE SCSLVQGFLA ESAGRLFLGH AQTQLKTGLQ TQERHFFLFN DTLLVAKAKS
     QTHFKVKSQV RVCEMWTANC MEEVCEGSTN PDRSFVMGWP TCNYVATFSS EELKDKWLAL
     INGRISEGKE KDDPKTVPLK IFAKDIGNCA YAKTLAVNNT DTTTDVIRMS LQQFGISSCI
     KDLRLWVNSS KDDPPYPLIG HEFPFCIKMS HIRDGGSCPG GIGRDPMSPT DCPGVLLLDQ
     CLPPDTQCQF ILKPNKVLLS PQELLEPGQH KTFKRKRSLI NWPFWRGSSS QLDGLPLSPT
     FSAAQGRLFG RPLSSVCSAD HGLPKPVMDM LVFLYLEGPY TKGVFRRSAG AKACRELRDR
     LDNGTDNPDI KHQPVFVIAA VLKDFLRNIP GSLLCADLYD QWMDTMEQEG EDQKMEAIQR
     LLPLLPAENL LLLRHLIAVL HCIQGNAQEN QMNAFNLAVC IAPSILCPPA PSTPEMEGEA
     TKKVCELVHF LIENCSGILG DVTSLFRAFC QKSSGSDHGS DVSSFQMNDS SYDSLENELN
     DDPESPYQEQ LPLRDKDKPD SCSRDSVITL SDGDPDPDHD SELTLQLPPQ ARPRKFSPAA
     RQPRARQANC SLQGPRRLRR CSEPALVLAP TASLNSTVAL GETRHQPVRK ASYDASMEGE
     GEEDEVFLEQ ELGRLHLKEE GRDGSEKKAA KVSTCGKRKA KPAPPPPLRL DASCSSLSSP
     ATSPTGSSLS SLDSAFSQYS TDYTVKWPVS QQSPRDSPPQ REATPHLQPS SHPQPTNQTA
     SHGLHPNTWL KRDRRLSLKQ SEDGQSEGSS VGNGTSLLAN NGHSAANQEA GTVKQNCHQR
     SGSPPSYHQA LLQLQRNRTP FYRGTEKAPT VKELRQLHDP PATYRTSKPT SPNNLKLLQS
     EGAQRLAGTG KHVQPPKGIF FGQNATTLIL QRSKSHSLTP PMDVHKLSKT LPRRASEPAK
     VSADSHHSTS LTLDRLPAFK AKCQDARLGL ADSEPHRSAS PFCLSSSSAR AVRDYFCSQG
     QADPEACLRR SQEVVVAIVQ GKEWQSKRCS DPPMEDFEQL FFAEESYV
//
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