ID A0A8C2VQZ0_CHILA Unreviewed; 1156 AA.
AC A0A8C2VQZ0;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 10-JUN-2026, entry version 20.
DE RecName: Full=Rho GTPase-activating protein 20 {ECO:0000256|ARBA:ARBA00070254};
DE AltName: Full=RA and RhoGAP domain-containing protein {ECO:0000256|ARBA:ARBA00078758};
DE AltName: Full=Rho-type GTPase-activating protein 20 {ECO:0000256|ARBA:ARBA00083374};
GN Name=ARHGAP20 {ECO:0000313|Ensembl:ENSCLAP00000017565.1};
OS Chinchilla lanigera (Long-tailed chinchilla) (Chinchilla villidera).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha;
OC Chinchillidae; Chinchilla.
OX NCBI_TaxID=34839 {ECO:0000313|Ensembl:ENSCLAP00000017565.1, ECO:0000313|Proteomes:UP000694398};
RN [1] {ECO:0000313|Ensembl:ENSCLAP00000017565.1}
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 RefSeq; XP_005378111.1; XM_005378054.2.
DR AlphaFoldDB; A0A8C2VQZ0; -.
DR Ensembl; ENSCLAT00000017737.1; ENSCLAP00000017565.1; ENSCLAG00000012051.1.
DR GeneID; 102011293; -.
DR CTD; 57569; -.
DR GeneTree; ENSGT00940000154633; -.
DR OMA; IDDQHCK; -.
DR OrthoDB; 9994905at2759; -.
DR Proteomes; UP000694398; 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:UP000694398}.
FT DOMAIN 158..247
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT DOMAIN 329..515
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 702..748
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 769..812
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 880..919
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 945..975
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1021..1048
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1110..1156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 721..740
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 775..784
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 897..919
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 945..964
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1124..1133
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1147..1156
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1156 AA; 128058 MW; F509ACBF234E1F7D CRC64;
MKTLAERRRS APSLILDKAL QKQPSTRESP SAGVDTCAFL SSFVCPSRTL LIDGRVELKR
GLQRQERHLF LFSDLLVVVK IKYNNNFKIK NKIKLTDMWT ASCVDEVGEV NTNAMKSFVL
GWPTVNFVAT FSSPEQKDKW LFLLQRYINL EKEKDHPKSI PLKIFAKDIG NCAYSKTITV
MNSDTASEVI TMSLRMLGIT GSERDYQLWV NSGKEAAPYP LIGHEFPYGI KMNHLRDTAL
LAQGSKDSAA LSSLQEPFLM EQLPREMQCQ FILKPSRLAA TQHLSDSGQK TVRRRRSIIN
WAFWRGSSTH LDNLPVSPTS PIPGQLFGVS LQDICENDNL PKSVLDMLFF LNRKGPLTRG
IFRQSANVKS CRELKEKLNS GVEVHLDCES IFVIASVLKD FLRNIPGSIF LSDIYDHWVC
VMDQGNDEEK INTIRRLLDQ LPRANVILLR YLFGVLYNIE KNSSTNQMNA FNLAVCVTPS
LIWPPTPSSP ELEHEFTKKV SLLIQFLIEN CCRIFGHEIT SLFGEVSVRC DAKENSSDTS
CVQLNDSSYD SLENELNEDV DAPCSDLVKK LGQGSRSMDS VLTLSDYDID QPEVEGLLTL
NDFDLDCCKD QDIQMKWSPG SKQVNVLVMN RNASLVEHAG ASSGTCTPSY LSTAAAHAPK
SLRRHRRCSE PSIDHQDSKV SYLKEFHQKK LRKSSCDAIL SQKDEDDLKQ TQPLPEEGKT
SSEQSLVTDT DPSRKNATSK NIKKKSLSGN EGNHVKLFIK SKPVAISVAS HSHMSRQDHS
RNQHFDANTS GYSPPHTAGP LKSSRTHRRC SEPNIDEQSC RLTYLRGIYS KKQHKISCEG
GLLQGEEDYL KRHKSLQMEG QKLINQSLVL GIEVGRSSAT HQSTDKVLPP RLNLCPSTSS
SSLSSPGTSP SGSSVSSQDS AFSQISEHSV FTPTETSSPI DCTFQTQKKQ ENPSSDVNTC
SLASQMPGPS VGQASGHLAY AKKDTVEWHS QMHSVTLHPS TWLKNSVASL KNWSLKRKAK
VARPEEKKIN PLKGPLESPP HASDVPETGS LQEIQKDLPV RAAEGLGALQ TAQPCSSGSC
QDSEKHCSSP FSLVESRLKF CVKSYKGEEA EGQCCSGPLP WEEASSSSGT ISDVASPDTG
PTLVSDGGDK HVTKDI
//
