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Database: UniProt
Entry: A0A2Y9T815_PHYMC
LinkDB: A0A2Y9T815_PHYMC
Original site: A0A2Y9T815_PHYMC 
ID   A0A2Y9T815_PHYMC        Unreviewed;      1191 AA.
AC   A0A2Y9T815;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Rho GTPase-activating protein 20 isoform X1 {ECO:0000313|RefSeq:XP_023987066.1};
GN   Name=ARHGAP20 {ECO:0000313|RefSeq:XP_023987066.1};
OS   Physeter macrocephalus (Sperm whale) (Physeter catodon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC   Physeteridae; Physeter.
OX   NCBI_TaxID=9755 {ECO:0000313|Proteomes:UP000248484, ECO:0000313|RefSeq:XP_023987066.1};
RN   [1] {ECO:0000313|RefSeq:XP_023987066.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_023987066.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   RefSeq; XP_023987066.1; XM_024131298.3.
DR   AlphaFoldDB; A0A2Y9T815; -.
DR   InParanoid; A0A2Y9T815; -.
DR   OrthoDB; 2964977at2759; -.
DR   Proteomes; UP000248484; Chromosome 16.
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   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; IPR001849; PH_domain.
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; PF00620; RhoGAP; 1.
DR   SMART; SM00233; PH; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000248484}.
FT   DOMAIN          194..283
FT                   /note="Ras-associating"
FT                   /evidence="ECO:0000259|PROSITE:PS50200"
FT   DOMAIN          365..551
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50238"
FT   REGION          1..47
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          675..702
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          934..954
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          981..1012
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1050..1082
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1142..1171
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..26
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        678..692
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1053..1067
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1152..1170
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1191 AA;  132562 MW;  39CAE2B760278295 CRC64;
     MEAMSPQQET LGGQPGRSSS LTGVSRIAGA PGTKKKMKTL AERRRSAPSL ILDKALQKRP
     STKESPSASV DTCAFLSSFL CSNRTLLIDG RVELKRGLQR QERHLFLFND LFIVAKIKYN
     NNFKIKNKIK LSDMWTASCV DEVGEGNTNA LKSFVLGWPT VNFVATFSSP EQKDKWLSLL
     QRYINLEKEK DYPKSIPLKI FAKDIGNCAY SKTITVTNSD TANEVINMSL PMLGITGSER
     EYQLWVNSGK EEAPYPLIGH EYPYGIKMSH LRDTALLTQG SKDSPTPSNF QEPFLMEQLP
     REMQCQFILK PSRLAVAQQL SDSGQKTFKR RRSIINWAFW RGSSTHLDNL PTSPTSPVPG
     QLFGVSLPNI CENDNLPKAV LDMLFFLNQK GPLTKGIFRQ SANVKSCREL KEKLNSGAEV
     QLDCESIFVI ASVLKDFLRN IPGSTFSSDL YDHWVCVMDQ GNDEEKINAV QRLLDQLPRA
     NVILLRYLFG VLYNIEQHSS SNQMTAFNLA VCIAPSILWP PTSSSPELEN EFTKKVSLLI
     QFLIENCCRI FGEEITSLLG EVSVRCDTRE NASADISCFQ LNDSSYDSLE NELNEDVDAP
     CSDLVKKLGQ GSRSMDSVLT LSDYDLDQPE VEGLLTLSDF DLDHSKDEDI QMEQPLESKP
     VNIAVYTKDP LQDHARAPSG MSTPSHLSTT AADAPKSLRR HRRCSEPSYD YLDSKLSYLR
     EFYQKKLRKS SCDAILSKKD ERHLNQNQPL QEEGKTCYKK SLVIGTDIKK NATNKNVKKK
     SLSDNEGNHV KLFPKSKPVA ISMASYSHMS SCEHPRNQTF DTDTSGYSPP HTTDAFKSSR
     RHRRCSEPNI DDQHCKLTYL RGIHSKKQHK ASYEASLLHG EEDYLKRHKS LQMEGQKLIN
     QSLVMGIEVG KTSATNQNTD KVLPPRLNIC SRTSYSSLSS PGTSPSGSSV SSQDSAFSQI
     SEHSVFTPTE TSSPIDCTFQ AQRKQEELSS DFSSSSLISG IPGPSSGQAS GRLAYTKKDS
     VEWHSQMHSV TLHPSTWLRN GVASLKNWSL KKKARAPRPE ENKIGSLKGH TEPPPHASGV
     PEANALHERQ KDMPRRAAEG LGAVQTARWY SSYPSQDSEK HCSSPVSLVE DRLGLCMKSP
     EEGEISGQCS PGTLPHGRSS PSSLTVDHVC SPDSGPTVVC DVEDRHLTKD I
//
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