GenomeNet

Database: UniProt
Entry: A0A9D3T323_MEGAT
LinkDB: A0A9D3T323_MEGAT
Original site: A0A9D3T323_MEGAT 
ID   A0A9D3T323_MEGAT        Unreviewed;      1149 AA.
AC   A0A9D3T323;
DT   03-MAY-2023, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2023, sequence version 1.
DT   10-JUN-2026, entry version 13.
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   ORFNames=MATL_G00151450 {ECO:0000313|EMBL:KAG7467253.1};
OS   Megalops atlanticus (Tarpon) (Clupea gigantea).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Elopiformes; Megalopidae; Megalops.
OX   NCBI_TaxID=7932 {ECO:0000313|EMBL:KAG7467253.1, ECO:0000313|Proteomes:UP001046870};
RN   [1] {ECO:0000313|EMBL:KAG7467253.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=YG-15Mar2019-1 {ECO:0000313|EMBL:KAG7467253.1};
RC   TISSUE=Brain {ECO:0000313|EMBL:KAG7467253.1};
RA   Zahm M., Roques C., Cabau C., Klopp C., Donnadieu C., Jouanno E.,
RA   Lampietro C., Louis A., Herpin A., Echchiki A., Berthelot C., Parey E.,
RA   Roest-Crollius H., Braasch I., Postlethwait J., Bobe J., Montfort J.,
RA   Bouchez O., Begum T., Mejri S., Adams A., Chen W.-J., Guiguen Y.;
RL   Submitted (JAN-2021) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: GTPase activator for the Rho-type GTPases by converting them
CC       to an inactive GDP-bound state. {ECO:0000256|ARBA:ARBA00055252}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KAG7467253.1}.
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DR   EMBL; JAFDVH010000012; KAG7467253.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A9D3T323; -.
DR   OrthoDB; 9994905at2759; -.
DR   Proteomes; UP001046870; Chromosome 12.
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; 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   GTPase activation {ECO:0000256|ARBA:ARBA00022468, ECO:0000256|PROSITE-
KW   ProRule:PRU00172}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP001046870}.
FT   DOMAIN          195..277
FT                   /note="Ras-associating"
FT                   /evidence="ECO:0000259|PROSITE:PS50200"
FT   DOMAIN          364..553
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          589..617
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          726..786
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          800..845
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          868..926
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1007..1083
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        590..599
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        605..616
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        741..750
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        762..786
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        817..841
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        905..917
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1037..1050
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1061..1070
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1149 AA;  126798 MW;  E89E3B5E35BA732F CRC64;
     METMSPQQES TGQSRSASLT GETKICTLPE NKKKMKSLTQ RRQSAPSLVI SKALTKSRTL
     SRENCLSPIS PETCPLVQSF LTPSRTFVTH GHAQLKTGLQ TQERHLFLFN DILLIAKAKS
     STHFKLKAQV RVCEMWTASC MEDVCEGSTN PERSFVMGWP TFNCVATFSS VEQKERWLSF
     IKSRIKEEKE KDDPKTILLK IFAKDIADCA HAKTLTVSHS DCASEVTRMT LQQFGISGSE
     KDYQLWVSSR KDEPPYPLIG HEFPFSIRMS YIRERVSHAT GVKDPITPPD LQGALEQLPM
     DTQCQFILKP SRMATGQSLM EPAQKPLRRK RSFMNWAFWR GSSSQLDGLP VSPTSPAPGR
     LFGLPLSAVC EGGALPKPVM DMLTFLFREG PFTRGIFRRS ASAKACREMR DRLNSGTDSL
     PLTCESIFVI AAVFKDFLRN IPGSLLSQDL YEHWVGVMDQ AGEGEEDRVQ AIQRLVQRLP
     RENQLLLSHM LAVLHCIQRH SHHNQMNSFN LSVCIAPSML WAPAPCNPDM ESEGTKKVSE
     VVRFMIENCC RVLGDSITSL FGGFPQNGSS IDHRSDASAV QLNDSSYDSL ENELNDDTES
     PCQDLRGRKD KQENLSRDSV ITLSDCDLDQ PDPDPAPVQL QLPPLARPRR VTLAVHQPHP
     HAHRDAPQRK SLCPLGARRL RRCSEPAIGH LPLCPAPPPG QHGAVARKTS YDAVTDHVED
     EVFVERLQLD GRAGAGSGGG AEDRRDSRDA PRRRHKQPPP LQLDASCSSL SSPTTSPSGS
     SMSSLDSAFS QFSTDYNVLA PSDGRGGTLR AQGSSTSRSQ ASPVSPASVS PCSLAPVPSL
     STACPREASD WSHHRAADGL HPNTWLKKDH RLSLRQQDRG DWEDTGGSPE RPLISNGSTE
     ALLNGERKAS ELEDLSKRRS SSPPSYPQAL LLQCSKSLFC KGKDKVLTVK ELRQLHDQAA
     TRSSGSDAAP MITSAARSNL PQGVFYGHSS SCLTLQRQKS HSLITAGEVS GRNPAGGRRV
     SEPLVDSCSM GRSSTSDLEK LHRQALDHRG KAPAGRTQQD SCRKGPDAEP LHGSTNQNPE
     PRFCLSPSAT QTVKDYFSLT HTDPDTCLRR SQEVAIAIVQ GKRDWQSRRC SDPRIDDFDQ
     MFFAEESYV
//
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