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Database: UniProt
Entry: A0A3Q1HVV4_ANATE
LinkDB: A0A3Q1HVV4_ANATE
Original site: A0A3Q1HVV4_ANATE 
ID   A0A3Q1HVV4_ANATE        Unreviewed;       806 AA.
AC   A0A3Q1HVV4;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   02-JUN-2021, sequence version 2.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=Rho GTPase-activating protein 12-like {ECO:0000313|Ensembl:ENSATEP00000013132.2};
OS   Anabas testudineus (Climbing perch) (Anthias testudineus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Anabantaria; Anabantiformes; Anabantoidei; Anabantidae; Anabas.
OX   NCBI_TaxID=64144 {ECO:0000313|Ensembl:ENSATEP00000013132.2, ECO:0000313|Proteomes:UP000265040};
RN   [1] {ECO:0000313|Ensembl:ENSATEP00000013132.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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DR   AlphaFoldDB; A0A3Q1HVV4; -.
DR   Ensembl; ENSATET00000013348.2; ENSATEP00000013132.2; ENSATEG00000009114.2.
DR   GeneTree; ENSGT00950000182860; -.
DR   Proteomes; UP000265040; Unplaced.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   CDD; cd13233; PH_ARHGAP9-like; 1.
DR   CDD; cd04403; RhoGAP_ARHGAP27_15_12_9; 1.
DR   CDD; cd12070; SH3_ARHGAP12; 1.
DR   CDD; cd00201; WW; 1.
DR   Gene3D; 2.20.70.10; -; 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   Gene3D; 2.30.30.40; SH3 Domains; 1.
DR   InterPro; IPR035491; ARHGAP12_SH3.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR000198; RhoGAP_dom.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR001202; WW_dom.
DR   InterPro; IPR036020; WW_dom_sf.
DR   PANTHER; PTHR23176:SF107; RHO GTPASE-ACTIVATING PROTEIN 12; 1.
DR   PANTHER; PTHR23176; RHO/RAC/CDC GTPASE-ACTIVATING PROTEIN; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   Pfam; PF16618; SH3-WW_linker; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   Pfam; PF00397; WW; 1.
DR   SMART; SM00324; RhoGAP; 1.
DR   SMART; SM00456; WW; 2.
DR   SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF50044; SH3-domain; 1.
DR   SUPFAM; SSF51045; WW domain; 2.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
DR   PROSITE; PS50002; SH3; 1.
DR   PROSITE; PS50020; WW_DOMAIN_2; 2.
PE   4: Predicted;
KW   GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW   Reference proteome {ECO:0000313|Proteomes:UP000265040};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}.
FT   DOMAIN          8..70
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          268..295
FT                   /note="WW"
FT                   /evidence="ECO:0000259|PROSITE:PS50020"
FT   DOMAIN          360..387
FT                   /note="WW"
FT                   /evidence="ECO:0000259|PROSITE:PS50020"
FT   DOMAIN          429..535
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          615..804
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50238"
FT   REGION          79..98
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          104..237
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          282..340
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          541..583
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        79..95
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        121..145
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        184..212
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        213..237
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        295..335
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        550..583
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   806 AA;  91824 MW;  959FF1813AE62E56 CRC64;
     MAELPIAPGQ VYIEVEYDYD YKSKDRLVSI RQGECYMLVK KTNEDWWQVK KEEGAKPFYV
     PAQYVREVRK ALMPPPKPIT QLPAASNPPP PGGAALWVKP TNLDVGTRDR SPENLHGRES
     NYRRSPSAQT GHPSPPGQRR DTSNHHTPSS PTDHDRTLAD IVVPLPPQKG KSSTLPRTRP
     RSPEMVRAPL DVDSTHHCDS AGEERRTNDS ESGDELSSSS TEHLQTVSSS CQGRSESPVY
     TNLQELKITQ TNLPPQPSSS PIYVLGDWET HKDQNGRHFY YNRSTHERTW KPPRAKDTNS
     GNSRGESHSV GEPLSSEDTC FSTYSSQSDS QYGSPPRGWS EEMDEYGHTL YVSDYTNEKW
     LKHVDDQGRP YYYSADGSRS EWELPKYNLS PPQPCGDATK SHSLDRKHVE PIVLTKWRHS
     TYLLDPNDKL QYEQKYFCVS ELCCRKNWTS SWTVLQGTHL LFTKGQGGST SWFSQSKPEI
     TVDLRGGSAE WASKDKSSKK HVIEVKTRQG TELLIQSEND TLINDWYRVL QDVISTHAWE
     SDEAIEEDMP ESPGGEKHDK EKEHRDSKKG RGTSTSVDAT DHKKTKHKLK KFLSGRPTLQ
     SIRDKGYIKD LVFGCSLSSL CQRENSTVPA FVKMCIDHVE NSALCVDGLY RVSGNLAVIQ
     KLRYAVNHDE KVNLADGKWE DIHVTTGALK MYFRELPEPL FTYTFFHDFV NAIKTSDYRQ
     RVQGIKELVN KLPKPNHDTM QALFKHLRRV IEHGEENRMT TQSVAIVFGP TLLRPETETW
     NMAVHMVYQN QIVELILLEY ENIFGR
//
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