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Database: UniProt
Entry: A0A3B4TDT0_SERDU
LinkDB: A0A3B4TDT0_SERDU
Original site: A0A3B4TDT0_SERDU 
ID   A0A3B4TDT0_SERDU        Unreviewed;       798 AA.
AC   A0A3B4TDT0;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=Rho GTPase activating protein 12 {ECO:0000313|Ensembl:ENSSDUP00000004286.1};
GN   Name=ARHGAP12 {ECO:0000313|Ensembl:ENSSDUP00000004286.1};
OS   Seriola dumerili (Greater amberjack) (Caranx dumerili).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Carangiformes; Carangidae; Seriola.
OX   NCBI_TaxID=41447 {ECO:0000313|Ensembl:ENSSDUP00000004286.1, ECO:0000313|Proteomes:UP000261420};
RN   [1] {ECO:0000313|Ensembl:ENSSDUP00000004286.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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DR   AlphaFoldDB; A0A3B4TDT0; -.
DR   Ensembl; ENSSDUT00000004381.1; ENSSDUP00000004286.1; ENSSDUG00000003214.1.
DR   GeneTree; ENSGT00950000182860; -.
DR   OMA; KECAPAP; -.
DR   Proteomes; UP000261420; 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; cd12070; SH3_ARHGAP12; 1.
DR   CDD; cd00201; WW; 1.
DR   Gene3D; 2.20.70.10; -; 2.
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; PF00397; WW; 1.
DR   SMART; SM00233; PH; 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   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}.
FT   DOMAIN          11..73
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          269..296
FT                   /note="WW"
FT                   /evidence="ECO:0000259|PROSITE:PS50020"
FT   DOMAIN          359..392
FT                   /note="WW"
FT                   /evidence="ECO:0000259|PROSITE:PS50020"
FT   DOMAIN          469..571
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          653..798
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50238"
FT   REGION          98..141
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          159..239
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          289..347
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          434..461
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          575..620
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        98..124
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        159..194
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        214..239
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        296..340
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        440..461
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        586..609
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   798 AA;  90015 MW;  C1318F8D3865E9E0 CRC64;
     MADREGLPIA PGQVYIEVEY DYEYKAKDKM VAIRQGECYI LVRKTNEDWW QVRKEEGTKA
     FYVPAQYVKE VRRALMPPQK PTLRAKPTVL DICRASNENL NRPQPEMSSF GRPSPSSTPS
     PSSDRVTPPV LPKDANQNMG SPHHCKVVAE LVLLHNNNNH HHANNSTLPR TRADSPPLKV
     GNNHSRSPDS DKTSPPSELP GDGLNKLRND SESGDELSSS STEHMQTTSP TGQGRSDSPV
     YTNLQELKIS QSSLPPIPSG SPLHILGDWE THKDLSGRHF YYNRATGERT WKPPRTRDTS
     GSTSSIRGDS QGTVDSELLS SEENYHSTHS SQSDSQYGSP PRGWSEELDE HGHTLYVSEY
     TQEKWIKHVD EQGRPYYYSA DGSRSEWELP KYNISPQSGE VPKSRSLERK QQDPIVLTKW
     RHSTYVLDLN DKECAPVPKQ SSPDSDSCPS SPKHPSTPSE KCGVLNVTKI TENGKKVRKN
     WTSSWTVLQG SSLLFAKGQG GSTSWKFGSN QSKPEFTVDL RGGSVDWASK DKSSKKHVIE
     LKTRQGTELL IQSEIDSVIN DWFRALTETI NTHAWESDEA IEEDMPESPG AEKQDKEKDH
     RDSKKSRVMK TSVSMDSSDQ KKTRLKLKKF LTRRPTYQAV RDKGYIKDQV FGCSLTSLCQ
     RENTSVPNFV KMCIDHVENT GLSIDGLYRV SGNLAVIQKL RFAVNHDEKV ELNDSKWEDI
     HVTTGALKMF FRELPEPLFT YGSFNDFVNA IKCSDYKQRV NSIKDLIKKL PKPNHDTMQN
     LFKHLRRSNV AADLKGVD
//
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