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.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//