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Database: UniProt
Entry: A0A3Q3E1U9_9LABR
LinkDB: A0A3Q3E1U9_9LABR
Original site: A0A3Q3E1U9_9LABR 
ID   A0A3Q3E1U9_9LABR        Unreviewed;       763 AA.
AC   A0A3Q3E1U9;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Rho GTPase-activating protein 12-like {ECO:0000313|Ensembl:ENSLBEP00000001087.1};
OS   Labrus bergylta (ballan wrasse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Labriformes; Labridae; Labrus.
OX   NCBI_TaxID=56723 {ECO:0000313|Ensembl:ENSLBEP00000001087.1, ECO:0000313|Proteomes:UP000261660};
RN   [1] {ECO:0000313|Ensembl:ENSLBEP00000001087.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   AlphaFoldDB; A0A3Q3E1U9; -.
DR   STRING; 56723.ENSLBEP00000001087; -.
DR   Ensembl; ENSLBET00000001165.1; ENSLBEP00000001087.1; ENSLBEG00000000828.1.
DR   GeneTree; ENSGT00950000182860; -.
DR   InParanoid; A0A3Q3E1U9; -.
DR   Proteomes; UP000261660; 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; 2.
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   Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW   GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW   Reference proteome {ECO:0000313|Proteomes:UP000261660};
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          234..261
FT                   /note="WW"
FT                   /evidence="ECO:0000259|PROSITE:PS50020"
FT   DOMAIN          276..309
FT                   /note="WW"
FT                   /evidence="ECO:0000259|PROSITE:PS50020"
FT   DOMAIN          402..503
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          569..761
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50238"
FT   REGION          93..203
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          248..283
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          306..327
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          509..556
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        94..108
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        109..133
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        147..178
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        179..203
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        518..540
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   763 AA;  87607 MW;  651FF29A5ED9BB4E CRC64;
     MAELPIAPGQ VYIEVDYDYE YKSKDRVIGI HQGECYMLVK KTNEDWWQVR KDEGTKAFYV
     PAQYVREVRK ALMPPPKPFA LWVKPTNLDL GLHDRPPENL HRHESSNRRS PSAQTASSGH
     FSPPSQRRDC NNQAAIKGGS LPRNRARSPD MVRRLLDVDS TQHCDSAGEE RRTNDSESGD
     ELSSSSTEHL QTVSSSGHGR SESPVYTNLQ ELKITQTHQP PVPSGSPIHA LGDWETYKDQ
     NGRHFYYNRS TQERTWKPPR SRDASFGSSR GEGHSTGESA EWLKHTDEQG RPYYYSADGS
     RSEWELPKYN LSPPQPSGDT PKSRSLDRRQ VEPIVLTKWR HSAYVQDPND KFFFLTATFS
     PFIPLRLSIK MMDVYMTRFC FFFLSFFSIQ PSEKCGVLNV TKITEQGKKV RKNWTSSWTV
     LQGFTLLFAK GQGGGTSWFG GGQSKPEFTV DLRGGSVEWA SKDKSSKKHV LEVKTRYGTE
     LLIQSENDSF VNDWYRALQE TISTHAWESD EAFEEDMPEF SGAEKNDKEK DHRDSKKGRG
     VSLKTSTSMD GPDNKKTRHK LKKFLTRRPT LQAVRDKGYI KDQVFGCSLS DLCHRESVTV
     PSFVRMCIDH WNLAVIQKLR FAVNHDEKVN LVDSKWEDIH VTTGALKMYF RELPEPLFTY
     ALFHDFVSSI KLSEYKHRVQ SIKDLVRALP KPNHDTMQTL FKHLRRVIDH GEENRMTTQS
     VAIVFGPTLL RPETETLNMA VHMVYQNQIV ELILLEYENI FGR
//
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