ID W5MFH5_LEPOC Unreviewed; 838 AA.
AC W5MFH5;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Rho GTPase activating protein 9 {ECO:0000313|Ensembl:ENSLOCP00000007134.1};
GN Name=ARHGAP9 {ECO:0000313|Ensembl:ENSLOCP00000007134.1};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000007134.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000007134.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR EMBL; AHAT01018789; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01018790; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01018791; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01018792; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01018793; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 7918.ENSLOCP00000007134; -.
DR Ensembl; ENSLOCT00000007142.1; ENSLOCP00000007134.1; ENSLOCG00000005905.1.
DR eggNOG; KOG1450; Eukaryota.
DR GeneTree; ENSGT00950000182860; -.
DR HOGENOM; CLU_015883_6_1_1; -.
DR InParanoid; W5MFH5; -.
DR OMA; ELRAWHH; -.
DR Proteomes; UP000018468; Linkage group LG4.
DR Bgee; ENSLOCG00000005905; Expressed in camera-type eye and 13 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; 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; 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:SF103; RHO GTPASE-ACTIVATING PROTEIN 9; 1.
DR PANTHER; PTHR23176; RHO/RAC/CDC GTPASE-ACTIVATING PROTEIN; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR Pfam; PF00018; SH3_1; 1.
DR Pfam; PF00397; WW; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SMART; SM00326; SH3; 1.
DR SMART; SM00456; WW; 1.
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; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50238; RHOGAP; 1.
DR PROSITE; PS50002; SH3; 1.
DR PROSITE; PS50020; WW_DOMAIN_2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW Reference proteome {ECO:0000313|Proteomes:UP000018468};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 17..83
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 248..276
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 430..539
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 623..830
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 124..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 272..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 406..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 474..502
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 565..587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..296
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 299..327
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..433
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 486..502
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 838 AA; 94233 MW; 26B9DED480C1BC97 CRC64;
MLSGSWRKTA LPSAARGGSV VLEAQYDYSY RATDGRQVSM REGERFVLLR KANDDWWQVR
RMGAPPKSKP IYVPATYVTE VQANVRLVAR ASLTPCSQSP CPGKFQSAPA RTFCRSMEDL
NSTFRGRGAG GHFPTLPFAG PPPSSSSGHL LLPPDPSGPM ARSKSSSMLP QNPYQEPEAG
GSPSGAPHTK SYSQGDIVEA PRRHSHLQLG AQPYIPRHSL LESPLYSSRR LSEPPSPTQR
PLQVLDLWEQ HLDPVTGRCF YVNSVTRERS WKPPRRAKER AASRREHRHD LPDEGGTFPR
DSNQLSSPSQ DSGNGSLQKL SPGSSPVTYI YSVQDADSSW ELSQNIQRAA SSDALNSAPF
SPTEAQLRNS SALPKIERLN HARSMILTEQ SEAKMAQHRR NMSHHVLGGR GMEPLSPISS
PDSSESTTPE LEKAGMLNKT KIAEGGRKLR KNWNASWVVL VGNSLVFFKD PKTQTPSTWK
PXQRAGRGAE GKKVRDGGDE RDEQRVQELR TVTGNEFLLQ SETDSVIREW YSTIQSVIDR
LDRENPLDNV LLYSLRRAGS TEILDHSGDE DDIRASPVLR STSSAESSEK KRVKSRLKKL
ILKRPPLQAL QEKGLIKEQV FGCRLDALCE REKSSVPKFV RLCAEAVEKR GLETDGIYRV
SGNLAVIQKL RFKVDHERAV TTDGRYLFPE ELVQEEKLNL DDSEWEDIHV ITGALKMFFR
ELPEPLIPYS FFNDFVETVK IPDYMEKVER MKCLVKKLPP PNHDTLNYIL QHLKRVMEQS
DINRMTTQNI GIVFGPTLMR PERDNSNIAI NMVYQNQVVE LILSEYSQIF GPERPDFH
//
