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Database: UniProt
Entry: A0A2U9BRX7_SCOMX
LinkDB: A0A2U9BRX7_SCOMX
Original site: A0A2U9BRX7_SCOMX 
ID   A0A2U9BRX7_SCOMX        Unreviewed;      1091 AA.
AC   A0A2U9BRX7;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   08-NOV-2023, entry version 17.
DE   SubName: Full=Putative ras GTPase-activating protein 1 isoform 4 {ECO:0000313|EMBL:AWP06935.1};
GN   ORFNames=SMAX5B_010933 {ECO:0000313|EMBL:AWP06935.1};
OS   Scophthalmus maximus (Turbot) (Psetta maxima).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Pleuronectiformes; Pleuronectoidei; Scophthalmidae;
OC   Scophthalmus.
OX   NCBI_TaxID=52904 {ECO:0000313|EMBL:AWP06935.1, ECO:0000313|Proteomes:UP000246464};
RN   [1] {ECO:0000313|EMBL:AWP06935.1, ECO:0000313|Proteomes:UP000246464}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Martinez P.;
RT   "Integrating genomic resources of turbot (Scophthalmus maximus) in depth
RT   evaluation of genetic and physical mapping variation across individuals.";
RL   Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP026251; AWP06935.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2U9BRX7; -.
DR   STRING; 52904.ENSSMAP00000014837; -.
DR   Proteomes; UP000246464; Chromosome 9.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR   GO; GO:0050896; P:response to stimulus; IEA:UniProt.
DR   CDD; cd08400; C2_Ras_p21A1; 1.
DR   CDD; cd13260; PH_RASA1; 1.
DR   CDD; cd05391; RasGAP_p120GAP; 1.
DR   CDD; cd10354; SH2_Cterm_RasGAP; 1.
DR   CDD; cd10353; SH2_Nterm_RasGAP; 1.
DR   CDD; cd11788; SH3_RasGAP; 1.
DR   Gene3D; 2.60.40.150; C2 domain; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   Gene3D; 3.30.505.10; SH2 domain; 2.
DR   Gene3D; 2.30.30.40; SH3 Domains; 1.
DR   InterPro; IPR000008; C2_dom.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR039360; Ras_GTPase.
DR   InterPro; IPR035842; RasGAP_C_SH2.
DR   InterPro; IPR023152; RasGAP_CS.
DR   InterPro; IPR001936; RasGAP_dom.
DR   InterPro; IPR035841; RasGAP_N_SH2.
DR   InterPro; IPR035652; RasGAP_SH3.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR000980; SH2.
DR   InterPro; IPR036860; SH2_dom_sf.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   PANTHER; PTHR10194:SF146; RAS GTPASE-ACTIVATING PROTEIN 1; 1.
DR   PANTHER; PTHR10194; RAS GTPASE-ACTIVATING PROTEINS; 1.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF00616; RasGAP; 1.
DR   Pfam; PF00017; SH2; 2.
DR   Pfam; PF00018; SH3_1; 1.
DR   PRINTS; PR00401; SH2DOMAIN.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00323; RasGAP; 1.
DR   SMART; SM00252; SH2; 2.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR   SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF55550; SH2 domain; 2.
DR   SUPFAM; SSF50044; SH3-domain; 1.
DR   PROSITE; PS50004; C2; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS00509; RAS_GTPASE_ACTIV_1; 1.
DR   PROSITE; PS50018; RAS_GTPASE_ACTIV_2; 1.
DR   PROSITE; PS50001; SH2; 2.
DR   PROSITE; PS50002; SH3; 1.
PE   4: Predicted;
KW   GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000246464};
KW   SH2 domain {ECO:0000256|ARBA:ARBA00022999, ECO:0000256|PROSITE-
KW   ProRule:PRU00191};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}.
FT   DOMAIN          210..301
FT                   /note="SH2"
FT                   /evidence="ECO:0000259|PROSITE:PS50001"
FT   DOMAIN          308..370
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          380..470
FT                   /note="SH2"
FT                   /evidence="ECO:0000259|PROSITE:PS50001"
FT   DOMAIN          503..607
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          608..721
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   DOMAIN          779..973
FT                   /note="Ras-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50018"
FT   REGION          1..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          72..91
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          109..196
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        18..32
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        125..156
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        157..176
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1091 AA;  122508 MW;  D6697D0AF538036F CRC64;
     MSARRLETGE GEGGETEQRS SGRASSPPKT LTDYCESRGE GAGSLLDCFP PSTHCPNMMA
     AESSSRVRVA DLGAGPAPAL RQHSNASPDS LPDMSVIYPL PSGDLIGPAP AAAGSGGAGG
     GQPVFQGASS GTGGGVCCSP TSEGPASRIS PTSTGPEGPT GFPPLPPPPP PPPGCGGLGG
     TLDESDMQDG PEYEEEEVVF PLSAPPTNQW YHGKLDRTIA EERLRQARNP GSYLIRESDR
     RPGSFVLSFL SMTNVVNHFR IIAMCGDYYI GGRRFSSLSD LIGYYSYVSC LLKGEKLLSP
     VAPPEPVEDR RRVRAILPYT KVPDTDEISF LKGDMFIVHN ELDDGWMWVT NVRTEEQGLI
     VEDLVEEVGR EEDPHEGKVW YHGKITKQEA YNLLMTVGQV CSFLVRPSDN TPGDYSLFFR
     TNENIQRFKI SPTPNNQYMM GGRYYNSVDD IIEHYKKEQI VEGYNLKEPV SVQHQEQVLT
     DTVDGREIYN TIRRKTKDAF YKNIVKKGYL LFNKGKGKRW KNLYFILEGN DAQLIYFESE
     KRATKPKGLI DLSVCSVYGV HDSLFGRPNC FQIVVQHFSE EQYIFYFAGE VPEQAQDWMK
     CLQTFCSNLR KTTQPTSNKR LRQVSSLVLY VEEAHKLPVK YFTNPYCNIY LNSVQVAKTH
     PREGQNPVFT EEFIFDDLSS EINRFEISLS NKTKKSKESD ILFMRCQLNR LQKGQMIDEW
     FPLSSHVPLK GIEPGSLRVR ARYSMEKIMP EEEYSEFKEM ILQKEFHVIY ALAHVCGQDR
     TLLASLLLRI FRHEKAEAPL LRTLNDREIN VEDEATTLFR ATTLASTLME QYMKATATPF
     VHHALKDTIL KIMESKQSCE LNPSKLEKNE DVNLNLAHLL NILSELVEKI FMAAEILPPT
     LRFIYGCLQK SVQQKWPTNT TMRTRVVSGF VFLRLICPAI LNPRMFNIIA DPPSSTAGRT
     LTLVAKSVQN LANLVEFGAK EPYMEGVNPF IKNNKHRMIM FLDELGNVPD LPEATEHFRT
     DLSRDLAALH EVCATHSDEL RTLSNERGAQ QHVLKKLLAI TELLQQKQAQ YANSNRTECT
     IMSLAAAIQV M
//
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