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
//