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Database: UniProt
Entry: A0A060XQZ8_ONCMY
LinkDB: A0A060XQZ8_ONCMY
Original site: A0A060XQZ8_ONCMY 
ID   A0A060XQZ8_ONCMY        Unreviewed;       913 AA.
AC   A0A060XQZ8;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   24-JAN-2024, entry version 44.
DE   RecName: Full=Disabled homolog 2-interacting protein-like {ECO:0008006|Google:ProtNLM};
GN   ORFNames=GSONMT00005450001 {ECO:0000313|EMBL:CDQ79320.1};
OS   Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Oncorhynchus.
OX   NCBI_TaxID=8022 {ECO:0000313|EMBL:CDQ79320.1, ECO:0000313|Proteomes:UP000193380};
RN   [1] {ECO:0000313|EMBL:CDQ79320.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=24755649; DOI=10.1038/ncomms4657;
RA   Berthelot C., Brunet F., Chalopin D., Juanchich A., Bernard M., Noel B.,
RA   Bento P., Da Silva C., Labadie K., Alberti A., Aury J.M., Louis A.,
RA   Dehais P., Bardou P., Montfort J., Klopp C., Cabau C., Gaspin C.,
RA   Thorgaard G.H., Boussaha M., Quillet E., Guyomard R., Galiana D., Bobe J.,
RA   Volff J.N., Genet C., Wincker P., Jaillon O., Roest Crollius H.,
RA   Guiguen Y.;
RT   "The rainbow trout genome provides novel insights into evolution after
RT   whole-genome duplication in vertebrates.";
RL   Nat. Commun. 5:3657-3657(2014).
RN   [2] {ECO:0000313|EMBL:CDQ79320.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Genoscope - CEA;
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FR905438; CDQ79320.1; -; Genomic_DNA.
DR   STRING; 8022.A0A060XQZ8; -.
DR   PaxDb; 8022-A0A060XQZ8; -.
DR   Proteomes; UP000193380; Unassembled WGS sequence.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR   CDD; cd04013; C2_SynGAP_like; 1.
DR   CDD; cd05136; RasGAP_DAB2IP; 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   InterPro; IPR000008; C2_dom.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR021887; DAB2P_C.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR039360; Ras_GTPase.
DR   InterPro; IPR023152; RasGAP_CS.
DR   InterPro; IPR001936; RasGAP_dom.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   PANTHER; PTHR10194:SF26; DISABLED HOMOLOG 2-INTERACTING PROTEIN; 1.
DR   PANTHER; PTHR10194; RAS GTPASE-ACTIVATING PROTEINS; 1.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF12004; DAB2P_C; 1.
DR   Pfam; PF00616; RasGAP; 2.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00323; RasGAP; 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   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.
PE   4: Predicted;
KW   GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW   Reference proteome {ECO:0000313|Proteomes:UP000193380}.
FT   DOMAIN          1..78
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          69..187
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   DOMAIN          247..439
FT                   /note="Ras-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50018"
FT   REGION          530..552
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          603..877
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        530..544
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        603..663
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        686..729
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        742..761
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        772..807
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        830..867
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   913 AA;  100681 MW;  AD2A2597011051D0 CRC64;
     MPRLKESRSH ESLLSPSSAV EALDLSMEDE VLIKPVHGSI LGQDYCFEVT TSTGTKCFSC
     RSSAERDKWM ENLRRAVHPN KDNSRRVENL LKLWIIEAKD LPAKKRYFCE LCLDDTLYAR
     TTCKFKMDNV FWGEHFEFNN LPSVKSVTVH LYKESDKKKK KDKNNYVGLV NIPVGAVTGR
     QFVEKWYSVS TPNPNKGKTP GPMIRLKSRY QSMSILPMES YKEFAEYITN NYMLLCSILE
     PGLSVKNKEE MASALVHILQ STGKAKDFLT DLMMSEVDRC GENEHLIFRE NTLATKAIEE
     YLKLVGQKYL QDALGEFIKA LYESDENCEV DPGKCSSGDL PENQSNLKMC CELAFCKIID
     SYRVFPRELK EVFASWRQQC SSRGRPDISE RLISASLFLR FLCPAVMSPS LFNLMQEYPD
     DRTARTLTLI AKVTQNLANF TKFGNKEEYM SFMNHFLEHE WTNMQRFLLE ISNPETISNT
     AGFEGYIDLG RELSSLHSLL AEDVSQLDQS TASKLGPLAR ILRDVNSALT NPSGVQVSTP
     TDGTGSPPLP LPLASCSLST GLPLHKIVVD SELSGLVDFT RLPSPTPENK DIFFVTRNSG
     IQQSPARSSS YSEANEAEVQ LPNSSKSLSM VDLQDSRSLE STPGPSPGSP SDMLFNDSQS
     PVTPGPGGWA ARTPQGIIPT PGPGPTLRRT GQTPTTPSTE SSTPGRPTQL LAPLSFQNPV
     YQMATGMTMS VSPRGPLADS GSDGHSSVSS QGNNTEDTPK HPGVFLTQGV AVGSGGGSSS
     EFTTRRQLSL GEHQPNVPRQ NSAGPQRRID QPPPPVTRGR TPPNMLQTAY PGPRPSSGSM
     MSSSPDWGPS GGNRLRQQSS SSKGDSPETK QRTMHKSIMD CVEAAVIEHL HSDSNVLXXC
     IEHLHSDSNV LKV
//
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