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Database: UniProt
Entry: A0A3B3C1C9_ORYME
LinkDB: A0A3B3C1C9_ORYME
Original site: A0A3B3C1C9_ORYME 
ID   A0A3B3C1C9_ORYME        Unreviewed;      1182 AA.
AC   A0A3B3C1C9;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=DAB2 interacting protein {ECO:0000313|Ensembl:ENSOMEP00000011635.1};
OS   Oryzias melastigma (Marine medaka).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC   Oryzias.
OX   NCBI_TaxID=30732 {ECO:0000313|Ensembl:ENSOMEP00000011635.1, ECO:0000313|Proteomes:UP000261560};
RN   [1] {ECO:0000313|Ensembl:ENSOMEP00000011635.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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DR   AlphaFoldDB; A0A3B3C1C9; -.
DR   Ensembl; ENSOMET00000018771.1; ENSOMEP00000011635.1; ENSOMEG00000013086.1.
DR   GeneTree; ENSGT00940000155853; -.
DR   Proteomes; UP000261560; Unplaced.
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; SM00233; PH; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   GTPase activation {ECO:0000256|ARBA:ARBA00022468}.
FT   DOMAIN          165..199
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          190..308
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   DOMAIN          368..560
FT                   /note="Ras-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50018"
FT   REGION          1..77
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          653..672
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          705..815
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          837..992
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1156..1182
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1021..1094
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1124..1151
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        35..54
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        55..76
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        709..750
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        791..807
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        842..859
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        890..916
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        945..991
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1182 AA;  131788 MW;  B875F7523A333222 CRC64;
     MAGVTRKGSG RPSYYYRFLG KSRLQRQRSR SRSRTRSSAT RESPPERTGR RRSMPGSADK
     SSATMEPSST AATPFRVTGF LSRRLKGSIK RTKSQPKLDR NASFRHILPN FRSFDHDRSQ
     LMPRLKESRS HESLLSPSSA VEALDLSMED EVIIKPVHSS ILGQDYCFEV TTSTGSKCFS
     CRSAAERDKW MENLRRAVQP NKDNSRRVEN ILRLWVIEAK DLPAKKKYFC ELCLDESLYA
     RTTCKLKTDN VFWGEHFEFS NLPAVRSITA HLYKDTDKKK KKDKNNYIGL VNIPVAAVSG
     RQFVEKWYPV STPNPPKGKT SGPMIRIKTR YQSMSILPME MYKEFAEYTT NNYMLLCSVL
     EPGISVKNKE EMACALVHIL QSTGKAKDFL TDLMMSEVDR CGENEHLIFR ENTLATKAIE
     EYLKLVGQKY LQDTLGEFIK ALYESDENCE VDPSKCSSGD LPDHQSNLKM CCELAFCKII
     KSYCFFPREL KEVFASWRQE CSSRGRPDIS ERLISASLFL RFLCPAIMSP SLFNLTQEYP
     DDRTARTLTL IAKVTQNLAN FTKFGNKEEY MSFMNQFLEH EWSDMQRFLL EISNPETISN
     TAGFEGYIDL GRELSTLHSL LSEVVSQMDQ SVASKLGPLP RVLREVNNAL SNPSCVQMTP
     GQSSEQVNSP PAEAGCSIST GLQKMVIDSD LSGLVDFTRL PSPTPENKDL FFVTKSSGIQ
     PSPARSSSYS ETNEPDQGMA NGSKSLSMLD LQDPRSLDGG SGPSPSDGLE GLASGSCWAA
     KVPQGNTPGG PTLRRPGQTT TTPGAEGTPG RPAQLLAPLS FQNPVYQMAA CLPVSPRGMA
     DSGSECHSSV SSHSNNEDGP PGGKQAFLNP AGGGGGSSGD EYTRRPGEAN RRQLSLTETQ
     HQPSIPRQNS AGPQRRIDQP PPQLLNRGRT PPNLLGGGPY PRPSSGSMMA SSPDWPASGA
     RLRQQSSSSK GDSPETKQRV QHKQAPSPVN PSALDRTAAW LLNMNAHYLD HEGLETESLR
     NREDLTQVEK YQQEIAVLQE KLRASVQKLE EYEARLKGQD EQAQKVLMEY QARLEESEER
     LRRQQDDKDL QMKSIISRLM SVEEELKKDH SDMQAVVDSK QKIIDAQEKR IASLDAANAR
     LMSALAQLKE RYSMQTRNGI SPTNPTKLQI TENGEFRNSS NC
//
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