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Database: UniProt
Entry: A0A3Q3FWI8_KRYMA
LinkDB: A0A3Q3FWI8_KRYMA
Original site: A0A3Q3FWI8_KRYMA 
ID   A0A3Q3FWI8_KRYMA        Unreviewed;      1070 AA.
AC   A0A3Q3FWI8;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=DAB2 interacting protein {ECO:0000313|Ensembl:ENSKMAP00000016722.1};
OS   Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX   NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000016722.1, ECO:0000313|Proteomes:UP000264800};
RN   [1] {ECO:0000313|Ensembl:ENSKMAP00000016722.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   RefSeq; XP_017286738.1; XM_017431249.1.
DR   AlphaFoldDB; A0A3Q3FWI8; -.
DR   Ensembl; ENSKMAT00000016956.1; ENSKMAP00000016722.1; ENSKMAG00000012390.1.
DR   GeneID; 108244777; -.
DR   GeneTree; ENSGT00940000155853; -.
DR   OMA; RTRPARX; -.
DR   OrthoDB; 22721at2759; -.
DR   Proteomes; UP000264800; 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; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000264800}.
FT   DOMAIN          1..89
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          80..198
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   DOMAIN          258..450
FT                   /note="Ras-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50018"
FT   REGION          542..568
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          611..708
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          728..880
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1045..1070
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          909..982
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1012..1039
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        611..658
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        732..750
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        777..821
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        831..879
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1070 AA;  119353 MW;  05075C54BA07E83F CRC64;
     MFHIFSRSSQ LMPRLKESRS HESLLSPSSA VEALDLSMED EVIIKTVHSS ILGQDYCFEV
     TTSTGSKCFS CRSAAERDKW MENLRRAVQP NKDNSRRVEN LLRLWLIEAK DLPAKKKYFC
     ELCLDDSLYA RTTCKLKTDN VFWGEHFEFS NLPAVKSITA HLYKDTDKKK KKDKNNYIGL
     VTIPVAAVTG RQFVEKWYPV STPNPPKGKT SGPMIRIKAR YQSMSILPME MYKEFAEYTT
     NNYMLLCSVL EPGISVKNKE EMACALVHIL QSTGKAKDFL TDLMMSEVDR CGENEHLIFR
     ENTLATKAIE EYLKLVGQKY LQDALGEFIK ALYESDENCE VDPSKCSSGD LPEHQSNLKM
     CCELAFCKII NSYCVFPREL KEVFASWRQE CSNRGRPDIS ERLISASLFL RFLCPAIMSP
     SLFNLMQEYP DDRTARTLTL IAKVTQNLAN FTKFGNKEEY MSFMNQFVEH EWTNMQRFLL
     EISNPETISN TAGFEGYIDL GRELSTLHSL LSEVVSQTDQ NAASKLGPLP RILREVNTAL
     SNPSSVHMTP GPSSEPAHSP PAEAGSSISS GLQKMVIDSE LSGLVDFTRL PSPTPENKDL
     FFVTRSSAIQ SSPARSSSYS ETNEPDLSMT NGSKSLSMVD LQDPHTLDSG TGPSLSDALG
     EGQASGGGWS ARVSQGNIPA GPTPRRPGQT PTTPGTESTP GRPPQLLAPL SFQNPVYQMA
     ACLPVSPRGM TDSGSECHSS VSSHSNNEDG PAAGKQAFMN HGGGSSGDEY TRRSGDFNRR
     QLSLTETPHQ PTVPRQNSAG PQRRIDQPPP QSITRGRTPP NLLSSGPFPR PPSGNMMTSS
     PDWPAGGTRL RQQSSSSNID SPESKQRAQH KQAPSPVNPS ALDRTAAWLL NMNVQFLDHE
     GMEPESLRHT DHQTEVEKYQ QEIAVLQEKL RASVQKLEEY EARLKGQDEQ AQKVLMEYQA
     RLEESEERLR RQQDDKDLQM KSIISRLMSV EEELKKDHSD MQAVVDSKQK IIDAQEKRIA
     SLDAANARLM SALSQLKERY SIQTRNGISP TNPSKLQITE NGEFRNSSNC
//
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