ID A0A3P9A7E2_ESOLU Unreviewed; 1171 AA.
AC A0A3P9A7E2;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Disabled homolog 2-interacting protein {ECO:0000313|Ensembl:ENSELUP00000036645.1};
GN Name=DAB2IP {ECO:0000313|Ensembl:ENSELUP00000036645.1};
OS Esox lucius (Northern pike).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Esociformes;
OC Esocidae; Esox.
OX NCBI_TaxID=8010 {ECO:0000313|Ensembl:ENSELUP00000036645.1, ECO:0000313|Proteomes:UP000265140};
RN [1] {ECO:0000313|Ensembl:ENSELUP00000036645.1, ECO:0000313|Proteomes:UP000265140}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25069045;
RA Rondeau E.B., Minkley D.R., Leong J.S., Messmer A.M., Jantzen J.R.,
RA von Schalburg K.R., Lemon C., Bird N.H., Koop B.F.;
RT "The genome and linkage map of the northern pike (Esox lucius): conserved
RT synteny revealed between the salmonid sister group and the Neoteleostei.";
RL PLoS ONE 9:e102089-e102089(2014).
RN [2] {ECO:0000313|Ensembl:ENSELUP00000036645.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR RefSeq; XP_019908411.1; XM_020052852.1.
DR AlphaFoldDB; A0A3P9A7E2; -.
DR Ensembl; ENSELUT00000025439.2; ENSELUP00000036645.1; ENSELUG00000016051.2.
DR GeneID; 105014660; -.
DR GeneTree; ENSGT00940000155853; -.
DR OrthoDB; 22721at2759; -.
DR Proteomes; UP000265140; LG13.
DR Bgee; ENSELUG00000016051; Expressed in camera-type eye and 12 other cell types or tissues.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000265140}.
FT DOMAIN 132..166
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 157..275
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 335..527
FT /note="Ras-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50018"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 683..795
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 815..845
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 878..976
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1146..1171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1049..1083
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1113..1140
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 683..722
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 731..748
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 773..787
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 826..840
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 878..899
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 922..970
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1171 AA; 130112 MW; 38B52CD845E97FAD CRC64;
MELENTAEPE SYNEIPPEVA GRRRSMPGSP LDKSPPMEPT PFKVTGFLSR RLKGSIKRTK
SQPKLDRNSS FRNILPGFRT ADNDRSHLMP RLKESRSHES LLSPSSAVEA LDLSMEDEVL
IKPVHSSILG QDYCFEVTTS TGTKCFSCRS SAERDKWMEN LRRAVHPNKD NSRRVENLLK
LWIIEAKDLP AKKRYFCELC LDDTLYARTS CKLKTDNVFW GEHFEFNNLP AVSSATVHLY
KESDKKKKKD KNNYVGLVNI PVCAVTGRQF VEKWYSVSTP NPNKGKTPGP MIRLKSRYQS
MSILPMELYK EFAEYITNNY MLLCSVLEPG LSVKNKEEMA SALVHILQST GKAKDFLTDL
MMSEVDRCGE NEQLIFRENT LATKAIEEYL KLVGQKYLQD ALGEFIKALY ESDENCEVDP
GKCSSGDLLE HQSNLKMCCE LAFCKIIDSY RVFPRELKEV FASWRQECSS RGRPDISERL
ISASLFLRFL CPAVMSPSLF NLMQEYPDDR TARTLTLIAK VTQNLANFTK FGNKEEYMSF
MNQFLEHEWT NMQRFLLEIS NPETISNTAG FEGYIDLGRE LSTLHSLLAE AVSQLDQSTA
SKLGPLARIL RDVNSALTNP SGVQVSSTTE RMGSPPLPLA GCSLSTGLPL HKMVVDSELS
GLVDFTRLPS PTPENKDLFF VTRNSGVQQS PARSSSYSET NEADAQLPNG SKSLSMVDLQ
DGRSPESTPG PAAPGDSQSP SGPGCWTTRP TQGLVPGLVP GLIPGPGAGP TLRRTGQTPN
TDGSAPAPGR PSQLLAPLSF QNPVYQMATG MTVSVSPRGP LADSGSEGHS SVSSQGNNAE
EAPKHPGVFL TQGVAVGGGG GAEDFARRSG EFTARRQLSL TEPQHPSNVP RQNSAGPQRR
IDQPPPPVTR GRTPPNMLQT AYPGPRPSSG SMMSSSPDWG PNGGTRMRQQ SSSSKGDSPE
TKQHTAHKAP SPVNPNALDR TAAWLLNMNV QYLDHEGVDP DTKHREDLQN IEELTQTEKY
QQEIAILQEK LHLSAKKLEE YECHLSGQDE QTQKMLLEYQ ARLEDTEERL RRQQEDKELQ
MKSIITRLMS VEEELKKDHS DMQSIVDSKQ KIIEAQEKRI ASLDAANARL MSALTQLKER
YSLQTRNGIS PTNPSKLQIT ENGEFRNSGN C
//
