ID I3N2V9_ICTTR Unreviewed; 1148 AA.
AC I3N2V9;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 2.
DT 27-MAR-2024, entry version 70.
DE SubName: Full=DAB2 interacting protein {ECO:0000313|Ensembl:ENSSTOP00000018705.2};
GN Name=DAB2IP {ECO:0000313|Ensembl:ENSSTOP00000018705.2};
OS Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS tridecemlineatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC Xerinae; Marmotini; Ictidomys.
OX NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000018705.2, ECO:0000313|Proteomes:UP000005215};
RN [1] {ECO:0000313|Proteomes:UP000005215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Assembly & Analysis Group;
RG Computational R&D Group;
RG and Sequencing Platform;
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT "The Draft Genome of Spermophilus tridecemlineatus.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSTOP00000018705.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR EMBL; AGTP01019822; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01019823; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01019824; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; I3N2V9; -.
DR STRING; 43179.ENSSTOP00000018705; -.
DR Ensembl; ENSSTOT00000025784.2; ENSSTOP00000018705.2; ENSSTOG00000027582.2.
DR GeneTree; ENSGT00940000155853; -.
DR HOGENOM; CLU_001727_1_0_1; -.
DR InParanoid; I3N2V9; -.
DR TreeFam; TF105303; -.
DR Proteomes; UP000005215; Unassembled WGS sequence.
DR GO; GO:1990597; C:AIP1-IRE1 complex; IEA:Ensembl.
DR GO; GO:0044300; C:cerebellar mossy fiber; IEA:Ensembl.
DR GO; GO:0044301; C:climbing fiber; IEA:Ensembl.
DR GO; GO:0030139; C:endocytic vesicle; IEA:Ensembl.
DR GO; GO:0032809; C:neuronal cell body membrane; IEA:Ensembl.
DR GO; GO:1990032; C:parallel fiber; IEA:Ensembl.
DR GO; GO:0071889; F:14-3-3 protein binding; IEA:Ensembl.
DR GO; GO:0005123; F:death receptor binding; IEA:Ensembl.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0031434; F:mitogen-activated protein kinase kinase binding; IEA:Ensembl.
DR GO; GO:0031435; F:mitogen-activated protein kinase kinase kinase binding; IEA:Ensembl.
DR GO; GO:0036312; F:phosphatidylinositol 3-kinase regulatory subunit binding; IEA:Ensembl.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IEA:Ensembl.
DR GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; IEA:Ensembl.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0051721; F:protein phosphatase 2A binding; IEA:Ensembl.
DR GO; GO:0043539; F:protein serine/threonine kinase activator activity; IEA:Ensembl.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR GO; GO:0017124; F:SH3 domain binding; IEA:Ensembl.
DR GO; GO:0035591; F:signaling adaptor activity; IEA:Ensembl.
DR GO; GO:0043184; F:vascular endothelial growth factor receptor 2 binding; IEA:Ensembl.
DR GO; GO:0021814; P:cell motility involved in cerebral cortex radial glia guided migration; IEA:Ensembl.
DR GO; GO:0071347; P:cellular response to interleukin-1; IEA:Ensembl.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IEA:Ensembl.
DR GO; GO:0035924; P:cellular response to vascular endothelial growth factor stimulus; IEA:Ensembl.
DR GO; GO:0008625; P:extrinsic apoptotic signaling pathway via death domain receptors; IEA:Ensembl.
DR GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; IEA:Ensembl.
DR GO; GO:0021819; P:layer formation in cerebral cortex; IEA:Ensembl.
DR GO; GO:0016525; P:negative regulation of angiogenesis; IEA:Ensembl.
DR GO; GO:0043124; P:negative regulation of canonical NF-kappaB signal transduction; IEA:Ensembl.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IEA:Ensembl.
DR GO; GO:0010596; P:negative regulation of endothelial cell migration; IEA:Ensembl.
DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IEA:Ensembl.
DR GO; GO:0010719; P:negative regulation of epithelial to mesenchymal transition; IEA:Ensembl.
DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
DR GO; GO:0048147; P:negative regulation of fibroblast proliferation; IEA:Ensembl.
DR GO; GO:0070317; P:negative regulation of G0 to G1 transition; IEA:Ensembl.
DR GO; GO:0051898; P:negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IEA:Ensembl.
DR GO; GO:0042177; P:negative regulation of protein catabolic process; IEA:Ensembl.
DR GO; GO:0034144; P:negative regulation of toll-like receptor 4 signaling pathway; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0030948; P:negative regulation of vascular endothelial growth factor receptor signaling pathway; IEA:Ensembl.
DR GO; GO:1900747; P:negative regulation of vascular endothelial growth factor signaling pathway; IEA:Ensembl.
DR GO; GO:0048812; P:neuron projection morphogenesis; IEA:Ensembl.
DR GO; GO:2001235; P:positive regulation of apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:0043123; P:positive regulation of canonical NF-kappaB signal transduction; IEA:Ensembl.
DR GO; GO:1900006; P:positive regulation of dendrite development; IEA:Ensembl.
DR GO; GO:0046330; P:positive regulation of JNK cascade; IEA:Ensembl.
DR GO; GO:2001224; P:positive regulation of neuron migration; IEA:Ensembl.
DR GO; GO:1901800; P:positive regulation of proteasomal protein catabolic process; IEA:Ensembl.
DR GO; GO:0031334; P:positive regulation of protein-containing complex assembly; IEA:Ensembl.
DR GO; GO:0090129; P:positive regulation of synapse maturation; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0030163; P:protein catabolic process; IEA:Ensembl.
DR GO; GO:1900744; P:regulation of p38MAPK cascade; IEA:Ensembl.
DR GO; GO:0035148; P:tube formation; IEA:Ensembl.
DR GO; GO:0036324; P:vascular endothelial growth factor receptor-2 signaling pathway; IEA:Ensembl.
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:UP000005215}.
FT DOMAIN 127..161
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 152..270
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 330..522
FT /note="Ras-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50018"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 612..637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 674..701
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 715..736
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 762..782
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 802..824
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 854..957
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 974..993
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1123..1148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1090..1117
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 25..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 674..694
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 808..824
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 856..874
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 875..894
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 896..915
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 978..993
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1148 AA; 126808 MW; CD5000673145963B CRC64;
VRGWMRAAGR PPWMCFKSPQ ERPGSRRSLP GSLSEKSPSM EPSAASPFRV TVTISGRDKW
VGHSHPTWPG PDTSTAYLLR SHLMPRLKES RSHESLLSPS SAVEALDLSM EEEVVIKPVH
SSILGQDYCF EVTTSSGSKC FSCRSAAERD KWMENLRRAV HPNKDNSRRV EHILKLWVIE
AKDLPAKKKY LCELCLDDVL YARTTGKLKT DNVFWGEHFE FHNLPPLRTV TVHLYRETDK
KKKKERNSYL GLVSLPAASV AGRQFVEKWY PVVTPNPKGG KGPGPMIRIK ARYQTITILP
MEMYKEFAEH ITNHYLGLCA ALEPILSAKT KEEMASALVH ILQSTGKVKD FLTDLMMSEV
DRCGDNEHLI FRENTLATKA IEEYLKLVGQ KYLQDALGEF IKALYESDEN CEVDPSKCSA
ADLPEHQGNL KMCCELAFCK IINSYCVFPR ELKEVFASWR QECSSRGRPD ISERLISASL
FLRFLCPAIM SPSLFNLLQE YPDDRTARTL TLIAKVTQNL ANFAKFGSKE EYMSFMNQFL
EHEWTNMQRF LLEISNPETI SNTAGFEGYI DLGRELSSLH SLLWEAVSQL EQSIVSKLGP
LPRILRDVHT ALSTPGSGQL PGTNDLASTP GSGSSSISAG LQKMVIENDL SGLIDFTRLP
SPTPENKDLF FVTRSSGVQP SPARSSSYSE ANEPDLQMAN GGKSLSMVDL QDSRTLDGEA
GSPAGPDVLP TDGQAPTTQL VAGWPARAAP VSLAGLATVR RAGQTPTTPG TSEGAPGRPQ
LLAPLSFQNP VYQMAAGLPL SPRGLGDSGS EGHSSLSSHS NSEELAAAAK LGSFGTTAEE
LARRPGELAR RQMSLTEKGG QPTVPRQNSA GPQRRIDQPP PPPPPPPPAP RGRTPPTLLS
TLQYPRPSSG TLASASPDWA GPGARLRQQS SSSKGDSPEL KPRAVHKQGP SPVSPNALDR
TAAWLLTMNS QLLEDEGLGP DPPHRDRLRS KEELSQAEKD LAVLQDKLRI STKKLEEYET
LFKCQEETTQ KLVLEYQARL EEGEERLRRQ QEDKDIQMKG IISRLMSVEE ELKKDHAEMQ
AAVDSKQKII DAQEKRIASL DAANARLMSA LTQLKERYSM QARNGISPTN PTKLQITENG
EFRNSSNC
//
