ID A0A287DD75_ICTTR Unreviewed; 1127 AA.
AC A0A287DD75;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=DAB2 interacting protein {ECO:0000313|Ensembl:ENSSTOP00000031512.1};
GN Name=DAB2IP {ECO:0000313|Ensembl:ENSSTOP00000031512.1};
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:ENSSTOP00000031512.1, 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:ENSSTOP00000031512.1}
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; A0A287DD75; -.
DR Ensembl; ENSSTOT00000030517.1; ENSSTOP00000031512.1; ENSSTOG00000027582.2.
DR GeneTree; ENSGT00940000155853; -.
DR Proteomes; UP000005215; 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; 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 95..129
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 120..238
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 298..490
FT /note="Ras-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50018"
FT REGION 580..605
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 642..669
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 683..704
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 730..750
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 770..792
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 822..925
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 942..961
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1058..1085
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 642..662
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 776..792
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 824..842
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 843..862
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 864..883
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 946..961
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1127 AA; 124498 MW; 1270E12D08C01DC3 CRC64;
LSEKSPSMEP SAASPFRVTV TISGRDKWVG HSHPTWPGPD TSTAYLLRSH LMPRLKESRS
HESLLSPSSA VEALDLSMEE EVVIKPVHSS ILGQDYCFEV TTSSGSKCFS CRSAAERDKW
MENLRRAVHP NKDNSRRVEH ILKLWVIEAK DLPAKKKYLC ELCLDDVLYA RTTGKLKTDN
VFWGEHFEFH NLPPLRTVTV HLYRETDKKK KKERNSYLGL VSLPAASVAG RQFVEKWYPV
VTPNPKGGKG PGPMIRIKAR YQTITILPME MYKEFAEHIT NHYLGLCAAL EPILSAKTKE
EMASALVHIL QSTGKVKDFL TDLMMSEVDR CGDNEHLIFR ENTLATKAIE EYLKLVGQKY
LQDALGEFIK ALYESDENCE VDPSKCSAAD LPEHQGNLKM CCELAFCKII NSYCVFPREL
KEVFASWRQE CSSRGRPDIS ERLISASLFL RFLCPAIMSP SLFNLLQEYP DDRTARTLTL
IAKVTQNLAN FAKFGSKEEY MSFMNQFLEH EWTNMQRFLL EISNPETISN TAGFEGYIDL
GRELSSLHSL LWEAVSQLEQ SIVSKLGPLP RILRDVHTAL STPGSGQLPG TNDLASTPGS
GSSSISAGLQ KMVIENDLSG LIDFTRLPSP TPENKDLFFV TRSSGVQPSP ARSSSYSEAN
EPDLQMANGG KSLSMVDLQD SRTLDGEAGS PAGPDVLPTD GQAPTTQLVA GWPARAAPVS
LAGLATVRRA GQTPTTPGTS EGAPGRPQLL APLSFQNPVY QMAAGLPLSP RGLGDSGSEG
HSSLSSHSNS EELAAAAKLG SFGTTAEELA RRPGELARRQ MSLTEKGGQP TVPRQNSAGP
QRRIDQPPPP PPPPPPAPRG RTPPTLLSTL QYPRPSSGTL ASASPDWAGP GARLRQQSSS
SKGDSPELKP RAVHKQGPSP VSPNALDRTA AWLLTMNSQL LEDEGLGPDP PHRDRLRSKE
ELSQAEKDLA VLQDKLRIST KKLEEYETLF KCQEETTQKL VLEYQARLEE GEERLRRQQE
DKDIQMKGII SRLMSVEEEL KKDHAEMQAA VDSKQKIIDA QEKRIASLDA ANARLMSALT
QLKERYSMQQ SQGWASCRSH KVPRLLEKAA PPLPTEKPDI FFAQLIC
//
