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Database: UniProt
Entry: A0A287DDU2_ICTTR
LinkDB: A0A287DDU2_ICTTR
Original site: A0A287DDU2_ICTTR 
ID   A0A287DDU2_ICTTR        Unreviewed;      1650 AA.
AC   A0A287DDU2;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   05-JUN-2019, entry version 15.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSSTOP00000031722};
GN   Name=RAPGEF2 {ECO:0000313|Ensembl:ENSSTOP00000031722};
OS   Ictidomys tridecemlineatus (Thirteen-lined ground squirrel)
OS   (Spermophilus tridecemlineatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha;
OC   Sciuridae; Xerinae; Marmotini; Ictidomys.
OX   NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000031722, ECO:0000313|Proteomes:UP000005215};
RN   [1] {ECO:0000313|Ensembl:ENSSTOP00000031722, 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:ENSSTOP00000031722}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (OCT-2017) to UniProtKB.
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DR   EMBL; AGTP01065134; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGTP01065135; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGTP01065136; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGTP01065137; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGTP01065138; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   Ensembl; ENSSTOT00000041419; ENSSTOP00000031722; ENSSTOG00000010940.
DR   GeneTree; ENSGT00940000156418; -.
DR   Proteomes; UP000005215; Unassembled WGS sequence.
DR   GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
DR   GO; GO:0005923; C:bicellular tight junction; IEA:Ensembl.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0030139; C:endocytic vesicle; IEA:Ensembl.
DR   GO; GO:0005770; C:late endosome; IEA:Ensembl.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR   GO; GO:0031697; F:beta-1 adrenergic receptor binding; IEA:Ensembl.
DR   GO; GO:0030552; F:cAMP binding; IEA:Ensembl.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:Ensembl.
DR   GO; GO:0030165; F:PDZ domain binding; IEA:Ensembl.
DR   GO; GO:0070300; F:phosphatidic acid binding; IEA:Ensembl.
DR   GO; GO:0017034; F:Rap guanyl-nucleotide exchange factor activity; IEA:Ensembl.
DR   GO; GO:0050699; F:WW domain binding; IEA:Ensembl.
DR   GO; GO:0071880; P:adenylate cyclase-activating adrenergic receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0071320; P:cellular response to cAMP; IEA:Ensembl.
DR   GO; GO:0071321; P:cellular response to cGMP; IEA:Ensembl.
DR   GO; GO:0090557; P:establishment of endothelial intestinal barrier; IEA:Ensembl.
DR   GO; GO:0030033; P:microvillus assembly; IEA:Ensembl.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:Ensembl.
DR   GO; GO:0050774; P:negative regulation of dendrite morphogenesis; IEA:Ensembl.
DR   GO; GO:0031175; P:neuron projection development; IEA:Ensembl.
DR   GO; GO:0007218; P:neuropeptide signaling pathway; IEA:Ensembl.
DR   GO; GO:2000481; P:positive regulation of cAMP-dependent protein kinase activity; IEA:Ensembl.
DR   GO; GO:0043950; P:positive regulation of cAMP-mediated signaling; IEA:Ensembl.
DR   GO; GO:2000670; P:positive regulation of dendritic cell apoptotic process; IEA:Ensembl.
DR   GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
DR   GO; GO:0072659; P:protein localization to plasma membrane; IEA:Ensembl.
DR   GO; GO:0032486; P:Rap protein signal transduction; IEA:Ensembl.
DR   GO; GO:1901888; P:regulation of cell junction assembly; IEA:Ensembl.
DR   CDD; cd00038; CAP_ED; 2.
DR   CDD; cd00155; RasGEF; 1.
DR   CDD; cd06224; REM; 1.
DR   Gene3D; 2.60.120.10; -; 2.
DR   InterPro; IPR018490; cNMP-bd-like.
DR   InterPro; IPR000595; cNMP-bd_dom.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR000159; RA_dom.
DR   InterPro; IPR030739; RapGEF2.
DR   InterPro; IPR008937; Ras-like_GEF.
DR   InterPro; IPR000651; Ras-like_Gua-exchang_fac_N.
DR   InterPro; IPR023578; Ras_GEF_dom_sf.
DR   InterPro; IPR001895; RASGEF_cat_dom.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   PANTHER; PTHR23113; PTHR23113; 1.
DR   PANTHER; PTHR23113:SF217; PTHR23113:SF217; 1.
DR   Pfam; PF00595; PDZ; 1.
DR   Pfam; PF00788; RA; 1.
DR   Pfam; PF00617; RasGEF; 1.
DR   Pfam; PF00618; RasGEF_N; 1.
DR   SMART; SM00100; cNMP; 2.
DR   SMART; SM00228; PDZ; 1.
DR   SMART; SM00314; RA; 1.
DR   SMART; SM00147; RasGEF; 1.
DR   SMART; SM00229; RasGEFN; 1.
DR   SUPFAM; SSF48366; SSF48366; 1.
DR   SUPFAM; SSF50156; SSF50156; 1.
DR   SUPFAM; SSF51206; SSF51206; 2.
DR   SUPFAM; SSF54236; SSF54236; 1.
DR   PROSITE; PS50042; CNMP_BINDING_3; 2.
DR   PROSITE; PS50106; PDZ; 1.
DR   PROSITE; PS50200; RA; 1.
DR   PROSITE; PS50009; RASGEF_CAT; 1.
DR   PROSITE; PS50212; RASGEF_NTER; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000005215};
KW   Guanine-nucleotide releasing factor {ECO:0000256|PROSITE-
KW   ProRule:PRU00168, ECO:0000256|SAAS:SAAS01081641};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005215}.
FT   DOMAIN        3     50       Cyclic nucleotide-binding.
FT                                {ECO:0000259|PROSITE:PS50042}.
FT   DOMAIN      262    362       Cyclic nucleotide-binding.
FT                                {ECO:0000259|PROSITE:PS50042}.
FT   DOMAIN      394    507       N-terminal Ras-GEF. {ECO:0000259|PROSITE:
FT                                PS50212}.
FT   DOMAIN      512    582       PDZ. {ECO:0000259|PROSITE:PS50106}.
FT   DOMAIN      733    819       Ras-associating. {ECO:0000259|PROSITE:
FT                                PS50200}.
FT   DOMAIN      844   1071       Ras-GEF. {ECO:0000259|PROSITE:PS50009}.
FT   REGION      167    186       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A287DDU2}.
FT   REGION      195    226       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A287DDU2}.
FT   REGION     1129   1178       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A287DDU2}.
FT   REGION     1219   1312       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A287DDU2}.
FT   REGION     1375   1408       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A287DDU2}.
FT   REGION     1456   1523       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A287DDU2}.
FT   REGION     1541   1650       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A287DDU2}.
FT   COILED      355    375       {ECO:0000256|SAM:Coils}.
FT   COMPBIAS    208    223       Acidic. {ECO:0000256|MobiDB-lite:
FT                                A0A287DDU2}.
FT   COMPBIAS   1232   1312       Polar. {ECO:0000256|MobiDB-lite:
FT                                A0A287DDU2}.
FT   COMPBIAS   1456   1487       Polar. {ECO:0000256|MobiDB-lite:
FT                                A0A287DDU2}.
FT   COMPBIAS   1490   1504       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                A0A287DDU2}.
FT   COMPBIAS   1506   1520       Polar. {ECO:0000256|MobiDB-lite:
FT                                A0A287DDU2}.
SQ   SEQUENCE   1650 AA;  184536 MW;  9982D6422A9F5F9C CRC64;
     MEALSNLREH QLRLMCETVR YERHEANEVL YYPDDIGTCW YILLSGSVFI KESMFLPRSS
     FGKRSAGSFR RGCECIVLEP SEMIVVDYMD ENEEYFQRQA SHRQSRRRFR KINQKGERQT
     IIDTVDPYPV GKPPLPRGYH TECTKSQLPA DFTKLHLTDS LHPQVTHVSS SHSGCSITSD
     SGSSSLSDIY QATESEAGDM DLSGLPETAV DSEDDDDEED IERASDPLMS RDIVRDCLEK
     DPIDRTDDDI EQLLEFMHQL PAFANMTMSV RRELCAVMVF AVVERAGTIV LNDGEELDSW
     SVILNGSVEV TYPDGKAEIL CMGNSFGVSP TMDKEYMKGV MRTKVDDCQF VCIAQQDYCR
     ILNQVEKNMQ KVEEEGEIVM VKEHRELDRT GTRKGHIVIK GTSERLTMHL VEEHSVVDPT
     FIEDFLLTYR TFLSSPMEVG KKLLEWFNDP SLRDKVTRVV LLWVNNHFND FEGDPAMTRF
     LEEFENNLER EKMGGHLRLL NIACAAKAKR RLMTLTKPSR EAPLPFILLG GSEKGFGIFV
     DSVDSGSKAT EAGLKRGDQI LEVNGQNFEN IQLSKAMEIL RNNTHLSITV KTNLFVFKEL
     LTRLSEEKRN GAPHLPKIGD IKKASRYSIP DLAVDVEQVI GLEKVNKKSK ANTVGGRNKL
     KKILDKTRIS ILPQKPYNDI GIGQSQDDSI VGLRQTKHIP TALPVSGTLS SSNPDLLQSH
     HRILDFSTTP DLPDQVLRVF KADQQSRYIM ISKDTTAKEV VIQAIREFAV TATPDQYSLC
     EVSVTPEGVI KQRRLPDQLS KLADRIQLSG RYYLKNNMET ETLCSDEDAQ ELLRESQISL
     LQLSTVEVAT QLSMRNFELF RNIEPTEYID DLFKLKSKTS CHNLKKFEEV INQETFWVAS
     EILRETNQLK RMKIIKHFIK IALHCRECKN FNSMFAIISG LNLAPVARLR ATWEKLPNKY
     EKLFQDLQDL FDPSRNMAKY RNVLNSQNLQ PPIIPLFPVI KKDLTFLHEG NDSKVDGLVN
     FEKLRMIAKE IRHVGRMASV NMDPALMFRT RKKKWRSLGS LSQGSTNATV LDVAQTGGHK
     KRVRRSSFLN AKKLYEDAQM ARKVKQYLSN LELEMDEESL QTLSLQCEPA TNTLPKNPGD
     KKPVKSETSP VAPRAGSQQK AQPQPPAQPQ QPPHKANQGL QVPAVALYPS RKKVPVKDLP
     PFGINSPQAL KKILSLSEEG SLERHKKPAD DTISNASSQL SSPPTSPQSS PRKGGSGNQL
     RSFGSGQLDL TSSSSSLGSY TLAPSGTVDN FSDSGHSEIS SRSSIVSNSS FDSVPVSLHD
     ERRQRHSVSI VETNLGVGRT ERRTMIEPDQ YSLGSYVPMS ESRGLYATAT VISSPSTEEL
     SQDQGDRASL DAADSGRGSW TSCSSGSHDN IQTIQHQRSW ETLPFGHTHF DYSGDPAGLW
     ASSSHMDQMM FSDHSAKYNR QNQSRESLEQ AQSRASWASS TGYWGEDSEG DTGTIKRRGG
     KDVSIEAEST SITSATTEET KPVPVPAHIA VTPSTAKGVI ARKEGRYREP PPTPPGYIGI
     PITDFPEGHS HPARKPPDYN VALQRSRMVA RSSDASGPSP GQQPPGPPTS SRPVSKPQWH
     KPSESDPRLA PRQSQGFSAE EDEDEQVSAV
//
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