IQEC2_MOUSE
ID IQEC2_MOUSE Reviewed; 1478 AA.
AC Q5DU25; E9QK46;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=IQ motif and SEC7 domain-containing protein 2;
GN Name=Iqsec2; Synonyms=Kiaa0522;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 833-1478.
RC TISSUE=Brain;
RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT screening of terminal sequences of cDNA clones randomly sampled from size-
RT fractionated libraries.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1148 AND SER-1151, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1119, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-383 AND SER-402, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82; SER-228; SER-383;
RP SER-402; SER-491; SER-518; SER-597; SER-617; SER-731; SER-734; SER-1148;
RP SER-1151; SER-1162 AND SER-1163, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, Spleen,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-1335, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Is a guanine nucleotide exchange factor for the ARF GTP-
CC binding proteins. {ECO:0000250|UniProtKB:Q5JU85}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the BRAG family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC083816; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK220345; BAD90410.1; -; mRNA.
DR RefSeq; XP_006528908.1; XM_006528845.1.
DR AlphaFoldDB; Q5DU25; -.
DR SMR; Q5DU25; -.
DR BioGRID; 232821; 11.
DR IntAct; Q5DU25; 8.
DR MINT; Q5DU25; -.
DR STRING; 10090.ENSMUSP00000093995; -.
DR iPTMnet; Q5DU25; -.
DR PhosphoSitePlus; Q5DU25; -.
DR jPOST; Q5DU25; -.
DR MaxQB; Q5DU25; -.
DR PaxDb; Q5DU25; -.
DR PRIDE; Q5DU25; -.
DR ProteomicsDB; 301667; -.
DR DNASU; 245666; -.
DR GeneID; 245666; -.
DR CTD; 23096; -.
DR MGI; MGI:3528396; Iqsec2.
DR eggNOG; KOG0931; Eukaryota.
DR InParanoid; Q5DU25; -.
DR OrthoDB; 837077at2759; -.
DR BioGRID-ORCS; 245666; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Iqsec2; mouse.
DR PRO; PR:Q5DU25; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q5DU25; protein.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0098684; C:photoreceptor ribbon synapse; IDA:SynGO.
DR GO; GO:0098839; C:postsynaptic density membrane; IDA:SynGO.
DR GO; GO:0099092; C:postsynaptic density, intracellular component; IDA:SynGO.
DR GO; GO:0098831; C:presynaptic active zone cytoplasmic component; IDA:SynGO.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; ISO:MGI.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISO:MGI.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; ISO:MGI.
DR GO; GO:1900454; P:positive regulation of long-term synaptic depression; ISO:MGI.
DR GO; GO:0051968; P:positive regulation of synaptic transmission, glutamatergic; ISO:MGI.
DR GO; GO:0032012; P:regulation of ARF protein signal transduction; IEA:InterPro.
DR GO; GO:0098696; P:regulation of neurotransmitter receptor localization to postsynaptic specialization membrane; ISO:MGI.
DR CDD; cd13318; PH_IQSEC; 1.
DR CDD; cd00171; Sec7; 1.
DR Gene3D; 1.10.1000.11; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR033742; IQSEC_PH.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR023394; Sec7_C_sf.
DR InterPro; IPR000904; Sec7_dom.
DR InterPro; IPR035999; Sec7_dom_sf.
DR Pfam; PF16453; IQ_SEC7_PH; 1.
DR Pfam; PF01369; Sec7; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00222; Sec7; 1.
DR SUPFAM; SSF48425; SSF48425; 1.
DR PROSITE; PS50096; IQ; 1.
DR PROSITE; PS50190; SEC7; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Methylation; Phosphoprotein; Reference proteome.
FT CHAIN 1..1478
FT /note="IQ motif and SEC7 domain-containing protein 2"
FT /id="PRO_0000245609"
FT DOMAIN 337..366
FT /note="IQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 736..929
FT /note="SEC7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00189"
FT DOMAIN 941..1075
FT /note="PH"
FT REGION 63..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 104..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 161..280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 469..568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 613..716
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1081..1249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1261..1478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 23..74
FT /evidence="ECO:0000255"
FT COMPBIAS 63..81
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..181
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..238
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..269
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..552
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 553..568
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 632..658
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 684..712
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1100..1114
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1148..1162
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1166..1183
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1184..1198
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1227..1241
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1264..1306
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1356..1370
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1413..1464
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 82
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 228
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 334
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5JU85"
FT MOD_RES 383
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 402
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 491
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 518
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 597
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 617
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 731
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 734
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1097
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5JU85"
FT MOD_RES 1119
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
FT MOD_RES 1133
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5JU85"
FT MOD_RES 1148
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1151
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1162
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1163
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1335
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT CONFLICT 833
FT /note="H -> L (in Ref. 2; BAD90410)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1478 AA; 161787 MW; E61C5F88BBF34578 CRC64;
MEAGSGPPGG PGSESPNRAV EYLLELNNII ESQQQLLETQ RRRIEELEGQ LDQLTQENRD
LREESQLHRG ELHRDPLGAR DSPGRESQYQ NLRETQFHHR ELRESQFHQA SRDVGYPNRD
GAYQNREAIY RDKEREASYQ LQDTTGYTAR ERDVAQCHLH HENPALGRER GGREAGPAHP
GREKEAGYSA AVGVGQRPPR ERGQLSRGAS RSSSPGAGGG HSTSTSTSPA TTLQRNVEGD
APGSDLSTAV DSPGSQPPYR LSQLPPTSSH MGGPPAGVGL PWAQRARLQP ASVALRKQEE
EEIKRSKALS DSYELSTDLQ DKKVEMLERK YGGSFLSRRA ARTIQTAFRQ YRMNKNFERL
RSSASESRMS RRIILSNMRM QFSFEEYEKA QNPAYFEGKP ASLDEGAMAG ARSHRLERGL
PYGGSCGGGI DGGGSSVTTS GEFSNDITEL EDSFSKQVKS LAESIDEALN CHPSGPMSEE
PGSAQLEKRE SKEQQEDSSA TSFSDLPLYL DDPVPPPSPE RLPSTEPPPQ GRPEFWAPAP
LPPVPPPMPP GTREDGSREE GTRRGPGCLE CRDFRLRAAH LPLLTIEPPS DSSVDLSDRS
DRGSVHRQLV YEADGCSPHG TLKHKGPPGR APIPHRHYPA PEGPAPAPPG PLPPAPNSGT
GPSGVAGGRR LGKCEAAGEN SDGGDNESLE SSSNSNETIN CSSGSSSRDS LREPPATGLC
KQTYQRETRH SWDSPAFNND VVQRRHYRIG LNLFNKKPEK GIQYLIERGF LSDTPVGVAH
FILERKGLSR QMIGEFLGNR QKQFNRDVLD CVVDEMDFSS MDLDDALRKF QSHIRVQGEA
QKVERLIEAF SQRYCVCNPA LVRQFRNPDT IFILAFAIIL LNTDMYSPSV KAERKMKLDD
FIKNLRGVDN GEDIPRDLLV GIYQRIQGRE LRTNDDHVSQ VQAVERMIVG KKPVLSLPHR
RLVCCCQLYE VPDPNRPQRL GLHQREVFLF NDLLVVTKIF QKKKILVTYS FRQSFPLVEM
HMQLFQNSYY QFGIKLLSAV PGGERKVLII FNAPSLQDRL RFTSDLRESI AEVQEMEKYR
VESELEKQKG MMRPNASQPG GAKDSVNGTL ARSSLEDTYG AGDGLKRGAL SSSLRDLSDA
GKRGRRNSVG SLDSTIEGSV ISSPRPHQRM PPPPPPPPPE EYKSQRPVSN SSSFLGSLFG
SKRGKGPFQM PPPPTGQASA SSSSASSTHH HHHHHHHGHS HGGLGVLPDG QSKLQALHAQ
YCQGPGPAPP PYLPPQQPPL PPPPQQPPPL PQLGSIPPPP ASAPPVGPHR HFHAHGPVPG
PQHYTLGRPG RAPRRGAGGH PQFAPHGRHP LHQPTSPLPL YSPAPQHPPA HKQGPKHFIF
SHHPQMMPAA GAAGGPGSRP PGGSYSHPHH PQSPLSPHSP IPPHPSYPPL PPPSPHTPHS
PLPPTSPHGP LHASGPPGTA NPPSANPKAK PSRISTVV
