IQEC3_MOUSE
ID IQEC3_MOUSE Reviewed; 1195 AA.
AC Q3TES0; Q3UHP8; Q80TJ8;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=IQ motif and SEC7 domain-containing protein 3;
GN Name=Iqsec3; Synonyms=Kiaa1110;
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 MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 285-1195.
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [3]
RP TISSUE SPECIFICITY.
RX PubMed=17981261; DOI=10.1016/j.bbrc.2007.10.041;
RA Hattori Y., Ohta S., Hamada K., Yamada-Okabe H., Kanemura Y., Matsuzaki Y.,
RA Okano H., Kawakami Y., Toda M.;
RT "Identification of a neuron-specific human gene, KIAA1110, that is a
RT guanine nucleotide exchange factor for ARF1.";
RL Biochem. Biophys. Res. Commun. 364:737-742(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-256, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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 [5]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH GPHN.
RX PubMed=27609886; DOI=10.1126/science.aag0821;
RA Uezu A., Kanak D.J., Bradshaw T.W., Soderblom E.J., Catavero C.M.,
RA Burette A.C., Weinberg R.J., Soderling S.H.;
RT "Identification of an elaborate complex mediating postsynaptic
RT inhibition.";
RL Science 353:1123-1129(2016).
CC -!- FUNCTION: Acts as a guanine nucleotide exchange factor (GEF) for ARF1.
CC {ECO:0000250|UniProtKB:Q9UPP2}.
CC -!- SUBUNIT: Interacts with DLG1 and DLG4 (By similarity). Interacts with
CC GPHN (PubMed:27609886). {ECO:0000250|UniProtKB:Q76M68,
CC ECO:0000269|PubMed:27609886}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9UPP2}.
CC Postsynaptic density {ECO:0000269|PubMed:27609886}.
CC -!- TISSUE SPECIFICITY: Expressed specifically in the adult brain, but not
CC in the fetal brain at 14 dpc. {ECO:0000269|PubMed:17981261}.
CC -!- SIMILARITY: Belongs to the BRAG family. {ECO:0000305}.
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DR EMBL; AK147268; BAE27809.1; -; mRNA.
DR EMBL; AK169437; BAE41178.1; -; mRNA.
DR EMBL; AK122446; BAC65728.1; -; mRNA.
DR CCDS; CCDS20491.1; -.
DR RefSeq; NP_001028526.1; NM_001033354.3.
DR AlphaFoldDB; Q3TES0; -.
DR SMR; Q3TES0; -.
DR BioGRID; 232542; 7.
DR IntAct; Q3TES0; 5.
DR MINT; Q3TES0; -.
DR STRING; 10090.ENSMUSP00000038653; -.
DR iPTMnet; Q3TES0; -.
DR PhosphoSitePlus; Q3TES0; -.
DR SwissPalm; Q3TES0; -.
DR MaxQB; Q3TES0; -.
DR PaxDb; Q3TES0; -.
DR PeptideAtlas; Q3TES0; -.
DR PRIDE; Q3TES0; -.
DR ProteomicsDB; 269327; -.
DR Antibodypedia; 50062; 65 antibodies from 14 providers.
DR DNASU; 243621; -.
DR Ensembl; ENSMUST00000046373; ENSMUSP00000038653; ENSMUSG00000040797.
DR GeneID; 243621; -.
DR KEGG; mmu:243621; -.
DR UCSC; uc009dom.2; mouse.
DR CTD; 440073; -.
DR MGI; MGI:2677208; Iqsec3.
DR VEuPathDB; HostDB:ENSMUSG00000040797; -.
DR eggNOG; KOG0931; Eukaryota.
DR GeneTree; ENSGT00940000155908; -.
DR HOGENOM; CLU_004328_2_0_1; -.
DR InParanoid; Q3TES0; -.
DR OMA; LGSCIQQ; -.
DR OrthoDB; 837077at2759; -.
DR PhylomeDB; Q3TES0; -.
DR TreeFam; TF323811; -.
DR BioGRID-ORCS; 243621; 6 hits in 73 CRISPR screens.
DR ChiTaRS; Iqsec3; mouse.
DR PRO; PR:Q3TES0; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q3TES0; protein.
DR Bgee; ENSMUSG00000040797; Expressed in central gray substance of midbrain and 83 other tissues.
DR ExpressionAtlas; Q3TES0; baseline and differential.
DR Genevisible; Q3TES0; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0098982; C:GABA-ergic synapse; IDA:SynGO.
DR GO; GO:0098690; C:glycinergic synapse; IDA:SynGO.
DR GO; GO:0060077; C:inhibitory synapse; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0014069; C:postsynaptic density; IDA:UniProtKB.
DR GO; GO:0045211; C:postsynaptic membrane; IDA:UniProtKB.
DR GO; GO:0099629; C:postsynaptic specialization of symmetric synapse; IDA:SynGO.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0090630; P:activation of GTPase activity; ISO:MGI.
DR GO; GO:0032012; P:regulation of ARF protein signal transduction; IEA:InterPro.
DR GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; ISO:MGI.
DR GO; GO:0050808; P:synapse organization; 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; 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; 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; Phosphoprotein; Reference proteome; Synapse.
FT CHAIN 1..1195
FT /note="IQ motif and SEC7 domain-containing protein 3"
FT /id="PRO_0000245611"
FT DOMAIN 312..341
FT /note="IQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 648..841
FT /note="SEC7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00189"
FT DOMAIN 854..987
FT /note="PH"
FT REGION 62..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 229..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 440..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 516..615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1004..1100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1138..1175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 20..56
FT /evidence="ECO:0000255"
FT COMPBIAS 64..80
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..135
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 596..615
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1004..1025
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1043..1057
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1066..1100
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1156..1174
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 256
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 285..298
FT /note="ASEYELSLDLKNKQ -> HRAEACLLRPGFPK (in Ref. 2;
FT BAE41178)"
FT /evidence="ECO:0000305"
FT CONFLICT 382
FT /note="P -> S (in Ref. 2; BAE41178)"
FT /evidence="ECO:0000305"
FT CONFLICT 722
FT /note="D -> E (in Ref. 1; BAE27809)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1195 AA; 129119 MW; 3674AA84857DD438 CRC64;
MESLLENPVR AVLYLKELTA IVQNQQSLIH TQRQRIDELE RRLDELSAEN RSLWEHQQLL
QAQPPPGLVP PPPSAPLPAP AVTAPAAAAA QEPLQDHGQL IPASPEPPLQ HHGQLLAQPQ
PAPSSRVQTP QSPHQHPVAP GAIADKEKER PSSCCAAAGA LLQHASPAAL GKGVLSRRPE
NETVLHQFCC PAADTEQKPA CSDLASQSDG SCAQAGGGME DSVVAAVAAG RPSAHAPKAQ
APELQQEEER PGAVGSPRAG PLRAASPGRQ QPALATALCS HTPAASEYEL SLDLKNKQIE
MLEHKYGGHL VSRRAACTIQ TAFRQYQLSK NFEKIRNSLL ESRLPRRISL RKVRAPTAES
LVAEKALLEG CGLLGLPLGR SPSLPPTFAG SLTELEDSFT EQVQSLAKSI DDALSTWSLK
TMCSLQESGA YQLHQALHPS AGQPGLETEA AAREPESGPG SGDEAGGLPQ GHSGTLMMAF
RDVTVQIANQ NISVSSSTAL SVANCLGAQT AQATAEPAAA QAEQEDTADQ EVSEVPASEQ
MDPPSEDSEA AESRAQSAQE PAVAQAVVEE AVATEAEEEE EGAKQAGKGA EAEGGDNSEQ
LSSSSASTKS AKSSSEASAA ASKEALQAVI LSLPRYHCEN PASCRSPTLS TDTLRKRLYR
IGLNLFNINP DKGIQFLISR GFIPDTPIGV AHFLLQRKGL SRQMIGEFLG NSKKQFNRDV
LDCVVDEMDF SNMELDEALR KFQAHIRVQG EAQKVERLIE AFSQRYCMCN PEVVQQFHNP
DTIFILAFAI ILLNTDMYSP NIKPDRKMML EDFIRNLRGV DDGADIPREL VVGIYERIQQ
KELKSNEDHV TYVTKVEKSI VGMKTVLSMP HRRLVCCSRL FEVTDVNKLQ KQAAHQREVF
LFNDLLVILK LCPKKKSSFT YTFCKAVGLL GMRFHLFENE YYSHGITLAT PLSGSEKKQV
LHFCALGSDE MQKFVEDLKE SIAEVTELEQ IRIEWELEKQ QGTKTLSVRS AGAQGDPQSK
QGSPTAKREA MAGEKAAESS GEVSIHNRLQ TSQHSPKLGV ERGAPAPSPP TSPPPLPPDP
QPSPLREQPP PLPLPPPTPP GTLVQCQQIV KVIVLDKPCL ARMEPLLSQA LSCYASSSSD
SCGSTPLRGP GSPVKVIHQP PLPPPPPPYN HPHQFCPPGS MLLRRRYSSG SRSLV
