IQCE_MOUSE
ID IQCE_MOUSE Reviewed; 778 AA.
AC Q6PCQ0; Q8CDZ1; Q9D9U3;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=IQ domain-containing protein E;
GN Name=Iqce;
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] (ISOFORMS 2 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Head, and Testis;
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] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-322 AND SER-661, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Pancreas;
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 [4]
RP FUNCTION, IDENTIFICATION IN THE EVC COMPLEX, INTERACTION WITH EFCAB7; EVC
RP AND EVC2, SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=24582806; DOI=10.1016/j.devcel.2014.01.021;
RA Pusapati G.V., Hughes C.E., Dorn K.V., Zhang D., Sugianto P., Aravind L.,
RA Rohatgi R.;
RT "EFCAB7 and IQCE regulate hedgehog signaling by tethering the EVC-EVC2
RT complex to the base of primary cilia.";
RL Dev. Cell 28:483-496(2014).
CC -!- FUNCTION: Component of the EvC complex that positively regulates
CC ciliary Hedgehog (Hh) signaling (PubMed:24582806). Required for proper
CC limb morphogenesis (By similarity). {ECO:0000250|UniProtKB:Q6IPM2,
CC ECO:0000269|PubMed:24582806}.
CC -!- SUBUNIT: Component of the EvC complex composed of EFCAB7, IQCE, EVC2
CC and EVC; built from two subcomplexes, EVC2:EVC and EFCAB7:IQCE
CC (PubMed:24582806). Interacts (via N-terminus) with EFCAB7 (via EF-hands
CC 1 and 2); this interaction anchors the EVC-EVC2 complex in a signaling
CC microdomain at the base of cilia and stimulates the Hedgehog (Hh)
CC pathway. Interacts with EVC2 (via N-terminal end) (PubMed:24582806).
CC Interacts with EVC (PubMed:24582806). {ECO:0000269|PubMed:24582806}.
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium membrane
CC {ECO:0000269|PubMed:24582806}; Peripheral membrane protein
CC {ECO:0000269|PubMed:24582806}; Cytoplasmic side
CC {ECO:0000269|PubMed:24582806}. Note=The EvC complex localizes at the
CC base of cilia in the EvC zone of primary cilia in a EFCAB7-dependent
CC manner (PubMed:24582806). {ECO:0000269|PubMed:24582806}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q6PCQ0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6PCQ0-2; Sequence=VSP_024436, VSP_024439;
CC Name=3;
CC IsoId=Q6PCQ0-3; Sequence=VSP_024436, VSP_024437, VSP_024438;
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DR EMBL; AK006472; BAB24605.1; -; mRNA.
DR EMBL; AK029333; BAC26400.1; -; mRNA.
DR EMBL; BC059223; AAH59223.1; -; mRNA.
DR CCDS; CCDS39358.1; -. [Q6PCQ0-1]
DR CCDS; CCDS84987.1; -. [Q6PCQ0-2]
DR RefSeq; NP_001334446.1; NM_001347517.1. [Q6PCQ0-2]
DR RefSeq; NP_083109.2; NM_028833.3. [Q6PCQ0-1]
DR AlphaFoldDB; Q6PCQ0; -.
DR SMR; Q6PCQ0; -.
DR BioGRID; 216599; 6.
DR STRING; 10090.ENSMUSP00000045913; -.
DR iPTMnet; Q6PCQ0; -.
DR PhosphoSitePlus; Q6PCQ0; -.
DR EPD; Q6PCQ0; -.
DR MaxQB; Q6PCQ0; -.
DR PaxDb; Q6PCQ0; -.
DR PRIDE; Q6PCQ0; -.
DR ProteomicsDB; 269087; -. [Q6PCQ0-1]
DR ProteomicsDB; 269088; -. [Q6PCQ0-2]
DR ProteomicsDB; 269089; -. [Q6PCQ0-3]
DR DNASU; 74239; -.
DR Ensembl; ENSMUST00000041783; ENSMUSP00000045913; ENSMUSG00000036555. [Q6PCQ0-1]
DR Ensembl; ENSMUST00000077890; ENSMUSP00000077050; ENSMUSG00000036555. [Q6PCQ0-2]
DR GeneID; 74239; -.
DR KEGG; mmu:74239; -.
DR UCSC; uc009ahx.1; mouse. [Q6PCQ0-1]
DR UCSC; uc009ahy.1; mouse. [Q6PCQ0-2]
DR UCSC; uc009ahz.1; mouse. [Q6PCQ0-3]
DR CTD; 23288; -.
DR MGI; MGI:1921489; Iqce.
DR VEuPathDB; HostDB:ENSMUSG00000036555; -.
DR eggNOG; ENOG502QUCA; Eukaryota.
DR GeneTree; ENSGT00940000163679; -.
DR HOGENOM; CLU_015416_1_0_1; -.
DR InParanoid; Q6PCQ0; -.
DR OMA; DNQQMKA; -.
DR OrthoDB; 1143812at2759; -.
DR PhylomeDB; Q6PCQ0; -.
DR TreeFam; TF351136; -.
DR BioGRID-ORCS; 74239; 4 hits in 71 CRISPR screens.
DR PRO; PR:Q6PCQ0; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q6PCQ0; protein.
DR Bgee; ENSMUSG00000036555; Expressed in spermatid and 215 other tissues.
DR ExpressionAtlas; Q6PCQ0; baseline and differential.
DR Genevisible; Q6PCQ0; MM.
DR GO; GO:0060170; C:ciliary membrane; IDA:UniProtKB.
DR GO; GO:0019898; C:extrinsic component of membrane; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0098797; C:plasma membrane protein complex; IDA:UniProtKB.
DR GO; GO:0035108; P:limb morphogenesis; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00612; IQ; 2.
DR SMART; SM00015; IQ; 2.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50096; IQ; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cell projection; Coiled coil;
KW Membrane; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..778
FT /note="IQ domain-containing protein E"
FT /id="PRO_0000284111"
FT DOMAIN 553..582
FT /note="IQ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 615..644
FT /note="IQ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT REGION 1..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 83..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 348..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 443..462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 474..529
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 573..612
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 651..778
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 157..323
FT /evidence="ECO:0000255"
FT COILED 398..486
FT /evidence="ECO:0000255"
FT COMPBIAS 1..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 353..384
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 496..511
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 587..602
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 735..749
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 322
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 661
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 87..131
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_024436"
FT VAR_SEQ 276..290
FT /note="PMVEKKLGVKRQKKM -> YALMWGLSPVSLWRL (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_024437"
FT VAR_SEQ 291..778
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_024438"
FT VAR_SEQ 669
FT /note="P -> PGKNSEASSGEAAKDEDEAEEPPDLQPYS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_024439"
FT CONFLICT 587
FT /note="P -> Q (in Ref. 1; BAB24605)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 778 AA; 86356 MW; 607FE6BDAED56BA6 CRC64;
MSLGTTDIAS ETGDDSLSAI TFESDIESKT KRKSFHKPPS TSPKSPYYSK PRKVTSWRSL
KTAGSMPLSS RMSLTPQKLW LGSSKQGSVA QPPSPTLTSE HAWTHPPSCT PDYLTEAVRA
KRADLRRSGS HGHVSGTSVY REKEDMYDEI IELKKSLHMQ KSDVDLMRTK LRRLEEENSR
KDRQIEQLLD PSRGPDFVRT LAEKKPDTGW VITGLKQRIF RLEQQCKEKD NTINKLQTDM
KTTNLEEMRI AMETYYEEIH RLQTLLASSE ATGKKPMVEK KLGVKRQKKM SSALLNLTRS
VQELTEENQS LKEDLDRMLS NSPTISKIKG YGDWSKPRLL RRIAELEKKV SSSESPKQST
SELVNPNPLV RSPSNISVQK QPKGDQSPED LPKVAPCEEQ EHLQGTVKSL REELGALQEQ
LLEKDLEMKQ LLQSKIDLEK ELETAREGEK GRQEQEQALR EEVEALTKKC QELEEAKREE
KNSFVAVTHE AHPELHAPSP CSRHSEPDSD NSAGEEGSSQ PPAPCSEERR EAAIRTLQAQ
WKAHRRKKRE AALDEAATVL QAAFRGHLAR SKLVRSKVPD SRSPSLPGLL SPLNQSSPAP
RVLSPISPAE ENPTQEEAVI VIQSILRGYL AQARFIASCC REIAASSQRE TVSLTPSGSA
SPPSLRASPG VIRKELCASE ELRETSASEP APSVPYSAQG GHGDCPSSSS LEAVPSMKDA
MCEERSSSPR SAGPSLAEPS PPELQPLSPP PVEDICSDDS DDIIFSPFLP RKKSPSPF
