ID IQCB1_MOUSE Reviewed; 598 AA. AC Q8BP00; Q3TNK4; Q8K306; DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot. DT 10-MAY-2004, sequence version 2. DT 27-MAR-2024, entry version 151. DE RecName: Full=IQ calmodulin-binding motif-containing protein 1; GN Name=Iqcb1; Synonyms=Kiaa0036; 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] (ISOFORM 1). RC STRAIN=C57BL/6J; TISSUE=Ovary, and Spleen; 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 2). RC TISSUE=Mammary cancer; 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 INTERACTION WITH CALMODULIN, AND TISSUE SPECIFICITY. RX PubMed=15723066; DOI=10.1038/ng1520; RA Otto E.A., Loeys B., Khanna H., Hellemans J., Sudbrak R., Fan S., Muerb U., RA O'Toole J.F., Helou J., Attanasio M., Utsch B., Sayer J.A., Lillo C., RA Jimeno D., Coucke P., De Paepe A., Reinhardt R., Klages S., Tsuda M., RA Kawakami I., Kusakabe T., Omran H., Imm A., Tippens M., Raymond P.A., RA Hill J., Beales P., He S., Kispert A., Margolis B., Williams D.S., RA Swaroop A., Hildebrandt F.; RT "Nephrocystin-5, a ciliary IQ domain protein, is mutated in Senior-Loken RT syndrome and interacts with RPGR and calmodulin."; RL Nat. Genet. 37:282-288(2005). RN [4] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=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 [5] RP SUBCELLULAR LOCATION, AND INTERACTION WITH CEP290; NPHP1; INVS; NPHP4; RP RPGRIP1L AND ATXN10. RX PubMed=21565611; DOI=10.1016/j.cell.2011.04.019; RA Sang L., Miller J.J., Corbit K.C., Giles R.H., Brauer M.J., Otto E.A., RA Baye L.M., Wen X., Scales S.J., Kwong M., Huntzicker E.G., Sfakianos M.K., RA Sandoval W., Bazan J.F., Kulkarni P., Garcia-Gonzalo F.R., Seol A.D., RA O'Toole J.F., Held S., Reutter H.M., Lane W.S., Rafiq M.A., Noor A., RA Ansar M., Devi A.R., Sheffield V.C., Slusarski D.C., Vincent J.B., RA Doherty D.A., Hildebrandt F., Reiter J.F., Jackson P.K.; RT "Mapping the NPHP-JBTS-MKS protein network reveals ciliopathy disease genes RT and pathways."; RL Cell 145:513-528(2011). CC -!- FUNCTION: Involved in ciliogenesis. The function in an early step in CC cilia formation depends on its association with CEP290/NPHP6 (By CC similarity). Involved in regulation of the BBSome complex integrity, CC specifically for presence of BBS2 and BBS5 in the complex, and in CC ciliary targeting of selected BBSome cargos. May play a role in CC controlling entry of the BBSome complex to cilia possibly implicating CC CEP290/NPHP6 (By similarity). {ECO:0000250|UniProtKB:Q15051, CC ECO:0000269|PubMed:21565611}. CC -!- SUBUNIT: Interacts with calmodulin (PubMed:15723066). Interacts with CC CEP290/NPHP6; IQCB1/NPHP5 and CEP290/NPHP6; are proposed to form a CC functional NPHP5-6 module localized to the centrosome. Interacts with CC ATXN10. Interacts with NPHP1, INVS, NPHP4 and RPGRIP1L; these CC interactions likely require additional interactors (PubMed:21565611). CC Associates with the BBSome complex; interacts with BBS1, BBS2, BBS4, CC BBS5, BBS7, BBS8 and BBS9 (By similarity). CC {ECO:0000250|UniProtKB:Q15051, ECO:0000269|PubMed:15723066, CC ECO:0000269|PubMed:21565611}. CC -!- INTERACTION: CC Q8BP00; P28658: Atxn10; NbExp=2; IntAct=EBI-4282243, EBI-4284019; CC Q8BP00; Q6A078: Cep290; NbExp=6; IntAct=EBI-4282243, EBI-1811999; CC Q8BP00; O89019: Invs; NbExp=2; IntAct=EBI-4282243, EBI-4281337; CC Q8BP00; Q8CG73: Rpgrip1l; NbExp=2; IntAct=EBI-4282243, EBI-4281130; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing CC center, centrosome {ECO:0000250|UniProtKB:Q15051}. Note=Localization to CC the centrosome depends on the interaction with CEP290. CC {ECO:0000250|UniProtKB:Q15051}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q8BP00-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8BP00-2; Sequence=VSP_010246; CC -!- TISSUE SPECIFICITY: Localized to the outer segment and connecting cilia CC of photoreceptor cells. {ECO:0000269|PubMed:15723066}. CC -!- DOMAIN: The IQ domains mediate the interaction with calmodulin. CC {ECO:0000250|UniProtKB:Q15051}. 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; AK078554; BAC37333.1; -; mRNA. DR EMBL; AK165220; BAE38084.1; -; mRNA. DR EMBL; BC029084; AAH29084.1; -; mRNA. DR CCDS; CCDS28157.1; -. [Q8BP00-1] DR RefSeq; NP_796102.2; NM_177128.4. [Q8BP00-1] DR RefSeq; XP_006522310.1; XM_006522247.3. [Q8BP00-1] DR RefSeq; XP_006522311.1; XM_006522248.2. [Q8BP00-1] DR RefSeq; XP_006522312.1; XM_006522249.3. [Q8BP00-1] DR AlphaFoldDB; Q8BP00; -. DR SMR; Q8BP00; -. DR BioGRID; 235913; 168. DR CORUM; Q8BP00; -. DR IntAct; Q8BP00; 135. DR MINT; Q8BP00; -. DR STRING; 10090.ENSMUSP00000023535; -. DR iPTMnet; Q8BP00; -. DR PhosphoSitePlus; Q8BP00; -. DR SwissPalm; Q8BP00; -. DR EPD; Q8BP00; -. DR MaxQB; Q8BP00; -. DR PaxDb; 10090-ENSMUSP00000023535; -. DR PeptideAtlas; Q8BP00; -. DR ProteomicsDB; 301664; -. [Q8BP00-1] DR ProteomicsDB; 301665; -. [Q8BP00-2] DR Pumba; Q8BP00; -. DR Antibodypedia; 32846; 226 antibodies from 28 providers. DR Ensembl; ENSMUST00000023535.4; ENSMUSP00000023535.4; ENSMUSG00000022837.15. [Q8BP00-1] DR Ensembl; ENSMUST00000114819.8; ENSMUSP00000110467.2; ENSMUSG00000022837.15. [Q8BP00-2] DR GeneID; 320299; -. DR KEGG; mmu:320299; -. DR UCSC; uc007zda.1; mouse. [Q8BP00-2] DR UCSC; uc007zdb.2; mouse. [Q8BP00-1] DR AGR; MGI:2443764; -. DR CTD; 9657; -. DR MGI; MGI:2443764; Iqcb1. DR VEuPathDB; HostDB:ENSMUSG00000022837; -. DR eggNOG; KOG0160; Eukaryota. DR GeneTree; ENSGT00390000002188; -. DR HOGENOM; CLU_035387_0_0_1; -. DR InParanoid; Q8BP00; -. DR OMA; IHGGWAT; -. DR OrthoDB; 3670690at2759; -. DR PhylomeDB; Q8BP00; -. DR TreeFam; TF351884; -. DR Reactome; R-MMU-5620912; Anchoring of the basal body to the plasma membrane. DR BioGRID-ORCS; 320299; 1 hit in 77 CRISPR screens. DR ChiTaRS; Iqcb1; mouse. DR PRO; PR:Q8BP00; -. DR Proteomes; UP000000589; Chromosome 16. DR RNAct; Q8BP00; Protein. DR Bgee; ENSMUSG00000022837; Expressed in retinal neural layer and 218 other cell types or tissues. DR GO; GO:0005813; C:centrosome; ISO:MGI. DR GO; GO:0005929; C:cilium; IBA:GO_Central. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW. DR GO; GO:0045171; C:intercellular bridge; ISO:MGI. DR GO; GO:0015630; C:microtubule cytoskeleton; ISO:MGI. DR GO; GO:0072686; C:mitotic spindle; ISO:MGI. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0032391; C:photoreceptor connecting cilium; IDA:HGNC-UCL. DR GO; GO:0001750; C:photoreceptor outer segment; IDA:HGNC-UCL. DR GO; GO:0062063; F:BBSome binding; IEA:Ensembl. DR GO; GO:0005516; F:calmodulin binding; ISS:HGNC-UCL. DR GO; GO:0019899; F:enzyme binding; ISO:MGI. DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IEA:Ensembl. DR GO; GO:0060271; P:cilium assembly; IMP:UniProtKB. DR GO; GO:0061824; P:cytosolic ciliogenesis; IEA:Ensembl. DR GO; GO:0048496; P:maintenance of animal organ identity; ISS:HGNC-UCL. DR GO; GO:0045494; P:photoreceptor cell maintenance; ISS:HGNC-UCL. DR Gene3D; 1.20.5.190; -; 2. DR InterPro; IPR016024; ARM-type_fold. DR InterPro; IPR000048; IQ_motif_EF-hand-BS. DR InterPro; IPR028765; IQCB1. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR15673; IQ CALMODULIN-BINDING MOTIF CONTAINING PROTEIN 1; 1. DR PANTHER; PTHR15673:SF2; IQ CALMODULIN-BINDING MOTIF-CONTAINING PROTEIN 1; 1. DR Pfam; PF00612; IQ; 2. DR SMART; SM00015; IQ; 2. DR SUPFAM; SSF48371; ARM repeat; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS50096; IQ; 2. DR Genevisible; Q8BP00; MM. PE 1: Evidence at protein level; KW Alternative splicing; Calmodulin-binding; Cilium biogenesis/degradation; KW Coiled coil; Cytoplasm; Cytoskeleton; Reference proteome; Repeat. FT CHAIN 1..598 FT /note="IQ calmodulin-binding motif-containing protein 1" FT /id="PRO_0000084226" FT DOMAIN 294..317 FT /note="IQ 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116" FT DOMAIN 318..338 FT /note="IQ 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116" FT DOMAIN 387..416 FT /note="IQ 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116" FT DOMAIN 417..437 FT /note="IQ 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116" FT REGION 1..157 FT /note="Interaction with BBS1, BBS8 and BBS9" FT /evidence="ECO:0000250|UniProtKB:Q15051" FT REGION 287..598 FT /note="Interaction with CEP290, BBS1, BBS2, BBS4, BBS5, FT BBS7, BBS8 and BBS9" FT /evidence="ECO:0000250|UniProtKB:Q15051" FT REGION 530..598 FT /note="Interaction with BBS1, BBS2, BBS4, BBS7, BBS8 and FT BBS9" FT /evidence="ECO:0000250|UniProtKB:Q15051" FT COILED 336..362 FT /evidence="ECO:0000255" FT VAR_SEQ 523..598 FT /note="KAPSLKEAEGKEPEQFLSRSRPVAAKAKQAHLTTLKHIQAPWWKKLGEEPGD FT EVDVPKDELSIDLGMLFIGGTKPP -> SMLYLHPCFINGIPLARDVASKLFRRKVPQV FT VFIQVLGKSYIIPVFNSIPSVCACYKFKYFSFIKITNFKEVIIF (in isoform FT 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_010246" FT CONFLICT 4 FT /note="A -> P (in Ref. 1; BAC37333)" FT /evidence="ECO:0000305" FT CONFLICT 9 FT /note="R -> G (in Ref. 1; BAC37333)" FT /evidence="ECO:0000305" FT CONFLICT 19 FT /note="K -> R (in Ref. 1; BAC37333)" FT /evidence="ECO:0000305" FT CONFLICT 32 FT /note="L -> V (in Ref. 1; BAC37333)" FT /evidence="ECO:0000305" FT CONFLICT 352 FT /note="L -> W (in Ref. 1; BAC37333)" FT /evidence="ECO:0000305" SQ SEQUENCE 598 AA; 68734 MW; 87FBCB9B68899997 CRC64; MKPAGTDPRI LSLAAEVAKS PEQNVPVILL KLKEIINNTP LGSSELKKVK QDIYCYDLIQ YCLLVLSQDS SRIQGGWSTI SQLTQILSHC CVGLEPGEDG EEFYKELLPS AAENFLILGR RLQTCFINAT KGEEQDKLLH FFQIVTDSLF WLLGGHVQLI QNVLQSDHFL HLLQTDNVQI GASVMTLLQN ILQINSGNLL KIEGKALHSI LDEILFKLLS TPSPVIRSTA TKLLLVLAES HQEILILLRL SACYKGLRSL LNKQETLTEF SRELRQLVDL LTPKIHQEVE EQKLHKAACL IQAYWKGFQT RKRLKKLPSA VIALQRSFRS KRTKMMLELN RQKEEEDLRL KLQLQRQRAM RLSRESRLNM LEIIHPGQVE KYNREMEEKS ALTIQKHWRG YRERKNFRQQ RPSLTEYKAA VTLQRAVLKF LAKCRKKKKL FASWHGLQEL TDARRVELKQ QVDDYVKRHP CSQMSEAASR ELHAQAQERL QHYFMGRAIE ERAQQHREAL MAQISTNIEQ LMKAPSLKEA EGKEPEQFLS RSRPVAAKAK QAHLTTLKHI QAPWWKKLGE EPGDEVDVPK DELSIDLGML FIGGTKPP //