IQCB1_MOUSE
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 03-AUG-2022, entry version 142.
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}.
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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 EPD; Q8BP00; -.
DR MaxQB; Q8BP00; -.
DR PaxDb; Q8BP00; -.
DR PeptideAtlas; Q8BP00; -.
DR PRIDE; Q8BP00; -.
DR ProteomicsDB; 301664; -. [Q8BP00-1]
DR ProteomicsDB; 301665; -. [Q8BP00-2]
DR Antibodypedia; 32846; 197 antibodies from 28 providers.
DR Ensembl; ENSMUST00000023535; ENSMUSP00000023535; ENSMUSG00000022837. [Q8BP00-1]
DR Ensembl; ENSMUST00000114819; ENSMUSP00000110467; ENSMUSG00000022837. [Q8BP00-2]
DR GeneID; 320299; -.
DR KEGG; mmu:320299; -.
DR UCSC; uc007zda.1; mouse. [Q8BP00-2]
DR UCSC; uc007zdb.2; mouse. [Q8BP00-1]
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; SLGCEES; -.
DR OrthoDB; 852806at2759; -.
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 72 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 215 other tissues.
DR Genevisible; Q8BP00; MM.
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:0005516; F:calmodulin binding; ISS:HGNC-UCL.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0060271; P:cilium assembly; IMP:UniProtKB.
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 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; PTHR15673; 1.
DR Pfam; PF00612; IQ; 2.
DR SMART; SM00015; IQ; 2.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50096; IQ; 2.
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
