ID IQCB1_HUMAN Reviewed; 598 AA. AC Q15051; Q3KS08; Q3KS09; Q5DKQ7; Q8NI79; Q9BS08; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 27-MAR-2024, entry version 193. DE RecName: Full=IQ calmodulin-binding motif-containing protein 1; DE AltName: Full=Nephrocystin-5; DE AltName: Full=p53 and DNA damage-regulated IQ motif protein; DE Short=PIQ; GN Name=IQCB1; Synonyms=KIAA0036, NPHP5; ORFNames=OK/SW-cl.85; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), CALMODULIN BINDING, RP INDUCTION, AND TISSUE SPECIFICITY. RX PubMed=16322217; DOI=10.1158/0008-5472.can-05-1132; RA Luo X., He Q., Huang Y., Sheikh M.S.; RT "Cloning and characterization of a p53 and DNA damage down-regulated gene RT PIQ that codes for a novel calmodulin-binding IQ motif protein and is up- RT regulated in gastrointestinal cancers."; RL Cancer Res. 65:10725-10733(2005). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, INTERACTION RP WITH CALMODULIN, INVOLVEMENT IN SLSN5, AND VARIANT ASN-393. 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Bone marrow; RX PubMed=7584026; DOI=10.1093/dnares/1.1.27; RA Nomura N., Miyajima N., Sazuka T., Tanaka A., Kawarabayasi Y., Sato S., RA Nagase T., Seki N., Ishikawa K., Tabata S.; RT "Prediction of the coding sequences of unidentified human genes. I. The RT coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of RT randomly sampled cDNA clones from human immature myeloid cell line KG-1."; RL DNA Res. 1:27-35(1994). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RC TISSUE=Colon adenocarcinoma; RA Shichijo S., Itoh K.; RT "Identification of immuno-peptidmics that are recognized by tumor-reactive RT CTL generated from TIL of colon cancer patients."; RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT TYR-434. RC TISSUE=Ovary; 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 [7] RP INTERACTION WITH CEP290. RX PubMed=18723859; DOI=10.1093/hmg/ddn260; RA Schaefer T., Puetz M., Lienkamp S., Ganner A., Bergbreiter A., RA Ramachandran H., Gieloff V., Gerner M., Mattonet C., Czarnecki P.G., RA Sayer J.A., Otto E.A., Hildebrandt F., Kramer-Zucker A., Walz G.; RT "Genetic and physical interaction between the NPHP5 and NPHP6 gene RT products."; RL Hum. Mol. Genet. 17:3655-3662(2008). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-572, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [9] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [10] RP FUNCTION. 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). RN [11] RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CEP290 AND CALMODULIN, RP MUTAGENESIS OF ALA-549, CHARACTERIZATION OF VARIANT ASN-393, AND POSSIBLE RP INVOLVEMENT IN LCA10. RX PubMed=23446637; DOI=10.1093/hmg/ddt100; RA Barbelanne M., Song J., Ahmadzai M., Tsang W.Y.; RT "Pathogenic NPHP5 mutations impair protein interaction with Cep290, a RT prerequisite for ciliogenesis."; RL Hum. Mol. Genet. 22:2482-2494(2013). RN [12] RP FUNCTION, INTERACTION WITH THE BBSOME COMPLEX, INTERACTION WITH CEP290, AND RP MUTAGENESIS OF ALA-549. RX PubMed=25552655; DOI=10.1093/hmg/ddu738; RA Barbelanne M., Hossain D., Chan D.P., Peraenen J., Tsang W.Y.; RT "Nephrocystin proteins NPHP5 and Cep290 regulate BBSome integrity, ciliary RT trafficking and cargo delivery."; RL Hum. Mol. Genet. 24:2185-2200(2015). CC -!- FUNCTION: Involved in ciliogenesis. The function in an early step in CC cilia formation depends on its association with CEP290/NPHP6 CC (PubMed:21565611, PubMed:23446637). Involved in regulation of the CC BBSome complex integrity, specifically for presence of BBS2 and BBS5 in CC the complex, and in ciliary targeting of selected BBSome cargos. May CC play a role in controlling entry of the BBSome complex to cilia CC possibly implicating CEP290/NPHP6 (PubMed:25552655). CC {ECO:0000269|PubMed:23446637, ECO:0000269|PubMed:25552655}. CC -!- SUBUNIT: Interacts with CEP290/NPHP6; IQCB1/NPHP5 and CEP290 are CC proposed to form a functional NPHP5-6 module/NPHP6; localized to the CC centrosome. Interacts with calmodulin, ATXN10 (PubMed:16322217, CC PubMed:15723066, PubMed:18723859, PubMed:21565611, PubMed:23446637, CC PubMed:25552655). Interacts with NPHP1, INVS, NPHP4 and RPGRIP1L; these CC interactions likely require additional interactors (By similarity). CC Associates with the BBSome complex; interacts with BBS1, BBS2, BBS4, CC BBS5, BBS7, BBS8 and BBS9 (PubMed:25552655). CC {ECO:0000250|UniProtKB:Q8BP00, ECO:0000269|PubMed:15723066, CC ECO:0000269|PubMed:18723859, ECO:0000269|PubMed:21565611, CC ECO:0000269|PubMed:23446637, ECO:0000269|PubMed:25552655}. CC -!- INTERACTION: CC Q15051; Q8NFJ9: BBS1; NbExp=4; IntAct=EBI-2805823, EBI-1805484; CC Q15051; Q9BXC9: BBS2; NbExp=8; IntAct=EBI-2805823, EBI-748297; CC Q15051; Q96RK4: BBS4; NbExp=5; IntAct=EBI-2805823, EBI-1805814; CC Q15051; Q8N3I7: BBS5; NbExp=8; IntAct=EBI-2805823, EBI-2892592; CC Q15051; Q8IWZ6: BBS7; NbExp=5; IntAct=EBI-2805823, EBI-1806001; CC Q15051; Q3SYG4: BBS9; NbExp=5; IntAct=EBI-2805823, EBI-2826852; CC Q15051; P62158: CALM3; NbExp=7; IntAct=EBI-2805823, EBI-397435; CC Q15051; O15078: CEP290; NbExp=24; IntAct=EBI-2805823, EBI-1811944; CC Q15051; Q9Y265: RUVBL1; NbExp=2; IntAct=EBI-2805823, EBI-353675; CC Q15051; Q8TAM2: TTC8; NbExp=5; IntAct=EBI-2805823, EBI-2892638; CC Q15051-2; P27482: CALML3; NbExp=3; IntAct=EBI-11944935, EBI-747537; CC Q15051-2; Q9HAQ2: KIF9; NbExp=3; IntAct=EBI-11944935, EBI-8472129; CC Q15051-2; O95751: LDOC1; NbExp=3; IntAct=EBI-11944935, EBI-740738; CC Q15051-2; Q8NEH6: MNS1; NbExp=3; IntAct=EBI-11944935, EBI-743811; CC Q15051-2; P22061-2: PCMT1; NbExp=3; IntAct=EBI-11944935, EBI-12386584; CC Q15051-2; O76083-2: PDE9A; NbExp=5; IntAct=EBI-11944935, EBI-11524542; CC Q15051-2; Q86VW0: SESTD1; NbExp=3; IntAct=EBI-11944935, EBI-6117072; CC Q15051-2; Q96GM5: SMARCD1; NbExp=3; IntAct=EBI-11944935, EBI-358489; CC Q15051-2; Q9NZD8: SPG21; NbExp=3; IntAct=EBI-11944935, EBI-742688; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing CC center, centrosome {ECO:0000269|PubMed:21565611}. Cytoplasm, CC cytoskeleton, microtubule organizing center, centrosome, centriole CC {ECO:0000269|PubMed:23446637}. Note=Localization to the centrosome CC depends on the interaction with CEP290/NPHP6. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; Synonyms=PIQ-L; CC IsoId=Q15051-1; Sequence=Displayed; CC Name=2; Synonyms=PIQ-S; CC IsoId=Q15051-2; Sequence=VSP_010245; CC Name=3; CC IsoId=Q15051-3; Sequence=VSP_013943, VSP_013944; CC -!- TISSUE SPECIFICITY: Ubiquitously expressed in fetal and adult tissues. CC Localized to the outer segments and connecting cilia of photoreceptor CC cells. Up-regulated in a number of primary colorectal and gastric CC tumors. {ECO:0000269|PubMed:15723066, ECO:0000269|PubMed:16322217}. CC -!- INDUCTION: Down-regulated by DNA damage in a p53-dependent manner. CC {ECO:0000269|PubMed:16322217}. CC -!- DOMAIN: The IQ domains mediate the interaction with calmodulin. CC {ECO:0000269|PubMed:23446637}. CC -!- DISEASE: Senior-Loken syndrome 5 (SLSN5) [MIM:609254]: A renal-retinal CC disorder characterized by progressive wasting of the filtering unit of CC the kidney (nephronophthisis), with or without medullary cystic renal CC disease, and progressive eye disease. Typically this disorder becomes CC apparent during the first year of life. {ECO:0000269|PubMed:15723066}. CC Note=The disease is caused by variants affecting the gene represented CC in this entry. CC -!- DISEASE: Leber congenital amaurosis 10 (LCA10) [MIM:611755]: A severe CC dystrophy of the retina, typically becoming evident in the first years CC of life. Visual function is usually poor and often accompanied by CC nystagmus, sluggish or near-absent pupillary responses, photophobia, CC high hyperopia and keratoconus. {ECO:0000269|PubMed:23446637}. Note=The CC gene represented in this entry may be involved in disease pathogenesis. CC -!- MISCELLANEOUS: [Isoform 2]: Low abundance isoform. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA04968.2; Type=Erroneous initiation; Evidence={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; AY964667; AAY46029.1; -; mRNA. DR EMBL; AY964668; AAY46030.1; -; mRNA. DR EMBL; AY714228; AAW47233.1; -; mRNA. DR EMBL; D25278; BAA04968.2; ALT_INIT; mRNA. DR EMBL; AB062481; BAB93506.1; -; mRNA. DR EMBL; CH471052; EAW79500.1; -; Genomic_DNA. DR EMBL; BC005806; AAH05806.1; -; mRNA. DR CCDS; CCDS33836.1; -. [Q15051-2] DR CCDS; CCDS33837.1; -. [Q15051-1] DR RefSeq; NP_001018864.2; NM_001023570.3. [Q15051-1] DR RefSeq; NP_001018865.2; NM_001023571.3. [Q15051-2] DR RefSeq; NP_001306036.1; NM_001319107.1. [Q15051-1] DR AlphaFoldDB; Q15051; -. DR SMR; Q15051; -. DR BioGRID; 115015; 284. DR ComplexPortal; CPX-2536; CEP290-NPHP5 transition zone complex. DR CORUM; Q15051; -. DR IntAct; Q15051; 228. DR MINT; Q15051; -. DR STRING; 9606.ENSP00000311505; -. DR iPTMnet; Q15051; -. DR PhosphoSitePlus; Q15051; -. DR BioMuta; IQCB1; -. DR DMDM; 3123054; -. DR EPD; Q15051; -. DR jPOST; Q15051; -. DR MassIVE; Q15051; -. DR MaxQB; Q15051; -. DR PaxDb; 9606-ENSP00000311505; -. DR PeptideAtlas; Q15051; -. DR ProteomicsDB; 60403; -. [Q15051-1] DR ProteomicsDB; 60404; -. [Q15051-2] DR ProteomicsDB; 60405; -. [Q15051-3] DR Pumba; Q15051; -. DR Antibodypedia; 32846; 226 antibodies from 28 providers. DR DNASU; 9657; -. DR Ensembl; ENST00000310864.11; ENSP00000311505.6; ENSG00000173226.17. [Q15051-1] DR Ensembl; ENST00000349820.10; ENSP00000323756.7; ENSG00000173226.17. [Q15051-2] DR Ensembl; ENST00000393650.7; ENSP00000377261.3; ENSG00000173226.17. [Q15051-3] DR GeneID; 9657; -. DR KEGG; hsa:9657; -. DR MANE-Select; ENST00000310864.11; ENSP00000311505.6; NM_001023570.4; NP_001018864.2. DR UCSC; uc003eek.3; human. [Q15051-1] DR AGR; HGNC:28949; -. DR CTD; 9657; -. DR DisGeNET; 9657; -. DR GeneCards; IQCB1; -. DR GeneReviews; IQCB1; -. DR HGNC; HGNC:28949; IQCB1. DR HPA; ENSG00000173226; Low tissue specificity. DR MalaCards; IQCB1; -. DR MIM; 609237; gene. DR MIM; 609254; phenotype. DR MIM; 611755; phenotype. DR neXtProt; NX_Q15051; -. DR OpenTargets; ENSG00000173226; -. DR Orphanet; 65; Leber congenital amaurosis. DR Orphanet; 3156; Senior-Loken syndrome. DR PharmGKB; PA134869761; -. DR VEuPathDB; HostDB:ENSG00000173226; -. DR eggNOG; KOG0160; Eukaryota. DR GeneTree; ENSGT00390000002188; -. DR HOGENOM; CLU_035387_0_0_1; -. DR InParanoid; Q15051; -. DR OMA; IHGGWAT; -. DR OrthoDB; 3670690at2759; -. DR PhylomeDB; Q15051; -. DR TreeFam; TF351884; -. DR PathwayCommons; Q15051; -. DR Reactome; R-HSA-5620912; Anchoring of the basal body to the plasma membrane. DR SignaLink; Q15051; -. DR BioGRID-ORCS; 9657; 95 hits in 1148 CRISPR screens. DR ChiTaRS; IQCB1; human. DR GeneWiki; IQCB1; -. DR GenomeRNAi; 9657; -. DR Pharos; Q15051; Tbio. DR PRO; PR:Q15051; -. DR Proteomes; UP000005640; Chromosome 3. DR RNAct; Q15051; Protein. DR Bgee; ENSG00000173226; Expressed in oocyte and 189 other cell types or tissues. DR ExpressionAtlas; Q15051; baseline and differential. DR GO; GO:0005814; C:centriole; IEA:UniProtKB-SubCell. DR GO; GO:0005813; C:centrosome; IDA:UniProtKB. DR GO; GO:0005929; C:cilium; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0045171; C:intercellular bridge; IDA:HPA. DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:HPA. DR GO; GO:0072686; C:mitotic spindle; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0032391; C:photoreceptor connecting cilium; IDA:HGNC-UCL. DR GO; GO:0001750; C:photoreceptor outer segment; IEA:Ensembl. DR GO; GO:0062063; F:BBSome binding; IDA:UniProt. DR GO; GO:0005516; F:calmodulin binding; IDA:HGNC-UCL. DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB. DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IDA:UniProt. DR GO; GO:0060271; P:cilium assembly; IDA:UniProt. DR GO; GO:0061824; P:cytosolic ciliogenesis; IDA:UniProt. DR GO; GO:0048496; P:maintenance of animal organ identity; IMP:HGNC-UCL. DR GO; GO:0045494; P:photoreceptor cell maintenance; IMP: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; Q15051; HS. PE 1: Evidence at protein level; KW Alternative splicing; Calmodulin-binding; Ciliopathy; KW Cilium biogenesis/degradation; Coiled coil; Cytoplasm; Cytoskeleton; KW Leber congenital amaurosis; Nephronophthisis; Phosphoprotein; KW Reference proteome; Repeat; Senior-Loken syndrome. FT CHAIN 1..598 FT /note="IQ calmodulin-binding motif-containing protein 1" FT /id="PRO_0000084225" 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:0000269|PubMed:25552655" FT REGION 287..598 FT /note="Interaction with CEP290, BBS1, BBS2, BBS4, BBS5, FT BBS7, BBS8 and BBS9" FT /evidence="ECO:0000269|PubMed:25552655" FT REGION 530..598 FT /note="Interaction with BBS1, BBS2, BBS4, BBS7, BBS8 and FT BBS9" FT /evidence="ECO:0000269|PubMed:25552655" FT COILED 336..373 FT /evidence="ECO:0000255" FT MOD_RES 572 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT VAR_SEQ 196..328 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:16322217" FT /id="VSP_010245" FT VAR_SEQ 293..303 FT /note="KLHQAACLIQA -> IQTIKDVAGDK (in isoform 3)" FT /evidence="ECO:0000303|Ref.4" FT /id="VSP_013943" FT VAR_SEQ 304..598 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|Ref.4" FT /id="VSP_013944" FT VARIANT 142 FT /note="F -> L (in dbSNP:rs11926958)" FT /id="VAR_051074" FT VARIANT 393 FT /note="I -> N (impairs interaction with calmodulin; FT dbSNP:rs1141528)" FT /evidence="ECO:0000269|PubMed:15723066" FT /id="VAR_051075" FT VARIANT 434 FT /note="C -> Y (in dbSNP:rs17849995)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_061668" FT VARIANT 435 FT /note="R -> C (in dbSNP:rs11920543)" FT /id="VAR_051076" FT MUTAGEN 549 FT /note="A->K: Disrupts interaction with CEP290, no effect on FT interaction with BBS1, BBS2, BBS4, BBS8 and BBS9, abolishes FT ciliogenesis." FT /evidence="ECO:0000269|PubMed:23446637, FT ECO:0000269|PubMed:25552655" FT CONFLICT Q15051-2:352 FT /note="Q -> P (in Ref. 1; AAY46029)" FT /evidence="ECO:0000305" SQ SEQUENCE 598 AA; 68929 MW; 5589FDE6B0D15D78 CRC64; MKPTGTDPRI LSIAAEVAKS PEQNVPVILL KLKEIINITP LGSSELKKIK QDIYCYDLIQ YCLLVLSQDY SRIQGGWTTI SQLTQILSHC CVGLEPGEDA EEFYNELLPS AAENFLVLGR QLQTCFINAA KAEEKDELLH FFQIVTDSLF WLLGGHVELI QNVLQSDHFL HLLQADNVQI GSAVMMMLQN ILQINSGDLL RIGRKALYSI LDEVIFKLFS TPSPVIRSTA TKLLLLMAES HQEILILLRQ STCYKGLRRL LSKQETGTEF SQELRQLVGL LSPMVYQEVE EQKLHQAACL IQAYWKGFQT RKRLKKLPSA VIALQRSFRS KRSKMLLEIN RQKEEEDLKL QLQLQRQRAM RLSRELQLSM LEIVHPGQVE KHYREMEEKS ALIIQKHWRG YRERKNFHQQ RQSLIEYKAA VTLQRAALKF LAKCRKKKKL FAPWRGLQEL TDARRVELKK RVDDYVRRHL GSPMSDVVSR ELHAQAQERL QHYFMGRALE ERAQQHREAL IAQISTNVEQ LMKAPSLKEA EGKEPELFLS RSRPVAAKAK QAHLTTLKHI QAPWWKKLGE ESGDEIDVPK DELSIELENL FIGGTKPP //