IQCB1_HUMAN
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 03-AUG-2022, entry version 184.
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};
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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; 275.
DR CORUM; Q15051; -.
DR IntAct; Q15051; 227.
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; Q15051; -.
DR PeptideAtlas; Q15051; -.
DR PRIDE; Q15051; -.
DR ProteomicsDB; 60403; -. [Q15051-1]
DR ProteomicsDB; 60404; -. [Q15051-2]
DR ProteomicsDB; 60405; -. [Q15051-3]
DR Antibodypedia; 32846; 197 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 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; SLGCEES; -.
DR OrthoDB; 852806at2759; -.
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 1073 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 187 other tissues.
DR ExpressionAtlas; Q15051; baseline and differential.
DR Genevisible; Q15051; HS.
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:0005516; F:calmodulin binding; IDA:HGNC-UCL.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0060271; P:cilium assembly; ISS:UniProtKB.
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 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; 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
