CE290_MOUSE
ID CE290_MOUSE Reviewed; 2472 AA.
AC Q6A078; Q8BIB8;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Centrosomal protein of 290 kDa;
DE Short=Cep290;
DE AltName: Full=Bardet-Biedl syndrome 14 protein homolog;
DE AltName: Full=Nephrocystin-6;
GN Name=Cep290 {ECO:0000312|MGI:MGI:2384917};
GN Synonyms=Kiaa0373 {ECO:0000312|EMBL:BAD32218.1},
GN Nphp6 {ECO:0000250|UniProtKB:O15078};
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] {ECO:0000305, ECO:0000312|EMBL:BAC26700.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC26700.1};
RC TISSUE=Testis {ECO:0000312|EMBL:BAC26700.1};
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3] {ECO:0000305, ECO:0000312|EMBL:BAD32218.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1103-2472 (ISOFORM 1).
RC TISSUE=Fetal brain {ECO:0000312|EMBL:BAD32218.1};
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [4] {ECO:0000305}
RP INVOLVEMENT IN EARLY-ONSET RETINAL DEGENERATION, FUNCTION, INTERACTION WITH
RP RPGR, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=16632484; DOI=10.1093/hmg/ddl107;
RA Chang B., Khanna H., Hawes N., Jimeno D., He S., Lillo C., Parapuram S.K.,
RA Cheng H., Scott A., Hurd R.E., Sayer J.A., Otto E.A., Attanasio M.,
RA O'Toole J.F., Jin G., Shou C., Hildebrandt F., Williams D.S.,
RA Heckenlively J.R., Swaroop A.;
RT "In-frame deletion in a novel centrosomal/ciliary protein CEP290/NPHP6
RT perturbs its interaction with RPGR and results in early-onset retinal
RT degeneration in the rd16 mouse.";
RL Hum. Mol. Genet. 15:1847-1857(2006).
RN [5] {ECO:0000305}
RP MUTAGENESIS OF TRP-7, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND TISSUE
RP SPECIFICITY.
RX PubMed=16682970; DOI=10.1038/ng1805;
RG International Joubert syndrome related disorders (JSRD) study group;
RA Valente E.M., Silhavy J.L., Brancati F., Barrano G., Krishnaswami S.R.,
RA Castori M., Lancaster M.A., Boltshauser E., Boccone L., Al-Gazali L.,
RA Fazzi E., Signorini S., Louie C.M., Bellacchio E., Bertini E.,
RA Dallapiccola B., Gleeson J.G.;
RT "Mutations in CEP290, which encodes a centrosomal protein, cause
RT pleiotropic forms of Joubert syndrome.";
RL Nat. Genet. 38:623-625(2006).
RN [6] {ECO:0000305}
RP SUBCELLULAR LOCATION.
RX PubMed=16682973; DOI=10.1038/ng1786;
RA Sayer J.A., Otto E.A., O'toole J.F., Nurnberg G., Kennedy M.A., Becker C.,
RA Hennies H.C., Helou J., Attanasio M., Fausett B.V., Utsch B., Khanna H.,
RA Liu Y., Drummond I., Kawakami I., Kusakabe T., Tsuda M., Ma L., Lee H.,
RA Larson R.G., Allen S.J., Wilkinson C.J., Nigg E.A., Shou C., Lillo C.,
RA Williams D.S., Hoppe B., Kemper M.J., Neuhaus T., Parisi M.A., Glass I.A.,
RA Petry M., Kispert A., Gloy J., Ganner A., Walz G., Zhu X., Goldman D.,
RA Nurnberg P., Swaroop A., Leroux M.R., Hildebrandt F.;
RT "The centrosomal protein nephrocystin-6 is mutated in Joubert syndrome and
RT activates transcription factor ATF4.";
RL Nat. Genet. 38:674-681(2006).
RN [7]
RP INTERACTION WITH PCM1.
RX PubMed=17705300; DOI=10.1002/humu.20614;
RA Frank V., den Hollander A.I., Bruechle N.O., Zonneveld M.N., Nuernberg G.,
RA Becker C., Du Bois G., Kendziorra H., Roosing S., Senderek J.,
RA Nuernberg P., Cremers F.P., Zerres K., Bergmann C.;
RT "Mutations of the CEP290 gene encoding a centrosomal protein cause Meckel-
RT Gruber syndrome.";
RL Hum. Mutat. 29:45-52(2008).
RN [8]
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 [9]
RP FUNCTION, AND INTERACTION WITH IQCB1.
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 [10]
RP FUNCTION, SUBCELLULAR LOCATION, AND IDENTIFICATION IN THE TECTONIC-LIKE
RP COMPLEX.
RX PubMed=21725307; DOI=10.1038/ng.891;
RA Garcia-Gonzalo F.R., Corbit K.C., Sirerol-Piquer M.S., Ramaswami G.,
RA Otto E.A., Noriega T.R., Seol A.D., Robinson J.F., Bennett C.L.,
RA Josifova D.J., Garcia-Verdugo J.M., Katsanis N., Hildebrandt F.,
RA Reiter J.F.;
RT "A transition zone complex regulates mammalian ciliogenesis and ciliary
RT membrane composition.";
RL Nat. Genet. 43:776-784(2011).
RN [11]
RP DISRUPTION PHENOTYPE.
RX PubMed=21623382; DOI=10.1038/nm.2380;
RA Lancaster M.A., Gopal D.J., Kim J., Saleem S.N., Silhavy J.L., Louie C.M.,
RA Thacker B.E., Williams Y., Zaki M.S., Gleeson J.G.;
RT "Defective Wnt-dependent cerebellar midline fusion in a mouse model of
RT Joubert syndrome.";
RL Nat. Med. 17:726-731(2011).
RN [12]
RP SUBCELLULAR LOCATION.
RX PubMed=23807208; DOI=10.1007/s00018-013-1401-6;
RA Kypri E., Christodoulou A., Maimaris G., Lethan M., Markaki M.,
RA Lysandrou C., Lederer C.W., Tavernarakis N., Geimer S., Pedersen L.B.,
RA Santama N.;
RT "The nucleotide-binding proteins Nubp1 and Nubp2 are negative regulators of
RT ciliogenesis.";
RL Cell. Mol. Life Sci. 71:517-538(2014).
RN [13]
RP SUBCELLULAR LOCATION.
RX PubMed=23943788; DOI=10.1093/hmg/ddt394;
RA Zhang Y., Seo S., Bhattarai S., Bugge K., Searby C.C., Zhang Q.,
RA Drack A.V., Stone E.M., Sheffield V.C.;
RT "BBS mutations modify phenotypic expression of CEP290-related
RT ciliopathies.";
RL Hum. Mol. Genet. 23:40-51(2014).
CC -!- FUNCTION: Involved in early and late steps in cilia formation
CC (PubMed:21565611). Its association with CCP110 is required for
CC inhibition of primary cilia formation by CCP110 (By similarity). May
CC play a role in early ciliogenesis in the disappearance of centriolar
CC satellites and in the transition of primary ciliar vesicles (PCVs) to
CC capped ciliary vesicles (CCVs). Required for the centrosomal
CC recruitment of RAB8A and for the targeting of centriole satellite
CC proteins to centrosomes such as of PCM1 (By similarity). Required for
CC the correct localization of ciliary and phototransduction proteins in
CC retinal photoreceptor cells; may play a role in ciliary transport
CC processes (PubMed:16632484). Required for efficient recruitment of
CC RAB8A to primary cilium (By similarity). In the ciliary transition zone
CC is part of the tectonic-like complex (also named B9 complex) which is
CC required for tissue-specific ciliogenesis and may regulate ciliary
CC membrane composition (PubMed:21725307). Involved in regulation of the
CC BBSome complex integrity, specifically for presence of BBS2, BBS5 and
CC BBS8/TTC8 in the complex, and in ciliary targeting of selected BBSome
CC cargos. May play a role in controlling entry of the BBSome complex to
CC cilia possibly implicating IQCB1/NPHP5 (By similarity). Activates ATF4-
CC mediated transcription (By similarity). {ECO:0000250|UniProtKB:O15078,
CC ECO:0000269|PubMed:16632484, ECO:0000269|PubMed:21565611,
CC ECO:0000269|PubMed:21725307}.
CC -!- SUBUNIT: Part of the tectonic-like complex (also named B9 complex)
CC (PubMed:21725307). Interacts with ATF4 via its N-terminal region (By
CC similarity). Associates with the BBSome complex, interacting (via N-
CC terminus) with BBS4 (By similarity). Interacts with IQCB1/NPHP5; IQCB1
CC and CEP290/NPHP6 are proposed to form a functional NPHP5-6 module
CC localized to the centrosome. Interacts with NPHP4; the interaction
CC likely requires additional interactors (PubMed:21565611). Interacts
CC with ZNF423, FAM161A, CEP162, CEP162, CEP131, TALPID3, CCDC13, CC2D2A,
CC RPGRIP1 (By similarity). Can self-associate (homo- or heteromeric) (By
CC similarity). Interacts with CCP110; required for suppressing cilia
CC formation (By similarity). Interacts with RPGR (PubMed:16632484).
CC Associates (via C-terminus) with microtubules; association to
CC microtubule is reduced in response to cellular stress, such as
CC ultraviolet light (UV) radiation or heat shock, in a process that
CC requires p38 MAP kinase signaling (By similarity). Interacts with
CC FAM161A (By similarity). Interacts with PCM1 (PubMed:17705300).
CC Interacts with CCDC66 (By similarity). Interacts with ARMC9 and CSPP1
CC (By similarity). {ECO:0000250|UniProtKB:O15078,
CC ECO:0000250|UniProtKB:Q9TU23, ECO:0000269|PubMed:16632484,
CC ECO:0000269|PubMed:17705300, ECO:0000269|PubMed:21565611,
CC ECO:0000269|PubMed:21725307}.
CC -!- INTERACTION:
CC Q6A078; Q7TSH4: Ccp110; NbExp=3; IntAct=EBI-1811999, EBI-646843;
CC Q6A078; O08788: Dctn1; NbExp=2; IntAct=EBI-1811999, EBI-776180;
CC Q6A078; Q8BP00: Iqcb1; NbExp=6; IntAct=EBI-1811999, EBI-4282243;
CC Q6A078; P28741: Kif3a; NbExp=3; IntAct=EBI-1811999, EBI-6169413;
CC Q6A078; Q9R0L6: Pcm1; NbExp=4; IntAct=EBI-1811999, EBI-4284371;
CC Q6A078; P48725: Pcnt; NbExp=2; IntAct=EBI-1811999, EBI-2290976;
CC Q6A078; Q9CU62: Smc1a; NbExp=2; IntAct=EBI-1811999, EBI-2550016;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000269|PubMed:16632484,
CC ECO:0000269|PubMed:16682970, ECO:0000269|PubMed:16682973}. Cytoplasm
CC {ECO:0000269|PubMed:16682973}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome, centriolar satellite
CC {ECO:0000269|PubMed:21725307}. Nucleus {ECO:0000269|PubMed:16632484,
CC ECO:0000269|PubMed:16682973}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome, centriole {ECO:0000269|PubMed:16632484,
CC ECO:0000269|PubMed:16682970, ECO:0000269|PubMed:23807208}. Cell
CC projection, cilium {ECO:0000269|PubMed:16632484,
CC ECO:0000269|PubMed:16682970, ECO:0000269|PubMed:23943788}. Cytoplasm,
CC cytoskeleton, cilium basal body {ECO:0000269|PubMed:23807208}.
CC Cytoplasmic vesicle {ECO:0000250|UniProtKB:O15078}. Note=Displaced from
CC centriolar satellites in response to cellular stress, such as
CC ultraviolet light (UV) radiation or heat shock (By similarity). Found
CC in the connecting cilium of photoreceptor cells (PubMed:16632484,
CC PubMed:23943788), base of cilium in kidney intramedullary collecting
CC duct cells (PubMed:16682970). Localizes at the transition zone, a
CC region between the basal body and the ciliary axoneme
CC (PubMed:21725307). Localization at the ciliary transition zone as well
CC as at centriolar satellites is BBsome-dependent (By similarity).
CC {ECO:0000250|UniProtKB:O15078, ECO:0000269|PubMed:16632484,
CC ECO:0000269|PubMed:16682970, ECO:0000269|PubMed:21725307,
CC ECO:0000269|PubMed:23943788}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:15368895};
CC IsoId=Q6A078-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:16141072};
CC IsoId=Q6A078-2; Sequence=VSP_052188, VSP_052189;
CC -!- TISSUE SPECIFICITY: Expressed in multiple organs during early postnatal
CC development, with highest levels in hindbrain.
CC {ECO:0000269|PubMed:16682970}.
CC -!- DEVELOPMENTAL STAGE: Similar levels from 7 dpc to 17 dpc in whole
CC embryo and brain. In the cerebellum, expressed most strongly in
CC dividing cells of the external granule layer.
CC {ECO:0000269|PubMed:16682970}.
CC -!- PTM: Ubiquitinated. May undergo monoubiquitination; monoubiquitination
CC is inhibited in response to cellular stress, such as ultraviolet light
CC (UV) radiation or heat shock, but does not cause it displacement from
CC centriolar satellites (By similarity). {ECO:0000250}.
CC -!- DISEASE: Note=Defects in Cep290 are a cause of early-onset retinal
CC degeneration with autosomal recessive inheritance. The rd16 mutant
CC carries a deletion of residues 1599-1897 in the Cep290 protein.
CC Homozygous rd16 mice are characterized by the appearance of white
CC retinal vessels at 1 month of age and large pigment patches at 2
CC months. Retinal degeneration is apparent as early as postnatal day 19
CC and progresses with age. The rd16 retina exhibits altered distribution
CC of Rpgr and phototransduction proteins within the photoreceptor cells.
CC -!- DISRUPTION PHENOTYPE: Knockout mice appear healthy overall with some
CC runting and a retinal degeneration phenotype. During embryonic
CC development, at 16.5 dpc, they show defective midline fusion. Adult
CC animals show a mild foliation defect in the cerebellum.
CC {ECO:0000269|PubMed:21623382}.
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; AK029960; BAC26700.1; -; mRNA.
DR EMBL; AC153501; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK172940; BAD32218.1; -; mRNA.
DR RefSeq; NP_666121.2; NM_146009.2.
DR RefSeq; XP_006513591.1; XM_006513528.2. [Q6A078-1]
DR AlphaFoldDB; Q6A078; -.
DR SMR; Q6A078; -.
DR BioGRID; 229729; 48.
DR CORUM; Q6A078; -.
DR DIP; DIP-46317N; -.
DR IntAct; Q6A078; 43.
DR STRING; 10090.ENSMUSP00000130899; -.
DR CarbonylDB; Q6A078; -.
DR iPTMnet; Q6A078; -.
DR PhosphoSitePlus; Q6A078; -.
DR jPOST; Q6A078; -.
DR MaxQB; Q6A078; -.
DR PaxDb; Q6A078; -.
DR PRIDE; Q6A078; -.
DR ProteomicsDB; 281448; -. [Q6A078-1]
DR ProteomicsDB; 281449; -. [Q6A078-2]
DR Antibodypedia; 29900; 262 antibodies from 35 providers.
DR Ensembl; ENSMUST00000219765; ENSMUSP00000151712; ENSMUSG00000019971. [Q6A078-1]
DR GeneID; 216274; -.
DR KEGG; mmu:216274; -.
DR UCSC; uc007gxw.2; mouse. [Q6A078-2]
DR CTD; 80184; -.
DR MGI; MGI:2384917; Cep290.
DR VEuPathDB; HostDB:ENSMUSG00000019971; -.
DR eggNOG; ENOG502QPTZ; Eukaryota.
DR GeneTree; ENSGT00730000111039; -.
DR InParanoid; Q6A078; -.
DR OrthoDB; 27774at2759; -.
DR PhylomeDB; Q6A078; -.
DR Reactome; R-MMU-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-MMU-380259; Loss of Nlp from mitotic centrosomes.
DR Reactome; R-MMU-380270; Recruitment of mitotic centrosome proteins and complexes.
DR Reactome; R-MMU-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR Reactome; R-MMU-380320; Recruitment of NuMA to mitotic centrosomes.
DR Reactome; R-MMU-5620912; Anchoring of the basal body to the plasma membrane.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-8854518; AURKA Activation by TPX2.
DR BioGRID-ORCS; 216274; 6 hits in 73 CRISPR screens.
DR ChiTaRS; Cep290; mouse.
DR PRO; PR:Q6A078; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q6A078; protein.
DR Bgee; ENSMUSG00000019971; Expressed in spermatid and 230 other tissues.
DR ExpressionAtlas; Q6A078; baseline and differential.
DR GO; GO:0034451; C:centriolar satellite; IDA:MGI.
DR GO; GO:0005814; C:centriole; IDA:MGI.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0036064; C:ciliary basal body; ISO:MGI.
DR GO; GO:0035869; C:ciliary transition zone; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; ISS:HGNC-UCL.
DR GO; GO:0036038; C:MKS complex; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:HGNC-UCL.
DR GO; GO:0032391; C:photoreceptor connecting cilium; IDA:UniProtKB.
DR GO; GO:0120206; C:photoreceptor distal connecting cilium; IDA:MGI.
DR GO; GO:0001750; C:photoreceptor outer segment; IDA:MGI.
DR GO; GO:0120205; C:photoreceptor proximal connecting cilium; IDA:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0120200; C:rod photoreceptor outer segment; IGI:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0043010; P:camera-type eye development; IBA:GO_Central.
DR GO; GO:0097711; P:ciliary basal body-plasma membrane docking; IMP:MGI.
DR GO; GO:1905349; P:ciliary transition zone assembly; IMP:MGI.
DR GO; GO:0060271; P:cilium assembly; IMP:UniProtKB.
DR GO; GO:0007368; P:determination of left/right symmetry; IMP:MGI.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IMP:MGI.
DR GO; GO:0042462; P:eye photoreceptor cell development; ISS:HGNC-UCL.
DR GO; GO:0007507; P:heart development; IMP:MGI.
DR GO; GO:0030902; P:hindbrain development; ISS:HGNC-UCL.
DR GO; GO:0001822; P:kidney development; IMP:MGI.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IGI:MGI.
DR GO; GO:1905515; P:non-motile cilium assembly; IMP:MGI.
DR GO; GO:0030916; P:otic vesicle formation; ISS:HGNC-UCL.
DR GO; GO:0045494; P:photoreceptor cell maintenance; IMP:MGI.
DR GO; GO:0090316; P:positive regulation of intracellular protein transport; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:HGNC-UCL.
DR GO; GO:0048793; P:pronephros development; ISS:HGNC-UCL.
DR GO; GO:0015031; P:protein transport; IMP:UniProtKB.
DR GO; GO:0070201; P:regulation of establishment of protein localization; ISO:MGI.
DR GO; GO:0060041; P:retina development in camera-type eye; IMP:MGI.
DR InterPro; IPR032321; Cep209_CC5.
DR InterPro; IPR026201; Cep290.
DR PANTHER; PTHR18879; PTHR18879; 3.
DR Pfam; PF16574; CEP209_CC5; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Cell projection; Cilium;
KW Cilium biogenesis/degradation; Coiled coil; Cytoplasm; Cytoplasmic vesicle;
KW Cytoskeleton; Nucleus; Protein transport; Reference proteome;
KW Transcription; Transcription regulation; Transport; Ubl conjugation.
FT CHAIN 1..2472
FT /note="Centrosomal protein of 290 kDa"
FT /id="PRO_0000258013"
FT REGION 1..689
FT /note="Self-association (with itself or C-terminus)"
FT /evidence="ECO:0000250|UniProtKB:O15078"
FT REGION 128..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 690..890
FT /note="Interaction with IQCB1"
FT /evidence="ECO:0000250|UniProtKB:O15078"
FT REGION 1691..1713
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1960..2472
FT /note="Self-association (with itself or N-terminus)"
FT /evidence="ECO:0000250|UniProtKB:O15078"
FT REGION 2451..2472
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 59..747
FT /evidence="ECO:0000255"
FT COILED 1129..1392
FT /evidence="ECO:0000255"
FT COILED 1459..1492
FT /evidence="ECO:0000255"
FT COMPBIAS 1693..1713
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..1664
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_052188"
FT VAR_SEQ 1665
FT /note="R -> M (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_052189"
FT MUTAGEN 7
FT /note="W->C: Centrosomal localization retained."
FT /evidence="ECO:0000269|PubMed:16682970"
FT CONFLICT 1425
FT /note="A -> P (in Ref. 3; BAD32218)"
FT /evidence="ECO:0000305"
FT CONFLICT 1470
FT /note="S -> A (in Ref. 3; BAD32218)"
FT /evidence="ECO:0000305"
FT CONFLICT 1533
FT /note="H -> Q (in Ref. 3; BAD32218)"
FT /evidence="ECO:0000305"
FT CONFLICT 1544
FT /note="N -> T (in Ref. 3; BAD32218)"
FT /evidence="ECO:0000305"
FT CONFLICT 1559
FT /note="K -> R (in Ref. 3; BAD32218)"
FT /evidence="ECO:0000305"
FT CONFLICT 1686
FT /note="H -> N (in Ref. 3; BAD32218)"
FT /evidence="ECO:0000305"
FT CONFLICT 2037
FT /note="Q -> E (in Ref. 3; BAD32218)"
FT /evidence="ECO:0000305"
FT CONFLICT 2134
FT /note="V -> L (in Ref. 3; BAD32218)"
FT /evidence="ECO:0000305"
FT CONFLICT 2158
FT /note="A -> G (in Ref. 3; BAD32218)"
FT /evidence="ECO:0000305"
FT CONFLICT 2345
FT /note="M -> L (in Ref. 3; BAD32218)"
FT /evidence="ECO:0000305"
FT CONFLICT 2389
FT /note="L -> S (in Ref. 3; BAD32218)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2472 AA; 289077 MW; D6ABC2C8A86340A0 CRC64;
MPPNIKWKEL IKVDPDDLPR QEELADKLLI SLSKVEVNEL KNEDQENMIH LFRITQSLMK
MKAQEVELAL EEVEKAGEEQ AKFENQLKTK VMKLENELEM AQQSAGGRDT RFLRDEIRQL
EKQLEQKDRE LEDMEKELDK EKKVNEQLAL RNEEAENENS KLRRENEQLR QDIIDYQKQI
DSQKESLLSR RGEDSDYRSQ LSKKNYELVQ YLDEIQTLTE ANEKIEVQNQ EMRKNLEESV
QEMEKMTDEY NRMKALVHQS DAVMDQIKKE NEHYRLQVRE LTDLLKAKDE EDDPVMMAVN
AKVEEWKLIL SSKDDEIIEY QQMLQSLRGK LKNAQLDADK SNIMALKQGI QERDSQIKML
TEQVEQYTKE MEKNTFIIED LKNELQKDKG TSNFYQQTHY MKIHSKVQIL EEKTKEAERI
AELAEADARE KDKELVEALK RLKDYESGVY GLEDAVIEIK NCKAQIKIRD GEMEVLTKEI
NKLEMKINDI LDENEALRER AGLEPKTMID LTEFRNSKRL KQQQYRAENQ VLLKEIESLE
EERLDLKRKI RQMAQERGKR NAASGLTIDD LNLSETFSHE NKIEGRKLNF MSLNNMNETQ
SKNEFLSREL AEKEKDLERS RTVIAKFQSK LKELVEENKQ LEEGMKEILQ AIKDMPKDSD
VKGGETSLII PSLERLVNAM ESKNAEGIFD ASLHLKAQVD QLTGRNEELR QELRQSRKEA
VNYSQQLVKA NLKIDHLEKE TDLLRQSAGS NVVYKGIDLP DGIAPSSAYI INSQNEYLIH
LLQELDNKEK KLKHLEDSLE DYNRKFAVIR HQQSLLYKEY LSEKDIWKTD SEMIREEKRK
LEDQAEQDAV KVKEYNNLLS ALQMDSNEMK KMLSENSRKI TVLQVNEKSL IRQYTTLVEM
ERHLRKENGK HRNDVIAMEA EVTEKLGSLQ RFKEMAIFKI AALQKVIDNS VSLSELELAN
KQYNELTTKY RDILQKDNML VQRTSNLEHL ECENASLKEQ MEAISKELEI TKEKLHTIEQ
AWEQETKLGN DSNMDKAKKS MTNSDIVSIS KKITVLEMKE LNERQRAEHC QKMYEHLRTS
LKQMEERNFE LETKFTELTK INLDAQKVEQ MLRDELADSV TKAVSDADRQ RILELEKSEV
ELKVEVSKLR EISDIAKRQV DFLNSQQQSR EKEVESLRTQ LLDFQAQSDE KALIAKLHQH
VVSLQISEAT ALGKLESVTS KLQKMEAYNL RLEQKLDEKE QALYYARLEG RNRAKHLRQT
IQSLRRQFSG ALPLAQQEKF SKTMIQLQND KLKIMQEMKN SQQEHRNMEN KTLELELKLK
GLEELISTLK DARGAQKVIN WHVKIEELRL QELKLNRELV KGKEEIKYLN NIISEYEHTI
NSLEEEIVQQ SKFHEERQMA WDQREVELER QLDIFDHQQN EILSAAQKFE DSTGSMPDPS
LPLPNQLEIA LRKIKENIQV ILKTQATCKS LEEKLKEKES ALRLAEQNIL SRDKVINELR
LRLPATADRE KLIAELERKE LEPKSHHTMK IAHQTIANMQ ARLNHKEEVL KKYQHLLEKA
REEQREIVKK HEEDLHVLHH KLEQQADNSL NKFRQTAQDL LKQSPAPVPT NKHFIRLAEM
EQTVAEQDDS LSSLLTKLKK VSKDLEKQKE ITELKVREFE NTKLRLQETH ASEVKKVKAE
VEDLRHALAQ AHKDSQSLKS ELQAQKEANS RAPTTTMRNL VDRLKSQLAL KEKQQKALSR
ALLELRSEMT AAAEERIIAV TSQKEANLNV QQVVERHTRE LKSQIEDLNE NLLKLKEALK
TSKNKENSLA DDLNELNNEL QKKQKAYNKI LREKDGIDQE NDELRRQIKR LSSGLQSKTL
IDNKQSLIDE LQKKVKKLES QLERKVDDVD IKPVKEKSSK EELIRWEEGK KWQTKVEGLR
NRLKEKEGEA HGLAKQLNTL KELFAKADKE KLTLQKKLKT TGMTVDQVLG VRALESEKEL
EELKKKNLDL ENDILYMRTQ QALPRDSVVE DLHLQNKYLQ EKLHTLEKKL SKEKYSQSLT
SEIESDDHCQ KEQELQKENL KLSSENIELK FQLEQANKDL PRLKNQVKDL KEMCEFLKKG
KLELERKLGQ VRGAGRSGKT IPELEKTIGL MKKVVEKVQR ENEQLKKASG ILTSEKMATI
EEENRNLKAE LEKLKAHFGR QLSMQFESKN KGTEKIVAEN ERLRKELKKE IEASEKLRIA
KNNLELVNDK MAAQLEETGK RLQFAESRAP QLEGADSKSW KSIVVSRVYE TKMKELESDI
AKKNQSITDL KQLVREATER EQKAKKYTED LEQQIEILKN VPEGAETEQE LIRELQLLRL
ANNQMDKERA ELIHQIEINK DQTRADSSIP DSDQLKEKIN DLETQLRKLE LEKQHSKEEV
KKLKKELENF DPSFFEEIED LKYNYKEEVK KNILLEEKLK KLSEQFGFEL PSPLAASEHS
EDGESPHSFP IY
