CE290_BOVIN
ID CE290_BOVIN Reviewed; 1468 AA.
AC Q9TU23; Q0P567;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 25-MAY-2022, entry version 108.
DE RecName: Full=Centrosomal protein of 290 kDa;
DE Short=Cep290;
DE AltName: Full=Nephrocystin-6;
DE Flags: Fragment;
GN Name=CEP290; Synonyms=NPHP6;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Trachea;
RA Jovov B., Ripoll P.J., Benos D.J.;
RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 685-1468 (ISOFORM 2).
RC STRAIN=Hereford; TISSUE=Basal ganglia;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP INTERACTION WITH FAM161A.
RX PubMed=22940612; DOI=10.1093/hmg/dds368;
RA Di Gioia S.A., Letteboer S.J., Kostic C., Bandah-Rozenfeld D.,
RA Hetterschijt L., Sharon D., Arsenijevic Y., Roepman R., Rivolta C.;
RT "FAM161A, associated with retinitis pigmentosa, is a component of the
RT cilia-basal body complex and interacts with proteins involved in
RT ciliopathies.";
RL Hum. Mol. Genet. 21:5174-5184(2012).
CC -!- FUNCTION: Involved in early and late steps in cilia formation. Its
CC association with CCP110 is required for inhibition of primary cilia
CC formation by CCP110. May play a role in early ciliogenesis in the
CC disappearance of centriolar satellites and in the transition of primary
CC ciliar vesicles (PCVs) to capped ciliary vesicles (CCVs). Required for
CC the centrosomal recruitment of RAB8A and for the targeting of centriole
CC satellite proteins to centrosomes such as of PCM1. Required for the
CC correct localization of ciliary and phototransduction proteins in
CC retinal photoreceptor cells; may play a role in ciliary transport
CC processes. Required for efficient recruitment of RAB8A to primary
CC cilium. In the ciliary transition zone is part of the tectonic-like
CC complex which is required for tissue-specific ciliogenesis and may
CC regulate ciliary membrane composition. 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. Activates ATF4-mediated
CC transcription. {ECO:0000250|UniProtKB:O15078,
CC ECO:0000250|UniProtKB:Q6A078}.
CC -!- SUBUNIT: Part of the tectonic-like complex (also named B9 complex) (By
CC similarity). Interacts with ATF4 via its N-terminal region. Associates
CC with the BBSome complex, interacting (via N-terminus) with BBS4.
CC Interacts with IQCB1/NPHP5; IQCB1 and CEP290/NPHP6 are proposed to form
CC a functional NPHP5-6 module localized to the centrosome. Interacts with
CC NPHP4; the interaction likely requires additional interactors.
CC Interacts with ZNF423, FAM161A, CEP162, CEP162, CEP131, TALPID3,
CC CCDC13, CC2D2A, RPGRIP1. Can self-associate (homo- or heteromeric).
CC Interacts with CCP110; required for suppressing cilia formation (By
CC similarity). Interacts with RPGR (By similarity). Associates (via C-
CC terminus) with microtubules; association to microtubule is reduced in
CC response to cellular stress, such as ultraviolet light (UV) radiation
CC or heat shock, in a process that requires p38 MAP kinase signaling (By
CC similarity). Interacts with FAM161A (PubMed:22940612). Interacts with
CC PCM1 (By similarity). Interacts with CCDC66 (By similarity). Interacts
CC with ARMC9 and CSPP1 (By similarity). {ECO:0000250|UniProtKB:O15078,
CC ECO:0000250|UniProtKB:Q6A078, ECO:0000269|PubMed:22940612}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000250|UniProtKB:O15078}. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome, centriolar
CC satellite {ECO:0000250|UniProtKB:O15078}. Nucleus
CC {ECO:0000250|UniProtKB:Q6A078}. Cell projection, cilium
CC {ECO:0000250|UniProtKB:O15078}. Cytoplasm, cytoskeleton, cilium basal
CC body {ECO:0000250|UniProtKB:Q6A078}. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome, centriole
CC {ECO:0000250|UniProtKB:O15078}. Cytoplasmic vesicle
CC {ECO:0000250|UniProtKB:O15078}. Note=Displaced from centriolar
CC satellites in response to cellular stress, such as ultraviolet light
CC (UV) radiation or heat shock (By similarity). Found in the connecting
CC cilium of photoreceptor cells, base of cilium in kidney intramedullary
CC collecting duct cells (By similarity). Localizes at the transition
CC zone, a region between the basal body and the ciliary axoneme.
CC Localization at the ciliary transition zone as well as at centriolar
CC satellites is BBsome-dependent (By similarity).
CC {ECO:0000250|UniProtKB:O15078, ECO:0000250|UniProtKB:Q6A078}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9TU23-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9TU23-2; Sequence=VSP_021028, VSP_021029;
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 -!- SEQUENCE CAUTION:
CC Sequence=AAF00990.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF176816; AAF00990.1; ALT_INIT; mRNA.
DR EMBL; BC120445; AAI20446.1; -; mRNA.
DR RefSeq; NP_777147.1; NM_174722.2.
DR AlphaFoldDB; Q9TU23; -.
DR SMR; Q9TU23; -.
DR IntAct; Q9TU23; 1.
DR STRING; 9913.ENSBTAP00000005450; -.
DR PaxDb; Q9TU23; -.
DR PRIDE; Q9TU23; -.
DR GeneID; 282707; -.
DR KEGG; bta:282707; -.
DR CTD; 80184; -.
DR eggNOG; ENOG502QPTZ; Eukaryota.
DR InParanoid; Q9TU23; -.
DR OrthoDB; 27774at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0034451; C:centriolar satellite; ISS:UniProtKB.
DR GO; GO:0005814; C:centriole; IEA:UniProtKB-SubCell.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0035869; C:ciliary transition zone; IBA:GO_Central.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0036038; C:MKS complex; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0032391; C:photoreceptor connecting cilium; ISS:UniProtKB.
DR GO; GO:0043010; P:camera-type eye development; IBA:GO_Central.
DR GO; GO:0097711; P:ciliary basal body-plasma membrane docking; IBA:GO_Central.
DR GO; GO:1905349; P:ciliary transition zone assembly; IBA:GO_Central.
DR GO; GO:0001822; P:kidney development; IBA:GO_Central.
DR GO; GO:1905515; P:non-motile cilium assembly; IBA:GO_Central.
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:UniProtKB.
DR GO; GO:0015031; P:protein transport; ISS:UniProtKB.
DR InterPro; IPR032321; Cep209_CC5.
DR InterPro; IPR026201; Cep290.
DR PANTHER; PTHR18879; PTHR18879; 1.
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; Transport;
KW Ubl conjugation.
FT CHAIN <1..1468
FT /note="Centrosomal protein of 290 kDa"
FT /id="PRO_0000089463"
FT REGION 1060..1468
FT /note="Self-association (with itself or N-terminus)"
FT /evidence="ECO:0000250|UniProtKB:O15078"
FT REGION 1130..1152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1..25
FT /evidence="ECO:0000255"
FT COILED 52..121
FT /evidence="ECO:0000255"
FT COILED 172..292
FT /evidence="ECO:0000255"
FT COILED 318..528
FT /evidence="ECO:0000255"
FT COILED 559..592
FT /evidence="ECO:0000255"
FT COILED 627..688
FT /evidence="ECO:0000255"
FT COILED 736..1441
FT /evidence="ECO:0000255"
FT VAR_SEQ 1140..1347
FT /note="TSGIDSDDHYQREQELQRENLKLSSENIELKFQLEQANKDLPRLKNQVRDLK
FT EMCEFLKKEKAEVERKLGRVRGSGRSGKTIPELEKTIGLMKKVVEKVQRENEQLKKASG
FT ILTSEKMANIEMENEKLKAELEKLKVHLGRQLSMHYESKAKGTEKIVAENERLRKELKK
FT IEILKHVPEGDETEQGLQRELRVLRLANSQLEKEKEEL -> NVLCDTTTLSPLAASVN
FT KYRHNIFHKKNTLHRKQNNRITELRIKNKKEIDVSANLHHQVPRHNLQYYSNEEKHEAE
FT DIVDPTELNKSESRTNNTSSLFRSTEGTLTDFNPNFENDPNSKVQKINQDCCENDEQKD
FT KNREEKAKQDEKEKGHLTEEVSHSKHTDPAEASGEDRGWATGVAALNQCAEEGAQAHPE
FT TNAPGQPRNEAAQL (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_021028"
FT VAR_SEQ 1348..1468
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_021029"
FT NON_TER 1
SQ SEQUENCE 1468 AA; 171787 MW; 18A31723723A873E CRC64;
ERQLRKENGK QKNELMAMEA EVGEKIGRLQ RFKEMAVFKI AALQKVVDNS VSLSELELAN
RQYNELTAKY RDILQKDNML VQRTNNLEHL ECENVSLKEQ MESINKELEI TKEKLHTIEQ
AWEQETKLGN ESNMDKAKKS VTNSEIVSIS KKITMLEMKE LNERQRAEHS QKMYEHVKTS
LQQVEERNFE LETKFAELTR INLEAQKVEQ MLRDELADSV SKTVSDADRQ HILELEKSEM
ELKVEVSKLK EISDIAKRQV EILNAQQQSR EKEVESLRTQ LLDYQAQSDE KALIAKLHQH
VVSLQASEAA ALGKVESVAS KLQKVEAHTL RLEQKLDEKE QALFYARLEG RNRAKHLRQT
IQSLRRQFSG ALPLAQQEKF SKTMIQLQND KLKIMEEMKN SQQEHRSLKN KTLEMELKLK
GLEDLISTLK DARGAQKVIS WHTKIEELRL QELKLNRELV KDKEEIKYLN NIISEYENTI
SSLEEEIVQQ NKFHEERQMA WDQREVELER QLDVFDRQQS EILREAQKFE EATGSMPDPS
LPIPNQLEIA LRKIKENIRI ILETQATCRS LEEKLREKES ALRLAEENIL SRDKVINELR
LRLPATAEQE KLLAEFSRKE VEPKSHHTLK LAHQTIANMQ ARLNQKEEVL KKYQHLLEKA
REEQREIVKK HEEELHTLHR KLELQADNSL SKFKETAWDL IKQSPTPVPT NKHFIRLAEM
EQTVAEQDDS LSSLVIKLKQ VSQDLERQKE ITELKIKEFE NMKLRLQENH ADEVKKIKAE
VEDLRCLLVQ SQKESQSLKS ELQTQKEANS RAPTTTMRNL VERLKSQLAL KEKQQKALSR
ALLELRAEMT AAAEERIISM TSQKEANLNV QQIVDRHTKE LKSQIEDLNE NILKLKEALK
TSKNRENTLT DNLNDLTNEL QNKQKAYGKV LREKDAVDQE NNELKRQIKR LTSGLQGKPL
IDNKQSLIEE LQKKIKKLES QLERKVDEAE MKPMKEKSAR EEVIRWEEGK KWQTKIEGIR
NKLKEKEGEV YILTKQLTTL KDLFAKADKE KLTLQRKLKT TGLTVDQVMA ARVLESEKEL
EELKKRNLDL ENDISYMRSH QALPRDSVIE DLHLQNKYLQ EKLHALEKQL SKDAYSRPST
SGIDSDDHYQ REQELQRENL KLSSENIELK FQLEQANKDL PRLKNQVRDL KEMCEFLKKE
KAEVERKLGR VRGSGRSGKT IPELEKTIGL MKKVVEKVQR ENEQLKKASG ILTSEKMANI
EMENEKLKAE LEKLKVHLGR QLSMHYESKA KGTEKIVAEN ERLRKELKKI EILKHVPEGD
ETEQGLQREL RVLRLANSQL EKEKEELIHR IEISKDQNGP DSTISDPDHL MEKIKDLETQ
LRTSDMEKQH LKEEIQKLKK ELENFDPSFF EEIEDLKYNY KEEVKKNILL EEKLKKLSEQ
FGVELTSPVA ASEQFEDEQE NPVNFPIY
