CE162_DANRE
ID CE162_DANRE Reviewed; 1367 AA.
AC E7F5E1;
DT 26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT 08-MAR-2011, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Centrosomal protein of 162 kDa;
DE Short=Cep162;
GN Name=cep162; ORFNames=si:ch211-198c19.2;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=23644468; DOI=10.1038/ncb2739;
RA Wang W.J., Tay H.G., Soni R., Perumal G.S., Goll M.G., Macaluso F.P.,
RA Asara J.M., Amack J.D., Bryan Tsou M.F.;
RT "CEP162 is an axoneme-recognition protein promoting ciliary transition zone
RT assembly at the cilia base.";
RL Nat. Cell Biol. 15:591-601(2013).
CC -!- FUNCTION: Required to promote assembly of the transition zone in
CC primary cilia. Acts by specifically recognizing and binding the
CC axonemal microtubule. {ECO:0000269|PubMed:23644468}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome, centriole {ECO:0000250}. Note=Localizes to the
CC distal end of centrioles throughout the cell cycle. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed during early embryonic
CC development. {ECO:0000269|PubMed:23644468}.
CC -!- DEVELOPMENTAL STAGE: Expressed maternally and zygotically.
CC -!- DISRUPTION PHENOTYPE: Cilia defects such as body curvature,
CC hydrocephalus and left-right asymmetry. Ciliogenesis is blocked at the
CC stage of transition zone assembly. {ECO:0000269|PubMed:23644468}.
CC -!- SIMILARITY: Belongs to the CEP162 family. {ECO:0000305}.
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DR EMBL; BX088579; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_690522.2; XM_685430.5.
DR AlphaFoldDB; E7F5E1; -.
DR SMR; E7F5E1; -.
DR STRING; 7955.ENSDARP00000121710; -.
DR PaxDb; E7F5E1; -.
DR Ensembl; ENSDART00000142104; ENSDARP00000121710; ENSDARG00000087369.
DR Ensembl; ENSDART00000178753; ENSDARP00000144310; ENSDARG00000087369.
DR GeneID; 562035; -.
DR CTD; 22832; -.
DR ZFIN; ZDB-GENE-100922-266; cep162.
DR eggNOG; ENOG502QSPF; Eukaryota.
DR GeneTree; ENSGT00390000009631; -.
DR HOGENOM; CLU_005179_0_0_1; -.
DR InParanoid; E7F5E1; -.
DR OMA; NESRGFD; -.
DR OrthoDB; 520583at2759; -.
DR PhylomeDB; E7F5E1; -.
DR TreeFam; TF330884; -.
DR PRO; PR:E7F5E1; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 16.
DR Bgee; ENSDARG00000087369; Expressed in testis and 20 other tissues.
DR ExpressionAtlas; E7F5E1; baseline.
DR GO; GO:0005879; C:axonemal microtubule; ISS:UniProtKB.
DR GO; GO:0005814; C:centriole; ISS:UniProtKB.
DR GO; GO:0005813; C:centrosome; IBA:GO_Central.
DR GO; GO:0060271; P:cilium assembly; IMP:UniProtKB.
DR GO; GO:0001947; P:heart looping; IMP:ZFIN.
DR InterPro; IPR038774; CEP162-like.
DR PANTHER; PTHR34031; PTHR34031; 1.
PE 2: Evidence at transcript level;
KW Cilium biogenesis/degradation; Coiled coil; Cytoplasm; Cytoskeleton;
KW Microtubule; Reference proteome.
FT CHAIN 1..1367
FT /note="Centrosomal protein of 162 kDa"
FT /id="PRO_0000422824"
FT REGION 21..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 158..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 251..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 337..500
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1015..1042
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1072..1123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 573..688
FT /evidence="ECO:0000255"
FT COILED 724..1081
FT /evidence="ECO:0000255"
FT COILED 1126..1345
FT /evidence="ECO:0000255"
FT COMPBIAS 21..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..118
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..174
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..196
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..404
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 405..420
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..453
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1015..1030
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1072..1101
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1367 AA; 155016 MW; D06F7B2DC44F9604 CRC64;
MAHRLTKEEL DQQFEQFLKE SVSDDSVDLG TSSKRPSVLD SLGKAPVRPV KKASASVPWW
QDDDDNDDDS EEKGMSSTGR SFLKSLRKTP SIKEVDEEQP KELFLEDEGN RDHVILSRDS
LEPEDSLVIP SAGARGLDTL DEDDDDARFL SNLKKVSSSS IDFSRINREQ ELSAPTSPLR
REEMDSTIEE EQRMNKDTAA SPAYSEDFEE EASDKSDVEP QEKKPERLGM LAKVSLHDSL
NSTDGALAPA VPSLAVAREN RPESKQTDMP ALEPAVQSYG QSGGSEMEAL QEAYRQISGS
AGVCEDGQVE AGRTPLSLST LQPASTVESD LPTAEELMQP IGPDSGFTRG FSLQPITEAV
PRSRDNQSPL RISSDESPFS SANEGYGGGN TANLTGGEHP DSYKFTQKSI SEEIRRLMQE
QDTSSQEPPP LKPKKRQVPA RSNASTSASS RKAPVPSVRV KKPESKPLHR VPAPSRAAQA
AKPPSPPTLR KAQNQTFKKT QNLNQTHTIK GLDTSLKLSS ELVESVQSFA AFLQHQVEAS
SLQDKGPFQA NKIASEAMTA HKGMQEKMDG GPELASLERL RLQLAKKERE LSLREDQLQE
QHKQELTALR QENYILQSKL HRAEEASNKR KWSFGEASDP VTEEKLKLIE KEMKEQETLI
QGYHQENEKL YLQMKALQAQ SKQNEEALFM ENQRLLTELS FARDRMNTNN IQRTIRERSI
VDQSFNIAEL TSQVQAAQKK EERLQEEVRR LKQEKQALHV DLEMMRKERD LAKVQAVCKS
GDKGFELKLL HDKHREEVTE LKKRLQWYAK NQELLDKDAA RLHAATAEIQ KLTEQVEKLK
AEVSRRANEQ QRKAKEKAGE AKRIQDLERQ LKQKEELLKR RHPNSLPALI LAAASTGAEE
DRLDVRSLAQ SSQTAALLER RVHRLEAELE GRDEAAKRSL RAMEQQYHRI KLQYEQQISD
LEQRLSEKSH SYPAISSELI KSHTQTLKAE LEEVKEVHQK QVSVLQAEVD SLQEQLRQAQ
ASTQTEKPAR SPSRHQLHAE AAQAARIERL TQELNSKSRS IQELTRTIER LQRERRTMLS
GPSHERPNNE PKRHLGTAKD TKKPSVETFP PTQDEKDYHP GAFSGTHISE VQLENDSLRT
KLEELEVLRE KEKVSLQAAV THAQNQLLRI EEQNAEQLTS VKAEHRKEIE HLLARHALEH
SSSRVAELTS QLNTQEIIVQ HLQGQVKELQ GTKEALAVTK LREETLQNQL SKLLEELKEA
KEAHSPELKH FTSLEQKIQS MEFRYSQREK QLQQVIADTR RVVEQEQQSE VERWRKLAQG
RAKELEAFRM ELDSILDVLR ELQRQGVVIP MPEHTSTNTH TYLPLRS
