CE162_MOUSE
ID CE162_MOUSE Reviewed; 1403 AA.
AC Q6ZQ06; B9EKN3; Q6P262;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Centrosomal protein of 162 kDa;
DE Short=Cep162;
DE AltName: Full=Protein QN1 homolog;
GN Name=Cep162; Synonyms=Kiaa1009, Qn1;
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]
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 114-733.
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
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. 10:167-180(2003).
RN [4]
RP PROTEIN SEQUENCE OF 1119-1128, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [5]
RP INTERACTION WITH CPNE4.
RX PubMed=12522145; DOI=10.1074/jbc.m212632200;
RA Tomsig J.L., Snyder S.L., Creutz C.E.;
RT "Identification of targets for calcium signaling through the copine family
RT of proteins. Characterization of a coiled-coil copine-binding motif.";
RL J. Biol. Chem. 278:10048-10054(2003).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-160, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Lung, Spleen, and 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).
CC -!- FUNCTION: Required to promote assembly of the transition zone in
CC primary cilia. Acts by specifically recognizing and binding the
CC axonemal microtubule. Localizes to the distal ends of centrioles before
CC ciliogenesis and directly binds to axonemal microtubule, thereby
CC promoting and restricting transition zone formation specifically at the
CC cilia base. Required to mediate CEP290 association with microtubules
CC (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with CPNE4 (PubMed:12522145). Interacts with alpha-
CC tubulin. Interacts with CEP290 (By similarity).
CC {ECO:0000250|UniProtKB:Q4KLH6, ECO:0000250|UniProtKB:Q5TB80,
CC ECO:0000269|PubMed:12522145}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome, centriole {ECO:0000250}. Cytoplasm, cytoskeleton,
CC spindle {ECO:0000250}. Nucleus {ECO:0000250}. Note=Localizes to the
CC distal end of centrioles throughout the cell cycle. During
CC ciliogenesis, found at the cilia base. Localizes to spindle
CC microtubules during mitosis (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the CEP162 family. {ECO:0000305}.
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DR EMBL; AC125370; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC150998; AAI50999.1; -; mRNA.
DR EMBL; BC151006; AAI51007.1; -; mRNA.
DR EMBL; AK129260; BAC98070.1; -; mRNA.
DR CCDS; CCDS52879.1; -.
DR RefSeq; NP_955020.2; NM_199316.2.
DR AlphaFoldDB; Q6ZQ06; -.
DR SMR; Q6ZQ06; -.
DR BioGRID; 238234; 6.
DR STRING; 10090.ENSMUSP00000091319; -.
DR iPTMnet; Q6ZQ06; -.
DR PhosphoSitePlus; Q6ZQ06; -.
DR EPD; Q6ZQ06; -.
DR MaxQB; Q6ZQ06; -.
DR PaxDb; Q6ZQ06; -.
DR PRIDE; Q6ZQ06; -.
DR ProteomicsDB; 281160; -.
DR Antibodypedia; 31712; 31 antibodies from 7 providers.
DR Ensembl; ENSMUST00000093802; ENSMUSP00000091319; ENSMUSG00000056919.
DR GeneID; 382090; -.
DR KEGG; mmu:382090; -.
DR UCSC; uc009qyg.1; mouse.
DR CTD; 22832; -.
DR MGI; MGI:1925343; Cep162.
DR VEuPathDB; HostDB:ENSMUSG00000056919; -.
DR eggNOG; ENOG502QSPF; Eukaryota.
DR GeneTree; ENSGT00390000009631; -.
DR HOGENOM; CLU_005179_0_0_1; -.
DR InParanoid; Q6ZQ06; -.
DR OMA; NESRGFD; -.
DR OrthoDB; 520583at2759; -.
DR PhylomeDB; Q6ZQ06; -.
DR TreeFam; TF330884; -.
DR Reactome; R-MMU-5620912; Anchoring of the basal body to the plasma membrane.
DR BioGRID-ORCS; 382090; 4 hits in 71 CRISPR screens.
DR ChiTaRS; Cep162; mouse.
DR PRO; PR:Q6ZQ06; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q6ZQ06; protein.
DR Bgee; ENSMUSG00000056919; Expressed in undifferentiated genital tubercle and 189 other tissues.
DR Genevisible; Q6ZQ06; MM.
DR GO; GO:0005879; C:axonemal microtubule; ISS:UniProtKB.
DR GO; GO:0034451; C:centriolar satellite; ISO:MGI.
DR GO; GO:0005814; C:centriole; ISS:UniProtKB.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0060271; P:cilium assembly; ISS:UniProtKB.
DR InterPro; IPR038774; CEP162-like.
DR PANTHER; PTHR34031; PTHR34031; 1.
PE 1: Evidence at protein level;
KW Cilium biogenesis/degradation; Coiled coil; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Microtubule; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..1403
FT /note="Centrosomal protein of 162 kDa"
FT /id="PRO_0000295629"
FT REGION 20..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 169..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 256..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 306..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 453..606
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1126..1147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 614..1124
FT /evidence="ECO:0000255"
FT COILED 1174..1386
FT /evidence="ECO:0000255"
FT COMPBIAS 182..210
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..235
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 453..472
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 504..528
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 537..553
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1126..1146
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 160
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 163
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4KLH6"
SQ SEQUENCE 1403 AA; 160855 MW; AA1363D5407D7FFF CRC64;
MAHYFKVDLD EEFERFMKEL SDDSFENSNK TPRQPNEDNK EMKKKDPVPW WIAEDDFEDD
GLLGTNVSYL KTKKTYQPVM DTEEESAEKV QFLKSSGTSI LSVDSLEANE LVVSEPHHST
LGLGLDTLEE QEEKEQFFAR LEKGLTSSID YSKLNQELDS DDSAQLKALH RYPRNTEPAE
DGCENESEQE ELPETYSDDF EDAEDADDPL ITKDEETHPK ENSESGKDSF PKQEEEKTGM
LANVVLLDSF DSVEDVGLSS QEKATPKAKA PPEITDDGPA ETGVPYGQSS GDTEALHQAY
CHVAHSLGDT GEPRIEASTV QTVRSSIKDG LQENEESSKN VSTTESDLPT VEELMQPIRI
DSYGIRAFDL QPISLKKATD SKEAESVGSL PLKTNTNTVS QDTRHAIQFP HKHDESVVLH
RTADEGMGSS CPATEEHLDK MYLEILKKKT SVNPSLLPQD DKMNQTSRSQ LGAGEEVPVI
GKQVPCKKAR STPSLPKRKP QSGLYASARS SGYGKPSSPL QLFSALEKKT SKDNTKTKSV
RSIPTSNQFR KREILSGTKL IKPAASNKPS PHREGSPATP KRPEDPSDDS FVQLQTEPLG
SYGGNREKEL LMLKRAQDAE EKWTGAQALM EQMKMTFCEK EKELENTVES LKRQQERELF
RLNQENYILQ AKLSSFEETS RKQRWLQFGE TSDPLTGEKL KQIQKEIQEQ ETLLQGYQQE
NERLYNQVKD LQEQNKKNEE RMFKENQNLF SELASLKEQM HKNHFLSQAV ENTEPTKNQS
FTDLLAELRA AQKEKNHLME DIKRLKQDKQ ALEVDLEKVK RERDQAKDQI AYATGEKLYE
IKILEETHKQ EVSRLQKRLQ WYAENQELLD RDAARLREAN EETEKLRLEI EKLKTESGSP
ATQQRLRSKE RALDAKRIQD LERQVKEMEG ILKRRYPNSL PALILAASAA GDSVDRNTVE
FMERRIKKLE ADLEGKDEEA KKSLRTMEQQ FQKMKIQYEQ RLEEQEQLLA HRQKEAPQSQ
RNSSSRLKAL ETELGDIKEA HQITVRKLEA EIDVLKHQNA DLEHKKNDKG DQGLQSIEFQ
VEQAQARAKL ARLNEELAAK GREIQDLTKT VERLQKERRM MLSRQIPRSR EETAAKRLKK
DPNRGHGNAF PETLDGKLYH PHTFTDSHIS EVLEENYRLR SELEGLILER SKLKMESEAA
VCQLENSMKR VKDDAAAHIA SLKASHEREI EKLLCQNAIE NSSSKVAELN RKIATQEVLL
KHFQGQVNEL QGKQESLAVS QVREEILQKQ ITKLLEELKE AKENHTPEMK HFMGLERKIK
QMEMRHRQRE QELQQIIQQT RQVVETEQNK EVEKWKRLAQ LKNRELDKFR TELDSILDVL
RELHRQGVVV PMALAGEENT AEF
