CP110_MOUSE
ID CP110_MOUSE Reviewed; 1004 AA.
AC Q7TSH4; Q6A072;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Centriolar coiled-coil protein of 110 kDa;
DE AltName: Full=Centrosomal protein of 110 kDa;
DE Short=Cep110;
DE Short=Cp110;
GN Name=Ccp110; Synonyms=Cep110, Cp110, Kiaa0419;
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 MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 165-959.
RC TISSUE=Embryonic intestine;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-364 AND SER-398, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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).
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=23141541; DOI=10.1016/j.cell.2012.10.010;
RA Goetz S.C., Liem K.F. Jr., Anderson K.V.;
RT "The spinocerebellar ataxia-associated gene tau tubulin kinase 2 controls
RT the initiation of ciliogenesis.";
RL Cell 151:847-858(2012).
RN [5]
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 [6]
RP SUBCELLULAR LOCATION.
RX PubMed=26670998; DOI=10.1016/j.cub.2015.10.028;
RA Stinchcombe J.C., Randzavola L.O., Angus K.L., Mantell J.M., Verkade P.,
RA Griffiths G.M.;
RT "Mother centriole distal appendages mediate centrosome docking at the
RT immunological synapse and reveal mechanistic parallels with ciliogenesis.";
RL Curr. Biol. 25:3239-3244(2015).
RN [7]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=26965371; DOI=10.1242/dev.130120;
RA Yadav S.P., Sharma N.K., Liu C., Dong L., Li T., Swaroop A.;
RT "Centrosomal protein CP110 controls maturation of mother centriole during
RT cilia biogenesis.";
RL Development 143:1491-1501(2016).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=30375385; DOI=10.1038/s41467-018-06990-9;
RA Huang N., Zhang D., Li F., Chai P., Wang S., Teng J., Chen J.;
RT "M-Phase Phosphoprotein 9 regulates ciliogenesis by modulating CP110-CEP97
RT complex localization at the mother centriole.";
RL Nat. Commun. 9:4511-4511(2018).
CC -!- FUNCTION: Necessary for centrosome duplication at different stages of
CC procentriole formation. Acts as a key negative regulator of
CC ciliogenesis in collaboration with CEP97 by capping the mother
CC centriole thereby preventing cilia formation (PubMed:23141541). Also
CC involved in promoting ciliogenesis. May play a role in the assembly of
CC the mother centriole subdistal appendages (SDA) thereby effecting the
CC fusion of recycling endosomes to basal bodies during cilia formation
CC (PubMed:26965371). Required for correct spindle formation and has a
CC role in regulating cytokinesis and genome stability via cooperation
CC with CALM1 and CETN2 (By similarity). {ECO:0000250|UniProtKB:O43303,
CC ECO:0000269|PubMed:23141541, ECO:0000269|PubMed:26965371}.
CC -!- SUBUNIT: Interacts with CALM1, CETN2, CEP76, CEP97, CEP104, CEP290,
CC TALPID3. Seems to associate with discrete CETN2, CEP97 and CEP290-
CC containing complexes. Interacts with NEURL4 and CCNF; these
CC interactions are not mutually exclusive and both lead to CCP110
CC ubiquitination and proteasome-dependent degradation. Via its
CC interaction with NEURL4, may indirectly interact with HERC2. Interacts
CC with KIF24, leading to its recruitment to centrioles. Interacts with
CC USP20 and USP33 (By similarity). Interacts with MPHOSPH9 (By
CC similarity). {ECO:0000250|UniProtKB:O43303}.
CC -!- INTERACTION:
CC Q7TSH4; P62204: Calm3; NbExp=4; IntAct=EBI-646843, EBI-397460;
CC Q7TSH4; Q6A078: Cep290; NbExp=3; IntAct=EBI-646843, EBI-1811999;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome, centriole {ECO:0000250|UniProtKB:O43303}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000269|PubMed:23807208, ECO:0000269|PubMed:30375385}. Cytoplasm,
CC cytoskeleton, cilium basal body {ECO:0000269|PubMed:23807208}.
CC Note=Recruited early and then associates with the growing distal tips
CC (PubMed:23141541). Recruited to the mother centriole by KIF24 (By
CC similarity). Removed from centrioles by TTBK2, leading to initiation of
CC ciliogenesis and localizes only to the daughter centriole in ciliated
CC cells (PubMed:23141541). In cytotoxic T lymphocytes remains associated
CC with the mother centriole during docking of the centrosome at the
CC immunological synapse upon target contact (PubMed:26670998). Recruited
CC at the distal end of the mother centriole by MPHOSPH9 (By similarity).
CC {ECO:0000250|UniProtKB:O43303, ECO:0000269|PubMed:23141541,
CC ECO:0000269|PubMed:26670998}.
CC -!- PTM: Phosphorylated by CDKs. {ECO:0000250}.
CC -!- PTM: Ubiquitinated by the SCF(CCNF) during G2 phase, leading to its
CC degradation by the proteasome and preventing centrosome reduplication.
CC Deubiquitinated by USP33 in S and G2/M phase, leading to stabilize
CC CCP110 during the period which centrioles duplicate and elongate (By
CC similarity). {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Lethal within a few hours after birth with
CC multiple defects in organogenesis. Mice show an early block in cilia
CC formation and a phenotype reminiscent of human short rib-polydactyly
CC syndrome. {ECO:0000269|PubMed:26965371}.
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DR EMBL; BC053103; AAH53103.1; -; mRNA.
DR EMBL; AK172946; BAD32224.1; -; mRNA.
DR CCDS; CCDS21775.1; -.
DR RefSeq; NP_892040.1; NM_182995.1.
DR AlphaFoldDB; Q7TSH4; -.
DR SMR; Q7TSH4; -.
DR BioGRID; 221690; 8.
DR CORUM; Q7TSH4; -.
DR IntAct; Q7TSH4; 13.
DR STRING; 10090.ENSMUSP00000102167; -.
DR iPTMnet; Q7TSH4; -.
DR PhosphoSitePlus; Q7TSH4; -.
DR EPD; Q7TSH4; -.
DR jPOST; Q7TSH4; -.
DR MaxQB; Q7TSH4; -.
DR PaxDb; Q7TSH4; -.
DR PRIDE; Q7TSH4; -.
DR ProteomicsDB; 283434; -.
DR Antibodypedia; 42931; 192 antibodies from 35 providers.
DR DNASU; 101565; -.
DR Ensembl; ENSMUST00000038650; ENSMUSP00000038881; ENSMUSG00000033904.
DR Ensembl; ENSMUST00000106557; ENSMUSP00000102167; ENSMUSG00000033904.
DR GeneID; 101565; -.
DR KEGG; mmu:101565; -.
DR UCSC; uc009jkj.1; mouse.
DR CTD; 9738; -.
DR MGI; MGI:2141942; Ccp110.
DR VEuPathDB; HostDB:ENSMUSG00000033904; -.
DR eggNOG; ENOG502QUVS; Eukaryota.
DR GeneTree; ENSGT00390000004090; -.
DR HOGENOM; CLU_302049_0_0_1; -.
DR InParanoid; Q7TSH4; -.
DR OMA; TDCVKEK; -.
DR OrthoDB; 408678at2759; -.
DR PhylomeDB; Q7TSH4; -.
DR TreeFam; TF332788; -.
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-5689880; Ub-specific processing proteases.
DR Reactome; R-MMU-8854518; AURKA Activation by TPX2.
DR Reactome; R-MMU-9013424; RHOV GTPase cycle.
DR BioGRID-ORCS; 101565; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Ccp110; mouse.
DR PRO; PR:Q7TSH4; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q7TSH4; protein.
DR Bgee; ENSMUSG00000033904; Expressed in superior cervical ganglion and 215 other tissues.
DR ExpressionAtlas; Q7TSH4; baseline and differential.
DR Genevisible; Q7TSH4; MM.
DR GO; GO:0005814; C:centriole; IDA:MGI.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005929; C:cilium; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005815; C:microtubule organizing center; IDA:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0007099; P:centriole replication; ISO:MGI.
DR GO; GO:0051298; P:centrosome duplication; ISS:UniProtKB.
DR GO; GO:0032053; P:ciliary basal body organization; IMP:UniProtKB.
DR GO; GO:1903723; P:negative regulation of centriole elongation; IBA:GO_Central.
DR GO; GO:1902018; P:negative regulation of cilium assembly; IDA:UniProtKB.
DR GO; GO:0045724; P:positive regulation of cilium assembly; IMP:UniProtKB.
DR GO; GO:0032465; P:regulation of cytokinesis; ISO:MGI.
DR InterPro; IPR033207; CCP110.
DR PANTHER; PTHR13594; PTHR13594; 1.
PE 1: Evidence at protein level;
KW Cell projection; Cilium; Cilium biogenesis/degradation; Coiled coil;
KW Cytoplasm; Cytoskeleton; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..1004
FT /note="Centriolar coiled-coil protein of 110 kDa"
FT /id="PRO_0000089461"
FT REGION 1..221
FT /note="CEP97 binding"
FT /evidence="ECO:0000250"
FT REGION 64..82
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000250"
FT REGION 67..82
FT /note="Required for interaction with CEP290"
FT /evidence="ECO:0000250|UniProtKB:O43303"
FT REGION 147..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 239..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 349..564
FT /note="Interaction with CEP76"
FT /evidence="ECO:0000250"
FT REGION 401..433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 773..813
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000250"
FT REGION 901..916
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000250"
FT REGION 955..1004
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 51..90
FT /evidence="ECO:0000255"
FT COILED 641..699
FT /evidence="ECO:0000255"
FT COMPBIAS 239..271
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..433
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 955..983
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 170
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43303"
FT MOD_RES 364
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 370
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43303"
FT MOD_RES 398
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 550
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43303"
SQ SEQUENCE 1004 AA; 111139 MW; C8D81F5F2FE213A8 CRC64;
MEEYEEFCEK ALGRAQEASL STGSFLPAQA ESVSLIRFHG VAVLSPLLTI EKRKKIQEEK
QKALDVQSRK QANRKKALLT RVQEILENVQ VRKAPNASDF DQWATETIYS NPEVTDLNVP
VRVPNSLPSP TEHCTSVKLE KITGLLPVNN EDQQTPKRVG LPGDSEVSGS LRQCESPESR
QAEDGAALRL SSASPQETII SDVLGKEEQD PSCLAEVTPD PYIMSLQNLM KRSKEYVERE
LSSRSLRNSL KRSVNETHSD RENDAAKASD CVKEKAPPMP IGRHCGSAIP DKPSLNKSNV
LLQGASQASS MGTAGLASFS KIDLPAGAAP PAAPDAGSDF TVIPTFVTEN KVKSLKGPYA
KLPSPEPSMS PTMHRRHSRS ASACQILINN PVNACELSPK GKEEAVDRTA PAAAETTNES
ETVPKSPTDL TGVCSSNVSA TKITSESTRE MVVGKPSQRQ QALGAHLGNN VTVERSAMEG
PFIADDRGAQ KVDGTCMAVP KLHELQPSSQ CVSSQTLEDV CELKSASLLA KNSCNLQMEL
NKSYDVKHPS PLLTQTQTSR QQMDTPPVFR GNEQFVDNSF EKVKRRLDLD VDSLQKENCP
YIITAGVAEQ ERDRLLERRY PKGFVHINKN KMLETSPKEG QELLKSKMLA FEEMRKRLEE
QHAQQLSLLI AEQEREQEQL QKEIEEQEKM LKEKAVTTDV SDLNSALEWR QRTDSALLET
MLSQVDSLQT SNNSGFITSA LQYSFGSAGE APFYLWGSLT SGVTRVSGTR PCGRAQAKWS
QVFNPEIHAK FNKITAVAKG FLTRKLMQTD KLKQLRQTVK DTMEFIRSFQ SEAPLKRGVV
SAQDASLQER VLAQLRAALY GIHDIFFVMD AAERMSILHH DREARKEKLL RQMDKMKSPR
VALSVATQKS LDRKKFMKVA EMGMPNKKFL LKQNPSETRV LQPNQGQNAP VHRLLSRQGT
PKTSVKGVVQ NRQKPSQSRV PNRAPVSGAY AGKTQRKRPN VATI
