CEP97_MOUSE
ID CEP97_MOUSE Reviewed; 856 AA.
AC Q9CZ62; Q8BL35;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Centrosomal protein of 97 kDa;
DE Short=Cep97;
DE AltName: Full=Leucine-rich repeat and IQ domain-containing protein 2;
GN Name=Cep97; Synonyms=Lrriq2;
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] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Corpora quadrigemina;
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 MRNA] (ISOFORM 1).
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-521, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, 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 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: Acts as a key negative regulator of ciliogenesis in
CC collaboration with CCP110 by capping the mother centriole thereby
CC preventing cilia formation. Required for recruitment of CCP110 to the
CC centrosome (By similarity). {ECO:0000250|UniProtKB:Q8IW35}.
CC -!- SUBUNIT: Interacts with CALM1, CEP76, CCP110, KIF24, TALPID3. Via its
CC interaction with CCP110, may indirectly interact with HERC2 and NEURL4
CC (By similarity). Interacts with MPHOSPH9 (By similarity).
CC {ECO:0000250|UniProtKB:Q8IW35}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000269|PubMed:30375385}. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome, centriole
CC {ECO:0000250|UniProtKB:Q8IW35}. Note=Recruited at the distal end of the
CC mother centriole by MPHOSPH9. {ECO:0000250|UniProtKB:Q8IW35}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9CZ62-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9CZ62-2; Sequence=VSP_021883;
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC32752.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK012971; BAB28575.1; -; mRNA.
DR EMBL; AK046486; BAC32752.1; ALT_FRAME; mRNA.
DR EMBL; AK154885; BAE32902.1; -; mRNA.
DR EMBL; BC067049; AAH67049.1; -; mRNA.
DR CCDS; CCDS28217.1; -. [Q9CZ62-1]
DR RefSeq; NP_001152836.1; NM_001159364.1.
DR RefSeq; NP_001152837.1; NM_001159365.1.
DR RefSeq; NP_001152838.1; NM_001159366.1.
DR RefSeq; NP_083091.1; NM_028815.4. [Q9CZ62-1]
DR AlphaFoldDB; Q9CZ62; -.
DR SMR; Q9CZ62; -.
DR BioGRID; 216572; 1.
DR IntAct; Q9CZ62; 3.
DR MINT; Q9CZ62; -.
DR STRING; 10090.ENSMUSP00000023270; -.
DR iPTMnet; Q9CZ62; -.
DR PhosphoSitePlus; Q9CZ62; -.
DR EPD; Q9CZ62; -.
DR MaxQB; Q9CZ62; -.
DR PaxDb; Q9CZ62; -.
DR PeptideAtlas; Q9CZ62; -.
DR PRIDE; Q9CZ62; -.
DR ProteomicsDB; 280006; -. [Q9CZ62-1]
DR ProteomicsDB; 280007; -. [Q9CZ62-2]
DR Antibodypedia; 15955; 169 antibodies from 25 providers.
DR DNASU; 74201; -.
DR Ensembl; ENSMUST00000023270; ENSMUSP00000023270; ENSMUSG00000022604. [Q9CZ62-1]
DR Ensembl; ENSMUST00000117468; ENSMUSP00000112687; ENSMUSG00000022604. [Q9CZ62-2]
DR Ensembl; ENSMUST00000118500; ENSMUSP00000112663; ENSMUSG00000022604. [Q9CZ62-2]
DR GeneID; 74201; -.
DR KEGG; mmu:74201; -.
DR UCSC; uc007zlr.2; mouse. [Q9CZ62-1]
DR CTD; 79598; -.
DR MGI; MGI:1921451; Cep97.
DR VEuPathDB; HostDB:ENSMUSG00000022604; -.
DR eggNOG; KOG0531; Eukaryota.
DR GeneTree; ENSGT00910000144283; -.
DR HOGENOM; CLU_016381_0_0_1; -.
DR InParanoid; Q9CZ62; -.
DR OMA; AYWRGFY; -.
DR OrthoDB; 1264004at2759; -.
DR PhylomeDB; Q9CZ62; -.
DR TreeFam; TF320816; -.
DR Reactome; R-MMU-5620912; Anchoring of the basal body to the plasma membrane.
DR Reactome; R-MMU-9013424; RHOV GTPase cycle.
DR BioGRID-ORCS; 74201; 5 hits in 70 CRISPR screens.
DR ChiTaRS; Cep97; mouse.
DR PRO; PR:Q9CZ62; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q9CZ62; protein.
DR Bgee; ENSMUSG00000022604; Expressed in rostral migratory stream and 225 other tissues.
DR ExpressionAtlas; Q9CZ62; baseline and differential.
DR Genevisible; Q9CZ62; MM.
DR GO; GO:0005814; C:centriole; ISO:MGI.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0030030; P:cell projection organization; IEA:UniProtKB-KW.
DR GO; GO:1902018; P:negative regulation of cilium assembly; IDA:UniProtKB.
DR GO; GO:1901673; P:regulation of mitotic spindle assembly; ISO:MGI.
DR Gene3D; 3.80.10.10; -; 2.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR032675; LRR_dom_sf.
DR PROSITE; PS50096; IQ; 1.
DR PROSITE; PS51450; LRR; 7.
PE 1: Evidence at protein level;
KW Alternative splicing; Cilium biogenesis/degradation; Cytoplasm;
KW Cytoskeleton; Leucine-rich repeat; Phosphoprotein; Reference proteome;
KW Repeat.
FT CHAIN 1..856
FT /note="Centrosomal protein of 97 kDa"
FT /id="PRO_0000263706"
FT REPEAT 37..58
FT /note="LRR 1"
FT REPEAT 59..80
FT /note="LRR 2"
FT REPEAT 81..102
FT /note="LRR 3"
FT REPEAT 103..124
FT /note="LRR 4"
FT REPEAT 125..146
FT /note="LRR 5"
FT REPEAT 147..168
FT /note="LRR 6"
FT REPEAT 171..192
FT /note="LRR 7"
FT REPEAT 196..205
FT /note="LRR 8"
FT DOMAIN 211..249
FT /note="LRRCT"
FT DOMAIN 550..579
FT /note="IQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT REGION 300..742
FT /note="CCP110-binding"
FT /evidence="ECO:0000250"
FT REGION 430..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 498..525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 579..853
FT /note="Interaction with MPHOSPH9"
FT /evidence="ECO:0000250|UniProtKB:Q8IW35"
FT REGION 646..672
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 737..840
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 431..451
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..522
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 648..662
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 737..754
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 755..773
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 784..807
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 808..833
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 308
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IW35"
FT MOD_RES 410
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IW35"
FT MOD_RES 497
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IW35"
FT MOD_RES 521
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 534
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8IW35"
FT MOD_RES 755
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IW35"
FT VAR_SEQ 1..72
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_021883"
SQ SEQUENCE 856 AA; 94641 MW; 619F0B577D0C15A9 CRC64;
MAVARVDGAL APGEGSVVNW SGQGLQKLGA NLPCEADVHT LILDKNQIIK LENLEKCKQL
IQLSVANNRL VRMMGVAKLT QLRVLNLPHN SIGCVEGLKD LVHLEWLNLA GNNLKTMEQV
NSCTALQHLD LSDNNIPQIG DVSKLISLKT LLLHGNIITS LRMAPAYLPR NLSILSLAEN
EIRDLNEISF LASLSELEQL SIMNNPCVMA TPSIPGFDYR PFIVSWCLNL RVLDGYVISQ
KESLKAEWLY SQGKGRSYRP GQHIQLVQYL ATVCPLTSAL GLQTAEDAKL EKILSKQRFH
QRQLMSQSQD EELSPLAAVE TRVHRTPECS SPGQDFQESE PVLQINSWVG ISSNDDQLYA
VKNNFPAAAH AARYSRNDLH LEDIQTDEDK LNCSLLSSES TFMPVASGLS PVSPTVELRL
QGINLGLEDD DGADEFTKGL ENQDEDKDKE KSLWDMSESC VEMLKRKIST EVSEAAGLLP
CPKSVIISAA LKEDTHSLTS LPESAGHSAS RTEANSEEAM SPATSEKFPC RILTQRPAAL
GQDKVTLQKL NAAATKLQAC WRGFYTRNYN QQAKGVRYEI RLRRMQEHIV CLTDEVRRLR
KERDEERVKT FVQEEAVRFL WNEVRSVQAW QQTVEQRLAS WPPDVPPISS TLASPKPPLF
PHHQDPSSDQ SSDWLVAEDE AAQGRSAPDF PDSGFHSSLT EQVPCLQDSL DFEKSSVESS
ENSVLGNSAD TVKCVKDRDS EATAEEHSDC SRESSASEQD NTLLQQYLTS VQQLDDAAEA
ADSDDVAGDG KRHLACSPER FDASSDSETH RVASTSQDEI SQTPENCQLN EEAQGQPPEC
DPAFQGLHVG VTVQPV
