CEP89_MOUSE
ID CEP89_MOUSE Reviewed; 791 AA.
AC Q9CZX2; Q8C127;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Centrosomal protein of 89 kDa;
DE Short=Cep89;
DE AltName: Full=Coiled-coil domain-containing protein 123;
GN Name=Cep89; Synonyms=Ccdc123;
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=Embryo, and Skin;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
CC -!- FUNCTION: Required for ciliogenesis. Also plays a role in mitochondrial
CC metabolism where it may modulate complex IV activity (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}.
CC Cytoplasm, cytoskeleton, spindle pole {ECO:0000250}. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome, centriole
CC {ECO:0000250}. Mitochondrion intermembrane space {ECO:0000250}.
CC Note=Localizes to the distal appendage region of the centriole, which
CC anchors the mother centriole to the plasma membrane. {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC26301.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK012067; BAB28005.1; -; mRNA.
DR EMBL; AK029107; BAC26301.1; ALT_FRAME; mRNA.
DR CCDS; CCDS39911.1; -.
DR RefSeq; NP_082396.1; NM_028120.2.
DR AlphaFoldDB; Q9CZX2; -.
DR SMR; Q9CZX2; -.
DR BioGRID; 215178; 4.
DR IntAct; Q9CZX2; 1.
DR MINT; Q9CZX2; -.
DR STRING; 10090.ENSMUSP00000078383; -.
DR iPTMnet; Q9CZX2; -.
DR PhosphoSitePlus; Q9CZX2; -.
DR MaxQB; Q9CZX2; -.
DR PaxDb; Q9CZX2; -.
DR PRIDE; Q9CZX2; -.
DR ProteomicsDB; 280072; -.
DR Antibodypedia; 47945; 121 antibodies from 16 providers.
DR DNASU; 72140; -.
DR Ensembl; ENSMUST00000079414; ENSMUSP00000078383; ENSMUSG00000023072.
DR GeneID; 72140; -.
DR KEGG; mmu:72140; -.
DR UCSC; uc009gjv.1; mouse.
DR CTD; 84902; -.
DR MGI; MGI:1919390; Cep89.
DR VEuPathDB; HostDB:ENSMUSG00000023072; -.
DR eggNOG; ENOG502QWK8; Eukaryota.
DR GeneTree; ENSGT00390000018876; -.
DR HOGENOM; CLU_023281_0_0_1; -.
DR InParanoid; Q9CZX2; -.
DR OMA; LRMGPNW; -.
DR OrthoDB; 476357at2759; -.
DR PhylomeDB; Q9CZX2; -.
DR TreeFam; TF329234; -.
DR Reactome; R-MMU-5620912; Anchoring of the basal body to the plasma membrane.
DR BioGRID-ORCS; 72140; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Cep89; mouse.
DR PRO; PR:Q9CZX2; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9CZX2; protein.
DR Bgee; ENSMUSG00000023072; Expressed in undifferentiated genital tubercle and 233 other tissues.
DR ExpressionAtlas; Q9CZX2; baseline and differential.
DR Genevisible; Q9CZX2; MM.
DR GO; GO:0005814; C:centriole; IDA:MGI.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0097539; C:ciliary transition fiber; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
DR GO; GO:0031514; C:motile cilium; IDA:MGI.
DR GO; GO:0097730; C:non-motile cilium; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0000922; C:spindle pole; ISS:UniProtKB.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0007268; P:chemical synaptic transmission; IEA:InterPro.
DR GO; GO:0060271; P:cilium assembly; ISS:UniProtKB.
DR GO; GO:0007005; P:mitochondrion organization; IBA:GO_Central.
DR GO; GO:1905515; P:non-motile cilium assembly; ISO:MGI.
DR InterPro; IPR033545; CEP89.
DR PANTHER; PTHR36170; PTHR36170; 1.
PE 1: Evidence at protein level;
KW Cilium biogenesis/degradation; Coiled coil; Cytoplasm; Cytoskeleton;
KW Mitochondrion; Phosphoprotein; Reference proteome.
FT CHAIN 1..791
FT /note="Centrosomal protein of 89 kDa"
FT /id="PRO_0000288810"
FT REGION 27..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 252..291
FT /evidence="ECO:0000255"
FT COILED 370..598
FT /evidence="ECO:0000255"
FT COILED 670..737
FT /evidence="ECO:0000255"
FT COMPBIAS 29..45
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..75
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..113
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..155
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..200
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 50
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96ST8"
SQ SEQUENCE 791 AA; 90320 MW; D0A53B950CB75113 CRC64;
MLLSFRRNRR SQFNHIIHGF LPAASIAPKP AVPRTPPPRS PNPSPERPRS ALAAAILATT
LTGQTVAIPQ PRQRSRSESD ASDIEKDSFI KPYATTSELR LRQSWQNEPR RTSLPSFEML
GYGEDEDAET QVSTSCRESE STWKDVGDGR DATYTVPHRD QVLPSQKLVR KDDAPQPDWL
SDSSSSSSSS TPQHTQQKDV KHSVLNLEGE KVRLHEKPPP SPDVAGRIHQ RYTEITKEKF
AELKEETVHL YSANQALSCE LSALRQAMKD LQLKLKLVEK DNRKLKETEK ASCQEGVTPE
LLCLRKQSQD LVDENEGLKM IVHRLNVELS RYQTKFRPLS EEESSHIQGL PSKGPTPPWL
VDIKYLSPLL LAYEDRMKEK DKLSTALEEE MKTFRLRVQE VVKENEALHQ ELTKRSPVTV
EEWRQLQTQA ELVLDENKLL IEQLEIQQAK ARDTHQAHLQ DVSKLTKQLV LLEAKTQGQE
KQLVESTEQL ESLQAKCTEL KAQLDSKIAV DVHTSIVNEL KSQLQKEEEK DSAEMEELMA
KLTALQVQKK SLLLEKSSWA TRNRALEAEL ERTRKANRRY QKRIDVLRKQ VEKAMGKEMS
AHQYLANLVG LAETVTKERD SLKYLAQCLE SEKHGVLNKI LKGNIRLGKL EERVKGYKKQ
AALKLGDIHH RLKEQQEDFA GKAAQYQKEV KHLHRMLQEK QEVLDEALQQ KRNMEGELEM
VLESTAKENR RMRSLLQATL ERRSTQHVTA PPDTCLRRSS QGDLLIGHDF SYGDVQLLAT
TNRQSLGESM A
