CEP83_MOUSE
ID CEP83_MOUSE Reviewed; 692 AA.
AC Q9D5R3; Q3U7X7; Q3UX57; Q80VF0;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Centrosomal protein of 83 kDa;
DE Short=Cep83;
DE AltName: Full=Coiled-coil domain-containing protein 41;
GN Name=Cep83; Synonyms=Ccdc41;
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; TISSUE=Bone marrow, and Testis;
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, and Czech II; TISSUE=Eye, and Mammary gland;
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-689, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Pancreas;
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.
RX PubMed=23348840; DOI=10.1101/gad.207043.112;
RA Tanos B.E., Yang H.J., Soni R., Wang W.J., Macaluso F.P., Asara J.M.,
RA Tsou M.F.;
RT "Centriole distal appendages promote membrane docking, leading to cilia
RT initiation.";
RL Genes Dev. 27:163-168(2013).
CC -!- FUNCTION: Component of the distal appendage region of the centriole
CC involved in the initiation of primary cilium assembly. May collaborate
CC with IFT20 in the trafficking of ciliary membrane proteins from the
CC Golgi complex to the cilium during the initiation of primary cilium
CC assembly. {ECO:0000269|PubMed:23348840}.
CC -!- SUBUNIT: Interacts with CEP164 and IFT20.
CC {ECO:0000250|UniProtKB:Q9Y592}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome, centriole {ECO:0000250|UniProtKB:Q9Y592}.
CC Note=Localizes specifically to the distal appendage region of the
CC centriole, which anchors the mother centriole to the plasma membrane.
CC Localizes to centrioles at all stages of the cell cycle, including
CC mitosis. {ECO:0000250|UniProtKB:Q9Y592}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9D5R3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9D5R3-2; Sequence=VSP_018333;
CC -!- SIMILARITY: Belongs to the CEP83 family. {ECO:0000305}.
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DR EMBL; AK015007; BAB29669.2; -; mRNA.
DR EMBL; AK135868; BAE22706.1; -; mRNA.
DR EMBL; AK152465; BAE31242.1; -; mRNA.
DR EMBL; AK152801; BAE31506.1; -; mRNA.
DR EMBL; AK153515; BAE32058.1; -; mRNA.
DR EMBL; AK151291; BAE30276.1; -; mRNA.
DR EMBL; BC043468; AAH43468.1; -; mRNA.
DR EMBL; BC070464; AAH70464.1; -; mRNA.
DR CCDS; CCDS36041.1; -. [Q9D5R3-1]
DR RefSeq; NP_084128.2; NM_029852.2. [Q9D5R3-1]
DR AlphaFoldDB; Q9D5R3; -.
DR SMR; Q9D5R3; -.
DR STRING; 10090.ENSMUSP00000020212; -.
DR iPTMnet; Q9D5R3; -.
DR PhosphoSitePlus; Q9D5R3; -.
DR EPD; Q9D5R3; -.
DR MaxQB; Q9D5R3; -.
DR PaxDb; Q9D5R3; -.
DR PRIDE; Q9D5R3; -.
DR ProteomicsDB; 280004; -. [Q9D5R3-1]
DR ProteomicsDB; 280005; -. [Q9D5R3-2]
DR Antibodypedia; 52583; 92 antibodies from 18 providers.
DR Ensembl; ENSMUST00000020212; ENSMUSP00000020212; ENSMUSG00000020024. [Q9D5R3-1]
DR GeneID; 77048; -.
DR KEGG; mmu:77048; -.
DR UCSC; uc007gvx.1; mouse. [Q9D5R3-1]
DR UCSC; uc007gvy.1; mouse. [Q9D5R3-2]
DR CTD; 51134; -.
DR MGI; MGI:1924298; Cep83.
DR VEuPathDB; HostDB:ENSMUSG00000020024; -.
DR eggNOG; ENOG502QWE2; Eukaryota.
DR GeneTree; ENSGT00940000154003; -.
DR HOGENOM; CLU_020145_1_0_1; -.
DR InParanoid; Q9D5R3; -.
DR OMA; KHQTENR; -.
DR OrthoDB; 1094723at2759; -.
DR PhylomeDB; Q9D5R3; -.
DR TreeFam; TF329199; -.
DR Reactome; R-MMU-5620912; Anchoring of the basal body to the plasma membrane.
DR BioGRID-ORCS; 77048; 4 hits in 71 CRISPR screens.
DR ChiTaRS; Cep83; mouse.
DR PRO; PR:Q9D5R3; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q9D5R3; protein.
DR Bgee; ENSMUSG00000020024; Expressed in spermatid and 255 other tissues.
DR Genevisible; Q9D5R3; MM.
DR GO; GO:0005814; C:centriole; IDA:MGI.
DR GO; GO:0097539; C:ciliary transition fiber; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0060271; P:cilium assembly; IMP:MGI.
DR GO; GO:0051660; P:establishment of centrosome localization; IMP:MGI.
DR GO; GO:0071539; P:protein localization to centrosome; ISO:MGI.
DR GO; GO:0048278; P:vesicle docking; ISO:MGI.
DR InterPro; IPR029631; Cep83.
DR PANTHER; PTHR23170:SF2; PTHR23170:SF2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cilium biogenesis/degradation; Coiled coil;
KW Cytoplasm; Cytoskeleton; Phosphoprotein; Reference proteome.
FT CHAIN 1..692
FT /note="Centrosomal protein of 83 kDa"
FT /id="PRO_0000234496"
FT COILED 32..625
FT /evidence="ECO:0000255"
FT COILED 656..689
FT /evidence="ECO:0000255"
FT MOD_RES 689
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..382
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_018333"
FT CONFLICT 690
FT /note="P -> S (in Ref. 2; AAH43468)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 692 AA; 81998 MW; 1635FB974AE16CDB CRC64;
MDTFPSLFPP GGDSRLNPEP EFQNMLIDER VRCEHHKHNY QALKIEHKRL QEEYVKSQNE
LKRVLIEKQA SQEKFQLLLE DLRGELVEKA RDIEKMKLQV LTPQKLELVK AQLQQELEAP
MRERFRTLDE EVERYRAEYN KLRYEYTFLK SEFEHQKEEF TRVSEEEKMK YKSEVARLEK
DKEELHNQLL SVDPTRDSKR MEQLVREKTH LLQKLKSLEA EVAELRAEKE NSGAQVENVQ
RIQVRQLAEM QATLRSLEAE KQSAKLQAER LEKELQSSNE QNTCLISKLH RADREISTLA
SEVKELKHAN KLEITDIKLE AARAKSELER ERNKIQSELD GLQSDNEILK STVEHHKALL
VEKDRELIRK VQAAKEEGYQ KLMVLQDEKL ELENRLSDLE KMKVERDVWR QSEKEQCEEK
LRASQMAEEA ARRELQSTRL KLQQQIVNTE KAEKEKLENS ELKQQISHLQ IQVTSLTQSE
NDLLNSNHML KDMVERLKQE CRNLRSQAEK AQLDVEKTLE EKQIQWLEEK HKLHERITDR
EEKYNQAKEK LQRAATAQKK RKSLHENKLK RLQEKVEVLE AKKEELETEN QVLNRQNVPF
EEYTRLQKRL KDIQRRHNEF RSLILVPNMP PTASISPANF QSAVTVPGAE LSFPPHLQEE
QHQRELSLLR KRLEELETTQ RKQLEELGSP GE
