CEP41_MOUSE
ID CEP41_MOUSE Reviewed; 373 AA.
AC Q99NF3; D3Z3U1; F7CSA6; Q3TTB5; Q8BT53;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Centrosomal protein of 41 kDa;
DE Short=Cep41;
DE AltName: Full=Testis-specific gene A14 protein;
GN Name=Cep41; Synonyms=Tsga14;
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 [MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J;
RA Brunner B., Kalamajka R., Ropers H.-H., Fundele R., Kalscheuer V.M.;
RT "Identification of a testis-specific gene (TSGA14) proximal to the
RT MEST/COPG2 imprinting cluster on chromosome 7.";
RL Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Embryo, Skin, 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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Eye;
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96; SER-99; THR-109; SER-114
RP AND SER-121, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, 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).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=22246503; DOI=10.1038/ng.1078;
RA Lee J.E., Silhavy J.L., Zaki M.S., Schroth J., Bielas S.L., Marsh S.E.,
RA Olvera J., Brancati F., Iannicelli M., Ikegami K., Schlossman A.M.,
RA Merriman B., Attie-Bitach T., Logan C.V., Glass I.A., Cluckey A.,
RA Louie C.M., Lee J.H., Raynes H.R., Rapin I., Castroviejo I.P., Setou M.,
RA Barbot C., Boltshauser E., Nelson S.F., Hildebrandt F., Johnson C.A.,
RA Doherty D.A., Valente E.M., Gleeson J.G.;
RT "CEP41 is mutated in Joubert syndrome and is required for tubulin
RT glutamylation at the cilium.";
RL Nat. Genet. 44:193-199(2012).
RN [9]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-343, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Required during ciliogenesis for tubulin glutamylation in
CC cilium. Probably acts by participating in the transport of TTLL6, a
CC tubulin polyglutamylase, between the basal body and the cilium.
CC {ECO:0000269|PubMed:22246503}.
CC -!- SUBUNIT: Found in a complex with TTLL6. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000250}. Cell projection, cilium
CC {ECO:0000269|PubMed:22246503}. Cytoplasm, cytoskeleton, cilium basal
CC body {ECO:0000269|PubMed:22246503}. Note=Localizes mainly to the cilium
CC basal body and in primary cilia.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q99NF3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q99NF3-2; Sequence=VSP_012249, VSP_012250;
CC -!- DISRUPTION PHENOTYPE: At 10-13 dpc, embryos show a range of phenotypes,
CC such as malformed hindbrain, exencephaly, brain hemorrhage, dilated
CC pericardial sac and lethality. For an unclear reason, some homozygous
CC mutants develop normally, suggesting presence of extragenic phenotypic
CC modifiers. {ECO:0000269|PubMed:22246503}.
CC -!- SIMILARITY: Belongs to the CEP41 family. {ECO:0000305}.
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DR EMBL; AJ278891; CAC33579.1; -; mRNA.
DR EMBL; AK019270; BAC25586.1; -; mRNA.
DR EMBL; AK132495; BAE21202.1; -; mRNA.
DR EMBL; AK161461; BAE36410.1; -; mRNA.
DR EMBL; AK170213; BAE41640.1; -; mRNA.
DR EMBL; AC155656; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466533; EDL13733.1; -; Genomic_DNA.
DR EMBL; BC031892; AAH31892.1; -; mRNA.
DR CCDS; CCDS19978.1; -. [Q99NF3-1]
DR RefSeq; NP_114387.1; NM_031998.3. [Q99NF3-1]
DR AlphaFoldDB; Q99NF3; -.
DR SMR; Q99NF3; -.
DR STRING; 10090.ENSMUSP00000031810; -.
DR iPTMnet; Q99NF3; -.
DR PhosphoSitePlus; Q99NF3; -.
DR EPD; Q99NF3; -.
DR MaxQB; Q99NF3; -.
DR PaxDb; Q99NF3; -.
DR PRIDE; Q99NF3; -.
DR ProteomicsDB; 279999; -. [Q99NF3-1]
DR ProteomicsDB; 280000; -. [Q99NF3-2]
DR Antibodypedia; 32076; 80 antibodies from 22 providers.
DR Ensembl; ENSMUST00000031810; ENSMUSP00000031810; ENSMUSG00000029790. [Q99NF3-1]
DR Ensembl; ENSMUST00000115130; ENSMUSP00000110783; ENSMUSG00000029790. [Q99NF3-2]
DR GeneID; 83922; -.
DR KEGG; mmu:83922; -.
DR UCSC; uc009bfr.2; mouse. [Q99NF3-1]
DR CTD; 95681; -.
DR MGI; MGI:1891414; Cep41.
DR VEuPathDB; HostDB:ENSMUSG00000029790; -.
DR eggNOG; ENOG502QR8A; Eukaryota.
DR GeneTree; ENSGT00390000002222; -.
DR HOGENOM; CLU_3241979_0_0_1; -.
DR InParanoid; Q99NF3; -.
DR OMA; DRCHIIS; -.
DR OrthoDB; 1216222at2759; -.
DR PhylomeDB; Q99NF3; -.
DR TreeFam; TF324682; -.
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-8854518; AURKA Activation by TPX2.
DR BioGRID-ORCS; 83922; 0 hits in 57 CRISPR screens.
DR ChiTaRS; Cep41; mouse.
DR PRO; PR:Q99NF3; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q99NF3; protein.
DR Bgee; ENSMUSG00000029790; Expressed in vestibular epithelium and 190 other tissues.
DR ExpressionAtlas; Q99NF3; baseline and differential.
DR Genevisible; Q99NF3; MM.
DR GO; GO:0005814; C:centriole; IDA:UniProtKB.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0036064; C:ciliary basal body; IDA:UniProtKB.
DR GO; GO:0005929; C:cilium; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0060271; P:cilium assembly; IMP:UniProtKB.
DR GO; GO:0018095; P:protein polyglutamylation; ISS:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 3.40.250.10; -; 1.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR036873; Rhodanese-like_dom_sf.
DR Pfam; PF00581; Rhodanese; 1.
DR SMART; SM00450; RHOD; 1.
DR SUPFAM; SSF52821; SSF52821; 1.
DR PROSITE; PS50206; RHODANESE_3; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell projection; Ciliopathy; Cilium;
KW Cilium biogenesis/degradation; Cytoplasm; Cytoskeleton; Methylation;
KW Phosphoprotein; Protein transport; Reference proteome; Transport.
FT CHAIN 1..373
FT /note="Centrosomal protein of 41 kDa"
FT /id="PRO_0000089490"
FT DOMAIN 169..266
FT /note="Rhodanese"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT REGION 91..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 317..373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..137
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..336
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..365
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 96
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 99
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 109
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 114
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 121
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 343
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT VAR_SEQ 33..43
FT /note="GNSMTKYIEKL -> ACASQLRVFGI (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_012249"
FT VAR_SEQ 44..373
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_012250"
SQ SEQUENCE 373 AA; 41442 MW; FA86F1DEA76999B4 CRC64;
MSARRHIGNP EYLTRRIPQN PRYQHVKSRL DTGNSMTKYI EKLEEIKKNY RYKKDELFKR
LKVTTFAQLV IQVASLSDQT LEVTAEEIQR LEDNDSATSE ADAEIAAKTN GKGSPEEQSP
SPVQFINSTG AGDSSRSTLQ SVISGVGELD VDKGLVKKEE PNGKDKPYPD CPFLLLDVRD
RDSYQQCHIV GAYSYPIATL SRTMNPYSND ILEYKNAHGK IIILYDEDER LASQAATTMC
ERGFENLFML SGGLKVLAQK FPEGLVTGSL PASCQQALPF GSVRKRRGPK MPALPAENKW
RFTPEDLKKI ECYLEEDQGP ADNPSRLNQN NSAGKDSKVA ACRGGQNLPT SCPASHSSPR
TLTSGHLQGK PWK
