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CEP41_RAT
ID   CEP41_RAT               Reviewed;         339 AA.
AC   Q4KM37; F1LXL2;
DT   21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 102.
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   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
RX   PubMed=15057822; DOI=10.1038/nature02426;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Spleen;
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-62; SER-65; SER-80 AND
RP   SER-87, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
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 (By
CC       similarity). {ECO:0000250}.
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:0000250}. Cytoplasm, cytoskeleton, cilium basal body
CC       {ECO:0000250}. Note=Localizes mainly to the cilium basal body and in
CC       primary cilia. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the CEP41 family. {ECO:0000305}.
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DR   EMBL; BC098832; AAH98832.1; -; mRNA.
DR   RefSeq; NP_001020941.1; NM_001025770.2.
DR   AlphaFoldDB; Q4KM37; -.
DR   SMR; Q4KM37; -.
DR   STRING; 10116.ENSRNOP00000014621; -.
DR   iPTMnet; Q4KM37; -.
DR   PhosphoSitePlus; Q4KM37; -.
DR   PaxDb; Q4KM37; -.
DR   PRIDE; Q4KM37; -.
DR   Ensembl; ENSRNOT00000014621; ENSRNOP00000014621; ENSRNOG00000010950.
DR   GeneID; 500069; -.
DR   KEGG; rno:500069; -.
DR   UCSC; RGD:1562034; rat.
DR   CTD; 95681; -.
DR   RGD; 1562034; Cep41.
DR   eggNOG; ENOG502QR8A; Eukaryota.
DR   GeneTree; ENSGT00390000002222; -.
DR   InParanoid; Q4KM37; -.
DR   PhylomeDB; Q4KM37; -.
DR   Reactome; R-RNO-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR   Reactome; R-RNO-380259; Loss of Nlp from mitotic centrosomes.
DR   Reactome; R-RNO-380270; Recruitment of mitotic centrosome proteins and complexes.
DR   Reactome; R-RNO-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR   Reactome; R-RNO-380320; Recruitment of NuMA to mitotic centrosomes.
DR   Reactome; R-RNO-5620912; Anchoring of the basal body to the plasma membrane.
DR   Reactome; R-RNO-8854518; AURKA Activation by TPX2.
DR   PRO; PR:Q4KM37; -.
DR   Proteomes; UP000002494; Chromosome 4.
DR   Bgee; ENSRNOG00000010950; Expressed in testis and 19 other tissues.
DR   ExpressionAtlas; Q4KM37; baseline and differential.
DR   Genevisible; Q4KM37; RN.
DR   GO; GO:0005814; C:centriole; ISS:UniProtKB.
DR   GO; GO:0005813; C:centrosome; ISO:RGD.
DR   GO; GO:0036064; C:ciliary basal body; ISS:UniProtKB.
DR   GO; GO:0005929; C:cilium; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0060271; P:cilium assembly; ISS: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   Cell projection; Ciliopathy; Cilium; Cilium biogenesis/degradation;
KW   Cytoplasm; Cytoskeleton; Methylation; Phosphoprotein; Protein transport;
KW   Reference proteome; Transport.
FT   CHAIN           1..339
FT                   /note="Centrosomal protein of 41 kDa"
FT                   /id="PRO_0000416265"
FT   DOMAIN          135..232
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT   REGION          56..99
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          283..339
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        78..99
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        287..301
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        314..332
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         62
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         65
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         75
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99NF3"
FT   MOD_RES         80
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         87
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         309
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99NF3"
SQ   SEQUENCE   339 AA;  36992 MW;  713A55C40774BB14 CRC64;
     MSDSPIDGSP QPEPDYRYKK DELFKRIKVT TFAQLVIQVA SLSDQTLEVT AEEIQRLEDS
     DSATSEADTD IAAKTNGKGS PEEQSPSPVQ FINSTGAGDA SRSTLQSVIS GVGELDVDKG
     LVKKEEPSGK DKPYPDCPFL LLDVRDRDSY QQCHIVGAYS YPIATLSRTM NPYSNDILEY
     KNAHGKIIIL YDDDERLASQ AATTMCERGF ENLFMLSGGL KVLAQKFPEG LVTGSLPASC
     QQALPFGSVR KRPGPKMPAL PAENKWRFTP EDLKKIECYL EADQGPANNP SRLNQNNSAG
     RDLKVPAGRG GQNLPTGCPT SHSNSRTLNS GHLQGKPWK
 
 
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