ID   CEP41_BOVIN             Reviewed;         373 AA.
AC   F1MUG2;
DT   21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT   16-NOV-2011, sequence version 2.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=Centrosomal protein of 41 kDa;
DE            Short=Cep41;
GN   Name=CEP41;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hereford;
RX   PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA   Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D.,
RA   Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G.,
RA   Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT   "A whole-genome assembly of the domestic cow, Bos taurus.";
RL   Genome Biol. 10:R42.01-R42.10(2009).
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; DAAA02011518; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; DAAA02011519; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; NP_001179050.1; NM_001192121.1.
DR   AlphaFoldDB; F1MUG2; -.
DR   SMR; F1MUG2; -.
DR   STRING; 9913.ENSBTAP00000009747; -.
DR   PaxDb; F1MUG2; -.
DR   PRIDE; F1MUG2; -.
DR   Ensembl; ENSBTAT00000009747; ENSBTAP00000009747; ENSBTAG00000007413.
DR   GeneID; 506914; -.
DR   KEGG; bta:506914; -.
DR   CTD; 95681; -.
DR   VEuPathDB; HostDB:ENSBTAG00000007413; -.
DR   VGNC; VGNC:27204; CEP41.
DR   eggNOG; ENOG502QR8A; Eukaryota.
DR   GeneTree; ENSGT00390000002222; -.
DR   HOGENOM; CLU_064316_0_0_1; -.
DR   InParanoid; F1MUG2; -.
DR   OMA; DRCHIIS; -.
DR   OrthoDB; 1216222at2759; -.
DR   TreeFam; TF324682; -.
DR   Proteomes; UP000009136; Chromosome 4.
DR   Bgee; ENSBTAG00000007413; Expressed in spermatid and 107 other tissues.
DR   GO; GO:0005814; C:centriole; ISS:UniProtKB.
DR   GO; GO:0005813; C:centrosome; IEA:Ensembl.
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   3: Inferred from homology;
KW   Cell projection; Ciliopathy; Cilium; Cilium biogenesis/degradation;
KW   Cytoplasm; Cytoskeleton; Methylation; Phosphoprotein; Protein transport;
KW   Reference proteome; Transport.
FT   CHAIN           1..373
FT                   /note="Centrosomal protein of 41 kDa"
FT                   /id="PRO_0000416264"
FT   DOMAIN          169..266
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT   REGION          89..127
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          275..300
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          315..373
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        100..127
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        348..364
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         96
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99NF3"
FT   MOD_RES         99
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99NF3"
FT   MOD_RES         109
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99NF3"
FT   MOD_RES         114
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99NF3"
FT   MOD_RES         121
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99NF3"
FT   MOD_RES         343
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99NF3"
SQ   SEQUENCE   373 AA;  41380 MW;  CA68B780BE736851 CRC64;
     MSVRRHIGNP EYLTRRIPQN PRYQHVKSRL DTGNSMTKYI EKLEEIKKNY RYKKDELFKR
     LKVTTFAQLV IQVASLSDQT LEVTAEEIQR LEDNDSATSE PDAEITAKTN GNGSPGEQSP
     SPVQFINSEG AGDFSRSTLQ SVISGVGELD LDKGLVKKTE PNTKDKPYPD CPFLLLDVRD
     RDSYQQCHIV GAYSYPIATL SRTMNPYSND ILEYKNAHGK IIILYDDDER LASQAATTMC
     ERGFENLFML SGGLKVLAQK FPEGLITGSL PASCQQALPP GSARKRSSPK VPPLPAENKW
     RFTPEDLKKI EYYLEEDQGP ADNPSRLSQA NASGRDAKVP GTRSGQNLPA GGPASHQNPR
     SLGSGHLQGK PWK