ID   CEP44_BOVIN             Reviewed;         385 AA.
AC   Q08DB0;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   25-MAY-2022, entry version 59.
DE   RecName: Full=Centrosomal protein of 44 kDa;
DE            Short=Cep44;
GN   Name=CEP44;
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 MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal skin;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Centriole-enriched microtubule-binding protein involved in
CC       centriole biogenesis. In collaboration with CEP295 and POC1B, is
CC       required for the centriole-to-centrosome conversion by ensuring the
CC       formation of bona fide centriole wall. Functions as a linker component
CC       that maintains centrosome cohesion. Associates with CROCC and regulates
CC       its stability and localization to the centrosome.
CC       {ECO:0000250|UniProtKB:Q9C0F1}.
CC   -!- SUBUNIT: Interacts with CROCC. Interacts with POC1B; the interaction is
CC       direct and recruits POC1B to centriolar microtubules. Binds to
CC       centriolar microtubules. {ECO:0000250|UniProtKB:Q9C0F1}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC       center, centrosome {ECO:0000250|UniProtKB:Q9C0F1}. Cytoplasm,
CC       cytoskeleton, microtubule organizing center, centrosome, centriole
CC       {ECO:0000250|UniProtKB:Q9C0F1}. Cytoplasm, cytoskeleton, spindle pole
CC       {ECO:0000250|UniProtKB:Q9C0F1}. Midbody {ECO:0000250|UniProtKB:Q9C0F1}.
CC       Note=Localizes to the proximal end of mother and daughter centrioles.
CC       {ECO:0000250|UniProtKB:Q9C0F1}.
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DR   EMBL; BC123850; AAI23851.1; -; mRNA.
DR   RefSeq; NP_001070301.1; NM_001076833.1.
DR   AlphaFoldDB; Q08DB0; -.
DR   SMR; Q08DB0; -.
DR   STRING; 9913.ENSBTAP00000026720; -.
DR   PaxDb; Q08DB0; -.
DR   GeneID; 510950; -.
DR   KEGG; bta:510950; -.
DR   CTD; 80817; -.
DR   eggNOG; ENOG502R3RQ; Eukaryota.
DR   InParanoid; Q08DB0; -.
DR   OrthoDB; 1589624at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005814; C:centriole; ISS:UniProtKB.
DR   GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
DR   GO; GO:0000922; C:spindle pole; ISS:UniProtKB.
DR   GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
DR   GO; GO:0007099; P:centriole replication; ISS:UniProtKB.
DR   GO; GO:0010457; P:centriole-centriole cohesion; ISS:UniProtKB.
DR   GO; GO:0007098; P:centrosome cycle; ISS:UniProtKB.
DR   InterPro; IPR033603; CEP44.
DR   InterPro; IPR029157; CEP44_CC.
DR   PANTHER; PTHR31477; PTHR31477; 2.
DR   Pfam; PF15007; CEP44; 1.
PE   2: Evidence at transcript level;
KW   Coiled coil; Cytoplasm; Cytoskeleton; Phosphoprotein; Reference proteome.
FT   CHAIN           1..385
FT                   /note="Centrosomal protein of 44 kDa"
FT                   /id="PRO_0000293721"
FT   REGION          11..192
FT                   /note="Binds with microtubules and centrioles"
FT                   /evidence="ECO:0000250|UniProtKB:Q9C0F1"
FT   REGION          126..154
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          303..348
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          230..271
FT                   /evidence="ECO:0000255"
FT   COILED          358..381
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        130..154
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        330..348
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         342
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9C0F1"
FT   MOD_RES         343
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9C0F1"
SQ   SEQUENCE   385 AA;  43580 MW;  2F59B1A897486424 CRC64;
     MATGDLKRSL RNLEQVLRSL NYPREVDCVG LVKGDTAASL PIISYSLTSY SPYVAELLVD
     SNIELLAKND LRFIDTVYKL LRDQFNYKPI LTKKQFIQCG FAEWKIQIIC DILNCVMKKH
     KELSSLEKTP SQQRKKTSSA KSEPCSSTEK TSTEPVGIDV TGRFVTSGKK KAVVIRHLYN
     EDGANIPEDT VTDVNEAFDV CDIKAAEITI PELQVPDINC EQEDITVNPE VTALQSMLAE
     CQEKLKKLTC IESRLESLEE KMKGKVLVNE KTWANLLSRV TLLETEMLLS KKNDEYMQFN
     EMSEDYSSSS DMDSLNPDRK SKEERHANIP LSSGYSTVSS DSTPRTSTVN YCGLKEISEE
     TTMQKMERMK KMFEETAELL KCPNH