ID   DEUP1_MACFA             Reviewed;         603 AA.
AC   Q95JK1;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 2.
DT   25-MAY-2022, entry version 56.
DE   RecName: Full=Deuterosome assembly protein 1 {ECO:0000250|UniProtKB:Q05D60};
DE   AltName: Full=Coiled-coil domain-containing protein 67;
GN   Name=DEUP1 {ECO:0000250|UniProtKB:Q05D60}; Synonyms=CCDC67;
GN   ORFNames=QtsA-16541;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RX   PubMed=12498619; DOI=10.1186/1471-2164-3-36;
RA   Osada N., Hida M., Kusuda J., Tanuma R., Hirata M., Suto Y., Hirai M.,
RA   Terao K., Sugano S., Hashimoto K.;
RT   "Cynomolgus monkey testicular cDNAs for discovery of novel human genes in
RT   the human genome sequence.";
RL   BMC Genomics 3:36-36(2002).
CC   -!- FUNCTION: Key structural component of the deuterosome, a structure that
CC       promotes de novo centriole amplification in multiciliated cells.
CC       Deuterosome-mediated centriole amplification occurs in terminally
CC       differentiated multiciliated cells and can generate more than 100
CC       centrioles. Probably sufficient for the specification and formation of
CC       the deuterosome inner core. Interacts with CEP152 and recruits PLK4 to
CC       activate centriole biogenesis (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with CEP152; the interaction is mutually exclusive
CC       with CEP63. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Localizes to the
CC       deuterosome. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the CEP63 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB63125.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence. The C-terminus was extended based on orthologous sequences.; Evidence={ECO:0000305};
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DR   EMBL; AB070180; BAB63125.1; ALT_SEQ; mRNA.
DR   RefSeq; XP_005579406.1; XM_005579349.2.
DR   RefSeq; XP_015291090.1; XM_015435604.1.
DR   AlphaFoldDB; Q95JK1; -.
DR   SMR; Q95JK1; -.
DR   STRING; 9541.XP_005579405.1; -.
DR   GeneID; 102122333; -.
DR   KEGG; mcf:102122333; -.
DR   CTD; 159989; -.
DR   VEuPathDB; HostDB:ENSMFAG00000032572; -.
DR   eggNOG; ENOG502QRBJ; Eukaryota.
DR   Proteomes; UP000233100; Chromosome 14.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0098536; C:deuterosome; ISS:UniProtKB.
DR   GO; GO:0030030; P:cell projection organization; IEA:UniProtKB-KW.
DR   GO; GO:0098535; P:de novo centriole assembly involved in multi-ciliated epithelial cell differentiation; ISS:UniProtKB.
DR   GO; GO:1903251; P:multi-ciliated epithelial cell differentiation; ISS:UniProtKB.
DR   InterPro; IPR031470; Cep63/Deup1_N.
DR   InterPro; IPR029611; Deup1.
DR   PANTHER; PTHR18875:SF5; PTHR18875:SF5; 1.
DR   Pfam; PF17045; CEP63; 1.
PE   2: Evidence at transcript level;
KW   Cilium biogenesis/degradation; Coiled coil; Cytoplasm; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..603
FT                   /note="Deuterosome assembly protein 1"
FT                   /id="PRO_0000297830"
FT   COILED          14..59
FT                   /evidence="ECO:0000255"
FT   COILED          85..197
FT                   /evidence="ECO:0000255"
FT   COILED          227..278
FT                   /evidence="ECO:0000255"
FT   COILED          336..399
FT                   /evidence="ECO:0000255"
FT   COILED          454..480
FT                   /evidence="ECO:0000255"
FT   COILED          557..600
FT                   /evidence="ECO:0000255"
FT   MOD_RES         546
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5U3Z6"
SQ   SEQUENCE   603 AA;  70882 MW;  F49F28ACE9E3CB05 CRC64;
     MENQAHNTMG TSPCEAELQE LMEQIDIMVS NKKMDWERKM RALETRLDLR DQELANAQTC
     LDQKGQEVGL LRQKLDSLEK CNLAMTQNYE GQLQSLKAQF SKLTNSFEKL RLHQMKQNKV
     PRKELPHLKE ELPFELSNLN QKLEEFRAKS REWDKQEILY QTHLISLDAQ QKLLSEKCNQ
     FQKQAQSYQT QLNGKKQCLE DSSSEIPRLI CDPDPNCEIG ERDEFIIEKL KSAVSEIALS
     RNKLQDENQK LLQELKMYQR QCQAMEAGLS EVKSELQSRD DLLRIIEMER LQLHRELLKI
     GECQNAQGNK KRLESSHLPS IKEPERKRKE LFSVMQDQPN HEKELNKIRS QLQQEEEYHN
     SEQERMRNEI SDLTEELHQK EITIATVTKK AALLEKQLKM ELEIKEKMLA KEQVSDMKYK
     AVRTENTHLK GMMGDLDPGR YMSMDFTNRE HSRHTSINKL EYENERLRND LAKLRVNGKS
     TRTNQNTYEE TGRYAYQSQI KVEKNEERLS HDCEPNRSTS PLPPLTFQTK EMTSPLVSDD
     DVFPLSPPDM SFPASLAAQH FLLEEEKRAK ELEKLLNTHI DELQRHTEFT LNKYSKLKQN
     RHI