DEUP1_RAT
ID DEUP1_RAT Reviewed; 601 AA.
AC Q5U3Z6;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 2.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Deuterosome assembly protein 1 {ECO:0000312|RGD:1306632};
DE AltName: Full=Coiled-coil domain-containing protein 67;
GN Name=Deup1 {ECO:0000312|RGD:1306632}; Synonyms=Ccdc67;
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 MRNA].
RC TISSUE=Testis;
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 [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-544, AND IDENTIFICATION BY
RP 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: 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 -!- CAUTION: It is uncertain whether Met-1 or Met-22 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH85333.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BC085333; AAH85333.1; ALT_INIT; mRNA.
DR RefSeq; NP_001014109.2; NM_001014087.1.
DR AlphaFoldDB; Q5U3Z6; -.
DR SMR; Q5U3Z6; -.
DR STRING; 10116.ENSRNOP00000015063; -.
DR CarbonylDB; Q5U3Z6; -.
DR iPTMnet; Q5U3Z6; -.
DR PhosphoSitePlus; Q5U3Z6; -.
DR PaxDb; Q5U3Z6; -.
DR PRIDE; Q5U3Z6; -.
DR GeneID; 315438; -.
DR KEGG; rno:315438; -.
DR UCSC; RGD:1306632; rat.
DR CTD; 159989; -.
DR RGD; 1306632; Deup1.
DR VEuPathDB; HostDB:ENSRNOG00000061247; -.
DR eggNOG; ENOG502QRBJ; Eukaryota.
DR HOGENOM; CLU_027471_1_0_1; -.
DR InParanoid; Q5U3Z6; -.
DR OMA; ARTSPCE; -.
DR OrthoDB; 943593at2759; -.
DR PhylomeDB; Q5U3Z6; -.
DR TreeFam; TF330595; -.
DR PRO; PR:Q5U3Z6; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Bgee; ENSRNOG00000061247; Expressed in testis and 5 other tissues.
DR Genevisible; Q5U3Z6; RN.
DR GO; GO:0005814; C:centriole; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0098536; C:deuterosome; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0030030; P:cell projection organization; IEA:UniProtKB-KW.
DR GO; GO:0007099; P:centriole replication; IBA:GO_Central.
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 1: Evidence at protein level;
KW Cilium biogenesis/degradation; Coiled coil; Cytoplasm; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..601
FT /note="Deuterosome assembly protein 1"
FT /id="PRO_0000297832"
FT REGION 115..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 188..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 307..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 14..59
FT /evidence="ECO:0000255"
FT COILED 86..197
FT /evidence="ECO:0000255"
FT COILED 226..278
FT /evidence="ECO:0000255"
FT COILED 340..397
FT /evidence="ECO:0000255"
FT COILED 555..586
FT /evidence="ECO:0000255"
FT COMPBIAS 115..130
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 544
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 601 AA; 70105 MW; 53E41733439FE787 CRC64;
MENQAHTTAG ASPCEAELQE LMEQIDIMVS NKKLDWERKM RALETRLDLR DQELANAQTC
LDQKGQEVGL LRQKLDSLEK CNLVMTQNYE GQLQTLKAQF SKLTNNFEKL RLHQMKQNQS
HRKEASNKDE TPFELSSLNQ KIEEFRAKSR EWDKQEILYQ THLVSLDAQQ KLLSEKCNQF
QKQAQNYQTQ LNGKQQRPED SSPETPRLVC ESSPGCEATQ RDEFIIEKLK SAVSEIALSR
NKLQDENQKL LQELKMYQRQ CQAMEAGLSE VKNELQSRDD LLRIIEMERL HLHRELLKMG
ELQTVQDNRK RVESSYSPST KEPERKRKEL FSVVSDQPNH EKELNKMRSQ LYQEEDLCSE
QERMRNEISE LTQELHQKEV TIATIMKKAA LLERQLKIEL EIKEKMLAKQ QISDRRYKAV
RTENTHLKGM MGDLDPARYL TVDFSNKEHS RHTSINKLEY ENERLRSDLA KLHINGKAAW
SNQSSYEGAG AYIYQSQLKT ETGGDRISED CEMNRSPTPL SPLPFQTKEM TSPLAGDNEV
LPLSPPDISF RASLAAQHFL MEEEKRAKEL EKLLNTHIDE LQRHTEFTLN KYTKLKQSRH
I
