CATAC_MOUSE
ID CATAC_MOUSE Reviewed; 332 AA.
AC Q4VA36; Q3TAL6; Q7TNQ4; Q8C702;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Centrosomal AT-AC splicing factor {ECO:0000305};
DE AltName: Full=Coiled-coil domain-containing protein 84;
GN Name=Cenatac; Synonyms=Ccdc84;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Kidney, and Spleen;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=FVB/N; TISSUE=Colon, and Mammary gland;
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).
CC -!- FUNCTION: Negative regulator of centrosome duplication. Constrains
CC centriole number by modulating the degradation of the centrosome-
CC duplication-associated protein SASS6 in an acetylation-dependent
CC manner. SIRT1 deacetylates CENATAC in G1 phase, allowing for SASS6
CC accumulation on the centrosome and subsequent procentriole assembly.
CC The CENATAC acetylation level is restored in mitosis by NAT10,
CC promoting SASS6 proteasome degradation by facilitating SASS6 binding to
CC APC/C E3 ubiquitin-protein ligase complex/FZR1.
CC {ECO:0000250|UniProtKB:Q86UT8}.
CC -!- SUBUNIT: Interacts with SASS6; the interaction increases with CENATAC
CC acetylation. {ECO:0000250|UniProtKB:Q86UT8}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q4VA36-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q4VA36-2; Sequence=VSP_022266, VSP_022267;
CC Name=3;
CC IsoId=Q4VA36-3; Sequence=VSP_022268, VSP_022269;
CC -!- PTM: Acetylated. Acetylation oscillates throughout the cell cycle, and
CC the acetylation state at Lys-31 is regulated by the deacetylase SIRT1
CC and the acetyltransferase NAT10. Deacetylated CENATAC is responsible
CC for its centrosome targeting, and acetylated CENATAC promotes SASS6
CC degradation by enhancing the binding affinity of SASS6 for APC/C E3
CC ubiquitin-protein ligase complex/FZR1. {ECO:0000250|UniProtKB:Q86UT8}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH55929.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK052757; BAC35135.1; -; mRNA.
DR EMBL; AK171754; BAE42652.1; -; mRNA.
DR EMBL; BC055929; AAH55929.1; ALT_INIT; mRNA.
DR EMBL; BC096560; AAH96560.1; -; mRNA.
DR EMBL; BC116877; AAI16878.1; -; mRNA.
DR EMBL; BC116879; AAI16880.1; -; mRNA.
DR CCDS; CCDS23110.1; -. [Q4VA36-1]
DR RefSeq; NP_958760.2; NM_201372.3. [Q4VA36-1]
DR AlphaFoldDB; Q4VA36; -.
DR IntAct; Q4VA36; 1.
DR STRING; 10090.ENSMUSP00000053216; -.
DR iPTMnet; Q4VA36; -.
DR PhosphoSitePlus; Q4VA36; -.
DR EPD; Q4VA36; -.
DR MaxQB; Q4VA36; -.
DR PaxDb; Q4VA36; -.
DR PeptideAtlas; Q4VA36; -.
DR PRIDE; Q4VA36; -.
DR ProteomicsDB; 281318; -. [Q4VA36-1]
DR ProteomicsDB; 281319; -. [Q4VA36-2]
DR ProteomicsDB; 281320; -. [Q4VA36-3]
DR Antibodypedia; 54439; 87 antibodies from 17 providers.
DR Ensembl; ENSMUST00000053286; ENSMUSP00000053216; ENSMUSG00000043923. [Q4VA36-1]
DR Ensembl; ENSMUST00000213813; ENSMUSP00000148874; ENSMUSG00000043923. [Q4VA36-3]
DR Ensembl; ENSMUST00000214494; ENSMUSP00000151113; ENSMUSG00000043923. [Q4VA36-2]
DR Ensembl; ENSMUST00000214702; ENSMUSP00000151118; ENSMUSG00000043923. [Q4VA36-2]
DR Ensembl; ENSMUST00000217270; ENSMUSP00000150949; ENSMUSG00000043923. [Q4VA36-2]
DR Ensembl; ENSMUST00000217351; ENSMUSP00000149682; ENSMUSG00000043923. [Q4VA36-2]
DR GeneID; 382073; -.
DR KEGG; mmu:382073; -.
DR UCSC; uc009pdo.1; mouse. [Q4VA36-1]
DR UCSC; uc009pdq.1; mouse. [Q4VA36-3]
DR UCSC; uc012grv.1; mouse. [Q4VA36-2]
DR CTD; 382073; -.
DR MGI; MGI:2685960; Ccdc84.
DR VEuPathDB; HostDB:ENSMUSG00000043923; -.
DR eggNOG; ENOG502QS8B; Eukaryota.
DR GeneTree; ENSGT00390000007799; -.
DR HOGENOM; CLU_041370_1_0_1; -.
DR InParanoid; Q4VA36; -.
DR OMA; YFPNHKK; -.
DR OrthoDB; 1213548at2759; -.
DR PhylomeDB; Q4VA36; -.
DR TreeFam; TF324670; -.
DR BioGRID-ORCS; 382073; 24 hits in 74 CRISPR screens.
DR ChiTaRS; Ccdc84; mouse.
DR PRO; PR:Q4VA36; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q4VA36; protein.
DR Bgee; ENSMUSG00000043923; Expressed in granulocyte and 245 other tissues.
DR ExpressionAtlas; Q4VA36; baseline and differential.
DR Genevisible; Q4VA36; MM.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0010826; P:negative regulation of centrosome duplication; ISS:UniProtKB.
DR GO; GO:0042176; P:regulation of protein catabolic process; ISS:UniProtKB.
DR InterPro; IPR028015; CCDC84-like.
DR PANTHER; PTHR31198; PTHR31198; 1.
DR Pfam; PF14968; CCDC84; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Alternative splicing; Coiled coil; Reference proteome.
FT CHAIN 1..332
FT /note="Centrosomal AT-AC splicing factor"
FT /id="PRO_0000271023"
FT REGION 1..169
FT /note="Required for centrosome location"
FT /evidence="ECO:0000250|UniProtKB:Q86UT8"
FT REGION 170..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 311..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 137..168
FT /evidence="ECO:0000255"
FT COMPBIAS 185..201
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 312..326
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 31
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q86UT8"
FT VAR_SEQ 172..194
FT /note="PQAESDPEEGSSAPESWKATNGH -> VGFPRRTQRTSGRVRSRRGLFST
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_022266"
FT VAR_SEQ 172..185
FT /note="PQAESDPEEGSSAP -> VGFPRRTQRSIQIH (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_022268"
FT VAR_SEQ 186..332
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_022269"
FT VAR_SEQ 195..332
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_022267"
SQ SEQUENCE 332 AA; 37701 MW; 8E8CE080764B00A2 CRC64;
MAPPQRCPLC RQTFFCGRGH VYSHKHQRQL KGALERLLPQ VEAARRAVRA AQVERYVPEH
DRCCWCPCCG CEVRKHLSHG NLTVLHGGLL EHLASPEHKK ATNKFWWENK ANAQMKEKFL
ISPQDYARFK KSMVKGLDSY EEKEDEVIKE MAAQIREVEQ SRQEVVRSVL EPQAESDPEE
GSSAPESWKA TNGHVASSSQ QVSHLALQPV AELDWMETGQ QLTFIGHQDT PGIGNIHSGA
TPPWMIQEEE HSSGSLPIGP SYEEFLKEKE KQKLKKLPPD RVGANFDHSS NTSAGWLPSF
GRVWNNGRRW QSRHQFKTEA ATRSKQPRKG KS
