CDC16_MOUSE
ID CDC16_MOUSE Reviewed; 620 AA.
AC Q8R349; Q9CYX9;
DT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Cell division cycle protein 16 homolog;
DE AltName: Full=Anaphase-promoting complex subunit 6;
DE Short=APC6;
DE AltName: Full=Cyclosome subunit 6;
GN Name=Cdc16; Synonyms=Anapc6;
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].
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 325-620.
RC STRAIN=C57BL/6J; TISSUE=Embryo;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-560, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Component of the anaphase promoting complex/cyclosome
CC (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls
CC progression through mitosis and the G1 phase of the cell cycle. The
CC APC/C complex acts by mediating ubiquitination and subsequent
CC degradation of target proteins: it mainly mediates the formation of
CC 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the
CC formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains (By
CC similarity). {ECO:0000250}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: V-shaped homodimer. The mammalian APC/C is composed at least
CC of 14 distinct subunits ANAPC1, ANAPC2, CDC27/APC3, ANAPC4, ANAPC5,
CC CDC16/APC6, ANAPC7, CDC23/APC8, ANAPC10, ANAPC11, CDC26/APC12, ANAPC13,
CC ANAPC15 and ANAPC16 that assemble into a complex of at least 19 chains
CC with a combined molecular mass of around 1.2 MDa; APC/C interacts with
CC FZR1 and FBXO5. Interacts with PPP5C and CDC20. Interacts with CDC26.
CC {ECO:0000250|UniProtKB:Q13042}.
CC -!- DOMAIN: TPR repeats 1-7 mediate homodimerization, while the C-terminal
CC TPR repeats bind to CDC26, burying its hydrophobic N-terminus.
CC {ECO:0000250|UniProtKB:Q13042}.
CC -!- PTM: Phosphorylated. Phosphorylation on Ser-560 occurs specifically
CC during mitosis (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the APC6/CDC16 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB28717.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; BC026606; AAH26606.1; -; mRNA.
DR EMBL; AK013213; BAB28717.1; ALT_SEQ; mRNA.
DR CCDS; CCDS22114.1; -.
DR RefSeq; NP_081552.2; NM_027276.2.
DR AlphaFoldDB; Q8R349; -.
DR SMR; Q8R349; -.
DR BioGRID; 213776; 53.
DR CORUM; Q8R349; -.
DR IntAct; Q8R349; 49.
DR STRING; 10090.ENSMUSP00000047950; -.
DR iPTMnet; Q8R349; -.
DR PhosphoSitePlus; Q8R349; -.
DR EPD; Q8R349; -.
DR jPOST; Q8R349; -.
DR MaxQB; Q8R349; -.
DR PaxDb; Q8R349; -.
DR PRIDE; Q8R349; -.
DR ProteomicsDB; 283763; -.
DR Antibodypedia; 11890; 431 antibodies from 40 providers.
DR DNASU; 69957; -.
DR Ensembl; ENSMUST00000043962; ENSMUSP00000047950; ENSMUSG00000038416.
DR GeneID; 69957; -.
DR KEGG; mmu:69957; -.
DR UCSC; uc009kyi.1; mouse.
DR CTD; 8881; -.
DR MGI; MGI:1917207; Cdc16.
DR VEuPathDB; HostDB:ENSMUSG00000038416; -.
DR eggNOG; KOG1173; Eukaryota.
DR GeneTree; ENSGT00950000182950; -.
DR HOGENOM; CLU_011751_3_2_1; -.
DR InParanoid; Q8R349; -.
DR OMA; DPFHNNA; -.
DR OrthoDB; 905026at2759; -.
DR PhylomeDB; Q8R349; -.
DR TreeFam; TF101054; -.
DR Reactome; R-MMU-141430; Inactivation of APC/C via direct inhibition of the APC/C complex.
DR Reactome; R-MMU-174048; APC/C:Cdc20 mediated degradation of Cyclin B.
DR Reactome; R-MMU-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
DR Reactome; R-MMU-174154; APC/C:Cdc20 mediated degradation of Securin.
DR Reactome; R-MMU-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR Reactome; R-MMU-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; R-MMU-176407; Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
DR Reactome; R-MMU-176408; Regulation of APC/C activators between G1/S and early anaphase.
DR Reactome; R-MMU-176409; APC/C:Cdc20 mediated degradation of mitotic proteins.
DR Reactome; R-MMU-176412; Phosphorylation of the APC/C.
DR Reactome; R-MMU-179409; APC-Cdc20 mediated degradation of Nek2A.
DR Reactome; R-MMU-2467813; Separation of Sister Chromatids.
DR Reactome; R-MMU-2559582; Senescence-Associated Secretory Phenotype (SASP).
DR Reactome; R-MMU-68867; Assembly of the pre-replicative complex.
DR Reactome; R-MMU-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 69957; 29 hits in 74 CRISPR screens.
DR ChiTaRS; Cdc16; mouse.
DR PRO; PR:Q8R349; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q8R349; protein.
DR Bgee; ENSMUSG00000038416; Expressed in floor plate of midbrain and 271 other tissues.
DR ExpressionAtlas; Q8R349; baseline and differential.
DR Genevisible; Q8R349; MM.
DR GO; GO:0005680; C:anaphase-promoting complex; ISS:UniProtKB.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0072686; C:mitotic spindle; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IBA:GO_Central.
DR GO; GO:0007091; P:metaphase/anaphase transition of mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0045842; P:positive regulation of mitotic metaphase/anaphase transition; IBA:GO_Central.
DR GO; GO:0070979; P:protein K11-linked ubiquitination; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR SMART; SM00028; TPR; 6.
DR SUPFAM; SSF48452; SSF48452; 2.
DR PROSITE; PS50005; TPR; 5.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Mitosis; Phosphoprotein; Reference proteome;
KW Repeat; TPR repeat; Ubl conjugation pathway.
FT CHAIN 1..620
FT /note="Cell division cycle protein 16 homolog"
FT /id="PRO_0000106268"
FT REPEAT 4..33
FT /note="TPR 1"
FT REPEAT 37..62
FT /note="TPR 2"
FT REPEAT 70..93
FT /note="TPR 3"
FT REPEAT 128..159
FT /note="TPR 4"
FT REPEAT 164..187
FT /note="TPR 5"
FT REPEAT 198..222
FT /note="TPR 6"
FT REPEAT 232..260
FT /note="TPR 7"
FT REPEAT 267..294
FT /note="TPR 8"
FT REPEAT 299..329
FT /note="TPR 9"
FT REPEAT 334..362
FT /note="TPR 10"
FT REPEAT 369..397
FT /note="TPR 11"
FT REPEAT 402..434
FT /note="TPR 12"
FT REPEAT 442..474
FT /note="TPR 13"
FT REPEAT 479..508
FT /note="TPR 14"
FT REGION 577..596
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 578..593
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 490
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13042"
FT MOD_RES 560
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 599
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q13042"
SQ SEQUENCE 620 AA; 71460 MW; A0E47748506CC14E CRC64;
MNLEPLRKRV RQYLDQQQYQ SALFWADKVA SLSHEEPQDV YWLAQCLYLT AQYHRAAHAL
RSRKLDKLYE ACRYLAARCH YAAKEHQQAL DILDMEEPIN RRLFEKYLKD DNGSRDPSSD
WEMSQSSIKS SICLLRGKIY DALDNRTLAT YSYKEALKLD VYCFEAFDLL TSHHMLTAQE
EKELLDSLPL NKLCAEEQEL LRFVFENKLK KYNKPSETVI PESVDGLQEN LDVVVSLAER
HYYNCDFKMC YKLTSTVMEK DPFHANCLPV HIGTLVELNK ANELFYLSHK LVDLYPSNPV
SWFAVGCYYL MVGHKNEHAR RYLSKATTLE KTYGPAWIAY GHSFAVESEH DQAMAAYFTA
AQLMKGCHLP MLYIGLEYGL TNNSKLAERF FGQALSIAPE DPFVIHEVGV VAFQNGEWKT
AEKWFLDALE KIKAIGNEVT VDKWEPLLNN LGHVCRKLKK YAEALDYHRQ ALVLIPQNAS
TYSAIGYIHS LMGNFENAVD YFHTALGLRR DDTFSVTMLG HCIEMYIGDS EAYIGADIKD
KLKCYDFDVH TMKTLKNIIS PPWDFRDFEV EKQNTEEAGL APLQNSTKAP ESRPNLEETF
EIEMNESDMM LETSMSDHST
