CDC16_DICDI
ID CDC16_DICDI Reviewed; 865 AA.
AC Q1ZXE6;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 1.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=Anaphase-promoting complex subunit 6;
DE Short=APC6;
DE AltName: Full=Cell division cycle protein 16 homolog;
GN Name=anapc6; Synonyms=apc6, cdc16; ORFNames=DDB_G0286233;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Component of the anaphase promoting complex/cyclosome
CC (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex
CC that controls progression through mitosis and the G1 phase of the cell
CC cycle. {ECO:0000250}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: The APC/C is composed of at least 13 subunits that stay
CC tightly associated throughout the cell cycle: anapc1, anapc2, anapc3,
CC anapc4, anapc5, anapc6, anapc7, anapc8, anapc10, anapc11, cdc20, cdc26
CC and cdh1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the APC6/CDC16 family. {ECO:0000305}.
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DR EMBL; AAFI02000085; EAS66852.1; -; Genomic_DNA.
DR RefSeq; XP_001134535.1; XM_001134535.1.
DR AlphaFoldDB; Q1ZXE6; -.
DR SMR; Q1ZXE6; -.
DR STRING; 44689.DDB0232238; -.
DR PaxDb; Q1ZXE6; -.
DR EnsemblProtists; EAS66852; EAS66852; DDB_G0286233.
DR GeneID; 8625512; -.
DR KEGG; ddi:DDB_G0286233; -.
DR dictyBase; DDB_G0286233; anapc6.
DR eggNOG; KOG1173; Eukaryota.
DR HOGENOM; CLU_011751_3_1_1; -.
DR InParanoid; Q1ZXE6; -.
DR OMA; CKIETNE; -.
DR PhylomeDB; Q1ZXE6; -.
DR Reactome; R-DDI-141430; Inactivation of APC/C via direct inhibition of the APC/C complex.
DR Reactome; R-DDI-174048; APC/C:Cdc20 mediated degradation of Cyclin B.
DR Reactome; R-DDI-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
DR Reactome; R-DDI-174154; APC/C:Cdc20 mediated degradation of Securin.
DR Reactome; R-DDI-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR Reactome; R-DDI-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; R-DDI-176407; Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
DR Reactome; R-DDI-176408; Regulation of APC/C activators between G1/S and early anaphase.
DR Reactome; R-DDI-176409; APC/C:Cdc20 mediated degradation of mitotic proteins.
DR Reactome; R-DDI-176412; Phosphorylation of the APC/C.
DR Reactome; R-DDI-179409; APC-Cdc20 mediated degradation of Nek2A.
DR Reactome; R-DDI-2467813; Separation of Sister Chromatids.
DR Reactome; R-DDI-2559582; Senescence-Associated Secretory Phenotype (SASP).
DR Reactome; R-DDI-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR Reactome; R-DDI-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q1ZXE6; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0005680; C:anaphase-promoting complex; ISS:dictyBase.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:dictyBase.
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:0016567; P:protein ubiquitination; IBA:GO_Central.
DR Gene3D; 1.25.40.10; -; 4.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF13181; TPR_8; 1.
DR SMART; SM00028; TPR; 7.
DR SUPFAM; SSF48452; SSF48452; 2.
DR PROSITE; PS50005; TPR; 5.
DR PROSITE; PS50293; TPR_REGION; 2.
PE 3: Inferred from homology;
KW Cell cycle; Cell division; Mitosis; Nucleus; Reference proteome; Repeat;
KW TPR repeat; Ubl conjugation pathway.
FT CHAIN 1..865
FT /note="Anaphase-promoting complex subunit 6"
FT /id="PRO_0000328531"
FT REPEAT 11..42
FT /note="TPR 1"
FT REPEAT 46..75
FT /note="TPR 2"
FT REPEAT 88..149
FT /note="TPR 3"
FT REPEAT 300..331
FT /note="TPR 4"
FT REPEAT 336..359
FT /note="TPR 5"
FT REPEAT 366..438
FT /note="TPR 6"
FT REPEAT 478..506
FT /note="TPR 7"
FT REPEAT 515..542
FT /note="TPR 8"
FT REPEAT 573..602
FT /note="TPR 9"
FT REPEAT 607..635
FT /note="TPR 10"
FT REPEAT 642..670
FT /note="TPR 11"
FT REPEAT 675..709
FT /note="TPR 12"
FT REPEAT 777..809
FT /note="TPR 13"
FT REPEAT 814..843
FT /note="TPR 14"
FT REGION 153..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 403..436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 738..767
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..174
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..202
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..293
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 865 AA; 99379 MW; 6C792634AF1C6451 CRC64;
MADNLYDSSI IEKQLKEKIE NALSIHSYPT AIFFSDKLLN LVTIHSKEYV KILYILCDAL
YLDRQFQRSS YLIQKYLNAI EEIDKKGEDY QYIDDIHSHH HNQQQNIFYK RIKKEKEDEQ
YTNTILKLKY LAAKCKIETN EFDQCLQILN KDNDSSENMD DENNNINNNN NKIKKENEIN
NDNCDDDDDD DDDDDDDDDD EKDSNQLLKF YTNSKSNKSK DISENNSNNE NTTKESINKN
NTDSSSIDNK NNNKNNNNNN NNNNNNNNNN NNNNNNNNNN NNNNNNNNNN NNFNKETLII
RSSISCLKGK CYESMDNLKK AKFWYIKALL TDYNCFEAFE SLTKNHLLTY QEEISLLEKL
KFSSDDSWIK EIYSLSLKKY DSPKFTFNYK YLELYDSLNH QNSNNNTFGA NNNNNNNNNN
NNNNNNNNNN NSNNDISTED LISVKTLSSS SSSPSKKQEN NNLITINEIR KKLIECNDIQ
TWISEYYFYR HQFQESYSIT KRILKQDKYY SNQICLMVNI SSMFELQLTN ELYFTCHQLV
DSFTSSLNNG SHGGSHGGGG GGSHGGSSGN GGAISWYGVA CYYHLIQNSD QTQRFFTKST
TLDSRMGASW LGFGHFFASK GEHDQAMAAY RTSSRLLTGC HLPLLCIGME LIRVHNLNLA
SQYILQAKDI CPYDPMIFNE LGIIEYKNSQ YNEAIKLFET ALEICKIKSK ASSSSSSSSN
YHNLNLSNIS FSGVGSSGIG NNNNNNNNRR TTTTTTTTSN NQKKNSSNNK TMIAYLESWE
PTIYNLAHCY RKLRKFELAL HYYTMSLSLL PNNPSTYSAL GFTHHLQGNF DEAIDYYHQS
LSIRDDTFTN VLLHKALSLS ILQYD
