APC5_DICDI
ID APC5_DICDI Reviewed; 1017 AA.
AC Q54VV5;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 108.
DE RecName: Full=Anaphase-promoting complex subunit 5;
DE Short=APC5;
GN Name=anapc5; Synonyms=apc5; ORFNames=DDB_G0280113;
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 APC5 family. {ECO:0000305}.
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DR EMBL; AAFI02000035; EAL67283.1; -; Genomic_DNA.
DR RefSeq; XP_641250.1; XM_636158.1.
DR AlphaFoldDB; Q54VV5; -.
DR SMR; Q54VV5; -.
DR STRING; 44689.DDB0234269; -.
DR PaxDb; Q54VV5; -.
DR EnsemblProtists; EAL67283; EAL67283; DDB_G0280113.
DR GeneID; 8622382; -.
DR KEGG; ddi:DDB_G0280113; -.
DR dictyBase; DDB_G0280113; anapc5.
DR eggNOG; KOG4322; Eukaryota.
DR HOGENOM; CLU_296727_0_0_1; -.
DR InParanoid; Q54VV5; -.
DR OMA; PHKITIC; -.
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:Q54VV5; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0005680; C:anaphase-promoting complex; ISS:dictyBase.
DR GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0045842; P:positive regulation of mitotic metaphase/anaphase transition; IBA:GO_Central.
DR GO; GO:0070979; P:protein K11-linked ubiquitination; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IC:dictyBase.
DR InterPro; IPR037679; Apc5.
DR InterPro; IPR026000; Apc5_dom.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR12830; PTHR12830; 1.
DR Pfam; PF12862; ANAPC5; 1.
DR Pfam; PF13181; TPR_8; 1.
PE 3: Inferred from homology;
KW Cell cycle; Cell division; Mitosis; Nucleus; Reference proteome; Repeat;
KW TPR repeat; Ubl conjugation pathway.
FT CHAIN 1..1017
FT /note="Anaphase-promoting complex subunit 5"
FT /id="PRO_0000328278"
FT REPEAT 30..63
FT /note="TPR 1"
FT REPEAT 182..214
FT /note="TPR 2"
FT REPEAT 252..286
FT /note="TPR 3"
FT REPEAT 337..370
FT /note="TPR 4"
FT REPEAT 508..541
FT /note="TPR 5"
FT REPEAT 642..675
FT /note="TPR 6"
FT REPEAT 756..790
FT /note="TPR 7"
FT REPEAT 838..871
FT /note="TPR 8"
FT REPEAT 876..908
FT /note="TPR 9"
FT REPEAT 931..964
FT /note="TPR 10"
FT REGION 451..527
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 617..636
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1017 AA; 117792 MW; 5558242D1F6BF2A6 CRC64;
MDKYRLTPHK ITICVLVEYY LNGTIKYHQK QSLSHLLIRH IKENNYQDTV KEVSLYDFIE
KELKYVLPIQ FINNEFLRMI QFDSVDDIYQ FMSSLKELFN GSNDHESINS KQMQLLDSKS
ILGIFIKKVI LNFNQILFDG LIKLYDQLDQ YLNDFYNEIN KIQQQQQQQQ QKEHCENDNS
IDMSMDQEQQ QQQQEDYNEI SNYENKIKFL SPLDEERFIY EETIRINSLI GIETPLEIEN
QVNRLKASLP NVKRVHLISL LFNIGYQDYD QSLEDLHRYF DYVNGQMTSS QWSSSASSFL
FTPNDNYQSG NSNSSNYYYN NYNFIGGSGD TTNLMLPYAV LNLVRLHYHF GHYEESYLAL
REAIRIAQER ADHSCLALAD HWLARLLKKS VYNSMESSNL LQYLLASHSD SEILKKSIER
SRDLEMPDLL ALNHTAFSKY KLENGEFSTN INSNNYNSNN NNNNNNSNTN NNTNNNNNTN
NANNNNNNNN NNTNNTNNNN NNNNNNNNNN NNNNNNNNSS NSNNNGGVNM FGKSFHLWND
IFQPIEISRL LDKSSSTAMI AHHLYSSSWE LLGNNDLAQF FTELAMKSYH SNDLSLQHDP
LRAVSSQNTI IYNIGTNNNN NNNNNNNQIK QQQQQNQQPP DLLSFCKLAL LYSKKSKYNE
AIQILIKCFS IYKTQHLCGN LLTFTVLSIL FDHLMINIDN NNNNNNNNNN NNNNNNNNNN
NDNELLISIV IESLINITNR FQSEDSVDGS GWSQIVICYQ KIIKYYCNVR GMYEKSMNLI
VKGIQISRDF GLDSQITHFY SLLSKIYEKS SPYRFSGLSD TLSALSLSNS YHLANSIADS
NIALIKIHLS TDRLDKAITL IKETLPMVLS DKLLNSQLYL LWAKSLISTS TKQSIDYLNR
SEQLFLQLFS NQSNNNNNNN NNNNNNNELL KEIYYLKSII YNDLGDIENR NLYAKKFKSI
LVPSSSIQQQ QQQQQQQQQQ QQQQQQQQQQ SNQSPVINSV QPTPKICLVP PILMKIR
