APC3_DICDI
ID APC3_DICDI Reviewed; 970 AA.
AC Q54J83;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 103.
DE RecName: Full=Anaphase-promoting complex subunit 3;
DE Short=APC3;
GN Name=anapc3; Synonyms=apc3, cdc27; ORFNames=DDB_G0288223;
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 APC3/CDC27 family. {ECO:0000305}.
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DR EMBL; AAFI02000109; EAL63342.1; -; Genomic_DNA.
DR RefSeq; XP_636853.1; XM_631761.1.
DR AlphaFoldDB; Q54J83; -.
DR SMR; Q54J83; -.
DR STRING; 44689.DDB0266416; -.
DR PaxDb; Q54J83; -.
DR EnsemblProtists; EAL63342; EAL63342; DDB_G0288223.
DR GeneID; 8626521; -.
DR KEGG; ddi:DDB_G0288223; -.
DR dictyBase; DDB_G0288223; anapc3.
DR eggNOG; KOG1126; Eukaryota.
DR HOGENOM; CLU_008850_1_1_1; -.
DR InParanoid; Q54J83; -.
DR OMA; LCGHEYL; -.
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:Q54J83; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0005680; C:anaphase-promoting complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; IPR001440; TPR_1.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF00515; TPR_1; 1.
DR Pfam; PF13181; TPR_8; 2.
DR SMART; SM00028; TPR; 9.
DR SUPFAM; SSF48452; SSF48452; 2.
DR PROSITE; PS50005; TPR; 7.
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..970
FT /note="Anaphase-promoting complex subunit 3"
FT /id="PRO_0000328277"
FT REPEAT 35..68
FT /note="TPR 1"
FT REPEAT 74..107
FT /note="TPR 2"
FT REPEAT 142..175
FT /note="TPR 3"
FT REPEAT 185..218
FT /note="TPR 4"
FT REPEAT 319..353
FT /note="TPR 5"
FT REPEAT 361..394
FT /note="TPR 6"
FT REPEAT 546..580
FT /note="TPR 7"
FT REPEAT 636..671
FT /note="TPR 8"
FT REPEAT 672..705
FT /note="TPR 9"
FT REPEAT 740..773
FT /note="TPR 10"
FT REPEAT 775..807
FT /note="TPR 11"
FT REPEAT 808..841
FT /note="TPR 12"
FT REPEAT 843..876
FT /note="TPR 13"
FT REPEAT 878..910
FT /note="TPR 14"
FT REPEAT 911..944
FT /note="TPR 15"
FT REGION 106..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 274..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 358..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 414..525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 556..582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 425..449
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 457..525
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 970 AA; 112327 MW; 415443340CE43048 CRC64;
MEEIMIQSID ESIHCGLIKN ALFLSERLYA STANEDNLFK IAQIYYQMGK INQCLLILQQ
HPQITMIKNL YLLALSNYDL GNIQEAESSI IKCCIYFEKY FQPNNNNNNN NNNNNNNNNN
NNNNNNNNKD KCNNSNKNND SNNNSNSNNN ENEYYGIYSD ILCEFDDIVD INSISYGFDS
PCSIGSVYYL MGLISKRKNQ KEKAIKYLKK SVYTYPFLWV AFEQLCNICP DEIDISDLFS
HTNLIHQINH LNQQQHQQHQ QFQQYLSNSL NQNKVNNNNN NNNNNNNNIN NNNSSNKNNE
QTITSTVATG TTNITTNTIK PNNFIKPPYH PNHRVGLTPS SFYDSSIHIT PINFKASIQQ
TNQQQQQQQQ QQPQQPSQQN LQKYNNRYFV TPQTPLSHIT PILSNRFSQN VVDPIPMVMD
TPDSKGSQHP PSSNSQTPYT PSTPGVHHHQ KQQPHQHKKS APPSQMIKKS MSNEFDTPMS
LDLKSPIFTT STSSDVHGFT SSTSKQQQQQ QQTKQQTTTT TTTTTSITDK EVLLTKTKKQ
VNFGKTEEFS LKSLSSSLSD DDYDEENHHY QQHHHLHHHN KSIDELELEE DDQLNITDNS
VQPNFYEFDE SSILDFNGGD LYEGLIELHK GQTQLLELFF ILADSYRLLC LYLCKEAIES
FKRLSEEQYR TGWVLTKVAK AYHELIDYKE ARSIFQEVSQ MEPYRLEGME LYSTLLWQMN
EDAELSYIAH KYSEFDRLSP YSWVVVGNCF SLQRDHEAAI KLFRRAIQLD PDMTYAYTLC
GHEYLANDEL ELALNAFRMA IRCDPRHYNA FYGIGLIYYR QEKYNLAEYH FRKALSINES
SSVLCCYLGM TLQHNPNKIQ DGIDMLYRSI EIQPKNTFAK FKLAAFLFAN QQYHHAIDQL
LEFKEIEPKE TPIYILLGKC YKQLGELDKA LDSLNTALDL DPKNSNYIRS LIDKLPLEDE
DDNQDYFQLN
