APC7_DICDI
ID APC7_DICDI Reviewed; 580 AA.
AC Q54D58;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 105.
DE RecName: Full=Anaphase-promoting complex subunit 7;
DE Short=APC7;
GN Name=anapc7; Synonyms=apc7; ORFNames=DDB_G0292470;
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 APC7 family. {ECO:0000305}.
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DR EMBL; AAFI02000190; EAL61214.1; -; Genomic_DNA.
DR RefSeq; XP_629638.1; XM_629636.1.
DR AlphaFoldDB; Q54D58; -.
DR SMR; Q54D58; -.
DR STRING; 44689.DDB0235159; -.
DR PaxDb; Q54D58; -.
DR EnsemblProtists; EAL61214; EAL61214; DDB_G0292470.
DR GeneID; 8628702; -.
DR KEGG; ddi:DDB_G0292470; -.
DR dictyBase; DDB_G0292470; anapc7.
DR eggNOG; KOG1174; Eukaryota.
DR HOGENOM; CLU_026953_0_1_1; -.
DR InParanoid; Q54D58; -.
DR OMA; AFGHCAR; -.
DR PhylomeDB; Q54D58; -.
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:Q54D58; -.
DR Proteomes; UP000002195; Chromosome 6.
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; IPR019734; TPR_repeat.
DR Pfam; PF13181; TPR_8; 1.
DR SMART; SM00028; TPR; 6.
DR SUPFAM; SSF48452; SSF48452; 2.
DR PROSITE; PS50005; TPR; 3.
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..580
FT /note="Anaphase-promoting complex subunit 7"
FT /id="PRO_0000328206"
FT REPEAT 50..83
FT /note="TPR 1"
FT REPEAT 107..140
FT /note="TPR 2"
FT REPEAT 141..175
FT /note="TPR 3"
FT REPEAT 253..286
FT /note="TPR 4"
FT REPEAT 321..354
FT /note="TPR 5"
FT REPEAT 356..388
FT /note="TPR 6"
FT REPEAT 390..421
FT /note="TPR 7"
FT REPEAT 422..456
FT /note="TPR 8"
FT REPEAT 458..490
FT /note="TPR 9"
FT REPEAT 491..523
FT /note="TPR 10"
FT REGION 539..580
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 545..580
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 580 AA; 66851 MW; 2BEDBEA0B67E8AC9 CRC64;
MIQQLPMVNV ELMISNLRIL VESKQFSSAE FLGNFVISVP NQQKTPHQNI ISFSLFGDSL
FGKNEFVRSL KYFKQSLDIL FKVYNNPNNN NNNNNKQADF DNKQFEYELK YKISLCYIKI
NRNNLAISYL ESIPFSSRGL DTHLTIARLY KDIGKEKSKE CIISYKEVIK LCPLCLEAIN
SLKEMGENVD QVLIPSINKF QQKNNSFNSN NIIDLSWISL LSMSQYEMKR NQPEKSLILL
KKVESKFSTN LYVLEKLALS YLYHDEPSII NTFNIFQKIR LLDPYYIGSM DIFCSLLKRR
SLQFELNKVC NDLVASNPYC AETWTSVALF YFLKENVEKS LENVDRAISI KESHEFAHSL
KGEILLSLDE PREALPSLER AFQLSKNILT ARELVRCHLI LNQMKEALVV AETINNLSPD
YSKTMALLGM VLANQPEERE EARKILTKAL TLSPHCTDTV LTLSKLNVVE GRFQEAIDIL
NSQLEYQETD LMHTEIAGVY LTKDYHEDAM IHYNSALEIN PQYEPASRGI ARLELIMKGI
DPDQELDQEN DDDDQEEGEG ENDQEENDDD DNDDDDEYIS
