APC8_SCHPO
ID APC8_SCHPO Reviewed; 565 AA.
AC O94556;
DT 30-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Anaphase-promoting complex subunit 8;
DE AltName: Full=20S cyclosome/APC complex protein apc8;
DE AltName: Full=Cell untimely torn protein 23;
GN Name=cut23; Synonyms=apc8; ORFNames=SPAC6F12.14;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=972 / ATCC 24843;
RX PubMed=10526233; DOI=10.1046/j.1365-2443.1999.00274.x;
RA Yamashita Y.M., Nakaseko Y., Kumada K., Nakagawa T., Yanagida M.;
RT "Fission yeast APC/cyclosome subunits, Cut20/Apc4 and Cut23/Apc8, in
RT regulating metaphase-anaphase progression and cellular stress responses.";
RL Genes Cells 4:445-463(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP SUBUNIT.
RX PubMed=12477395; DOI=10.1016/s0960-9822(02)01331-3;
RA Yoon H.-J., Feoktistova A., Wolfe B.A., Jennings J.L., Link A.J.,
RA Gould K.L.;
RT "Proteomics analysis identifies new components of the fission and budding
RT yeast anaphase-promoting complexes.";
RL Curr. Biol. 12:2048-2054(2002).
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. The APC/C is thought to confer substrate specificity and, in the
CC presence of ubiquitin-conjugating E2 enzymes, it catalyzes the
CC formation of protein-ubiquitin conjugates that are subsequently
CC degraded by the 26S proteasome. Has a role in promoting metaphase to
CC anaphase transition via the ubiquitination of specific mitotic
CC substrates. {ECO:0000269|PubMed:10526233}.
CC -!- SUBUNIT: The APC/C is composed of at least 13 subunits: apc1, apc2,
CC nuc2, apc4, apc5, cut9, apc8, apc10, apc11, hcn1, apc13, apc14 and
CC apc15. {ECO:0000269|PubMed:12477395}.
CC -!- INTERACTION:
CC O94556; P50528: plo1; NbExp=5; IntAct=EBI-1116472, EBI-1112601;
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DR EMBL; CU329670; CAB11101.2; -; Genomic_DNA.
DR PIR; T11665; T11665.
DR RefSeq; NP_593300.1; NM_001018730.2.
DR PDB; 3ZN3; X-ray; 1.90 A; A=19-301.
DR PDB; 5FTP; X-ray; 3.10 A; A/B=19-301.
DR PDBsum; 3ZN3; -.
DR PDBsum; 5FTP; -.
DR AlphaFoldDB; O94556; -.
DR SMR; O94556; -.
DR BioGRID; 279325; 17.
DR ComplexPortal; CPX-763; Anaphase-Promoting Complex variant 1.
DR ComplexPortal; CPX-764; Anaphase-Promoting Complex variant 2.
DR ComplexPortal; CPX-765; Anaphase-Promoting Complex variant 3.
DR ComplexPortal; CPX-766; Anaphase-Promoting Complex variant 4.
DR IntAct; O94556; 3.
DR STRING; 4896.SPAC6F12.14.1; -.
DR MaxQB; O94556; -.
DR PaxDb; O94556; -.
DR PRIDE; O94556; -.
DR EnsemblFungi; SPAC6F12.14.1; SPAC6F12.14.1:pep; SPAC6F12.14.
DR GeneID; 2542880; -.
DR KEGG; spo:SPAC6F12.14; -.
DR PomBase; SPAC6F12.14; cut23.
DR VEuPathDB; FungiDB:SPAC6F12.14; -.
DR eggNOG; KOG1155; Eukaryota.
DR HOGENOM; CLU_018320_2_1_1; -.
DR InParanoid; O94556; -.
DR OMA; PKYLAAW; -.
DR PhylomeDB; O94556; -.
DR Reactome; R-SPO-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR PRO; PR:O94556; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005680; C:anaphase-promoting complex; IDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0044732; C:mitotic spindle pole body; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
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:0051306; P:mitotic sister chromatid separation; IMP:PomBase.
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; -; 3.
DR InterPro; IPR007192; APC8.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF04049; ANAPC8; 1.
DR Pfam; PF13181; TPR_8; 4.
DR SMART; SM00028; TPR; 7.
DR SUPFAM; SSF48452; SSF48452; 2.
DR PROSITE; PS50005; TPR; 7.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Mitosis; Reference proteome;
KW Repeat; TPR repeat; Ubl conjugation pathway.
FT CHAIN 1..565
FT /note="Anaphase-promoting complex subunit 8"
FT /id="PRO_0000106282"
FT REPEAT 87..120
FT /note="TPR 1"
FT REPEAT 173..206
FT /note="TPR 2"
FT REPEAT 270..303
FT /note="TPR 3"
FT REPEAT 338..371
FT /note="TPR 4"
FT REPEAT 373..405
FT /note="TPR 5"
FT REPEAT 407..439
FT /note="TPR 6"
FT REPEAT 440..473
FT /note="TPR 7"
FT REPEAT 475..507
FT /note="TPR 8"
FT HELIX 20..36
FT /evidence="ECO:0007829|PDB:3ZN3"
FT HELIX 40..51
FT /evidence="ECO:0007829|PDB:3ZN3"
FT HELIX 79..86
FT /evidence="ECO:0007829|PDB:3ZN3"
FT HELIX 88..99
FT /evidence="ECO:0007829|PDB:3ZN3"
FT HELIX 103..109
FT /evidence="ECO:0007829|PDB:3ZN3"
FT TURN 110..112
FT /evidence="ECO:0007829|PDB:3ZN3"
FT HELIX 116..134
FT /evidence="ECO:0007829|PDB:3ZN3"
FT STRAND 150..152
FT /evidence="ECO:0007829|PDB:5FTP"
FT HELIX 155..168
FT /evidence="ECO:0007829|PDB:3ZN3"
FT HELIX 173..185
FT /evidence="ECO:0007829|PDB:3ZN3"
FT HELIX 189..202
FT /evidence="ECO:0007829|PDB:3ZN3"
FT HELIX 207..215
FT /evidence="ECO:0007829|PDB:3ZN3"
FT HELIX 220..227
FT /evidence="ECO:0007829|PDB:3ZN3"
FT HELIX 235..248
FT /evidence="ECO:0007829|PDB:3ZN3"
FT HELIX 253..265
FT /evidence="ECO:0007829|PDB:3ZN3"
FT HELIX 270..283
FT /evidence="ECO:0007829|PDB:3ZN3"
FT HELIX 296..298
FT /evidence="ECO:0007829|PDB:3ZN3"
SQ SEQUENCE 565 AA; 65855 MW; 02B4C9CC07D21BB0 CRC64;
MTVSLNTMMG VDGLEDQEQL REIRNCLLKC ISECSERGLV YAVRWAAEML NGMNPIEMEH
IPFSSTPTGE FDLDPDMANE KLLEVEEKNI YLLAKSYFDC KEFERAAYTL QNCKSSKSIF
LRLYSKYLAG EKKSEEENET LLNTNLTLSS TNREFYYISE VLESLHYQGN KDPYLLYLSG
VVYRKRKQDS KAIDFLKSCV LKAPFFWSAW LELSLSIDSL ETLTTVVSQL PSTHIMTKIF
YVYASHELHQ VNSSAYEKLA EAEIIFPNSR YLKTQRALLT YDSRDFDEAE SLFENILTND
PYRLDDMDTY SNVLFVLENK SKLGFLAQVA SSIDKFRPET CSIIGNYYSL LSEHEKAVTY
FKRALQLNRN YLSAWTLMGH EYVELKNTHA AIESYRLAVD VNRKDYRAWY GLGQTYEVLD
MHFYALYYFQ RATALRPYDQ RMWQALGNCY EKIDRPQEAI KSYKRALLGS QTNSSILVRL
GNLYEELQDL NSAASMYKQC IKTEETEISP ETIKARIWLA RWELGKKNYR EAELYLSEVL
NGDLELEEAK ALLRELRSRM EHSYD
