APC14_SCHPO
ID APC14_SCHPO Reviewed; 107 AA.
AC O42659;
DT 25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 25-MAY-2022, entry version 101.
DE RecName: Full=Anaphase-promoting complex subunit 14;
DE AltName: Full=20S cyclosome/APC complex protein apc14;
DE AltName: Full=Overlapping meiotic transcript protein 1;
GN Name=apc14 {ECO:0000312|PomBase:SPAC27D7.05c};
GN Synonyms=omt1 {ECO:0000303|PubMed:12786945};
GN ORFNames=SPAC27D7.05c {ECO:0000312|PomBase:SPAC27D7.05c};
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], FUNCTION, SUBCELLULAR LOCATION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=12786945; DOI=10.1046/j.1365-2443.2003.00654.x;
RA Kakihara Y., Nabeshima K., Hirata A., Nojima H.;
RT "Overlapping omt1+ and omt2+ genes are required for spore wall maturation
RT in Schizosaccharomyces pombe.";
RL Genes Cells 8:547-558(2003).
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 FUNCTION, AND 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. Appears to play a role in spore wall
CC formation. {ECO:0000269|PubMed:12477395, ECO:0000269|PubMed:12786945}.
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 O42659; O94688: apc15; NbExp=2; IntAct=EBI-1251592, EBI-1251604;
CC O42659; P41889: cut9; NbExp=2; IntAct=EBI-1251592, EBI-1160859;
CC -!- SUBCELLULAR LOCATION: Ascus epiplasm {ECO:0000269|PubMed:12786945}.
CC -!- DISRUPTION PHENOTYPE: Abnormal spore wall formation (PubMed:12786945).
CC Abnormal spore wall polysaccharide composition during sporulation
CC (PubMed:12786945). Irregular spore wall thickness (PubMed:12786945).
CC {ECO:0000269|PubMed:12786945}.
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DR EMBL; CU329670; CAA15824.1; -; Genomic_DNA.
DR PIR; T38438; T38438.
DR RefSeq; NP_594611.1; NM_001020039.2.
DR AlphaFoldDB; O42659; -.
DR SMR; O42659; -.
DR BioGRID; 278685; 6.
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; O42659; 4.
DR STRING; 4896.SPAC27D7.05c.1; -.
DR PaxDb; O42659; -.
DR PRIDE; O42659; -.
DR EnsemblFungi; SPAC27D7.05c.1; SPAC27D7.05c.1:pep; SPAC27D7.05c.
DR GeneID; 2542211; -.
DR KEGG; spo:SPAC27D7.05c; -.
DR PomBase; SPAC27D7.05c; apc14.
DR VEuPathDB; FungiDB:SPAC27D7.05c; -.
DR HOGENOM; CLU_2211479_0_0_1; -.
DR OMA; EAIDFWN; -.
DR PRO; PR:O42659; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005680; C:anaphase-promoting complex; IDA:PomBase.
DR GO; GO:0072324; C:ascus epiplasm; IDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; IMP:PomBase.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0051306; P:mitotic sister chromatid separation; IC:PomBase.
DR GO; GO:1905786; P:positive regulation of anaphase-promoting complex-dependent catabolic process; EXP:PomBase.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Mitosis; Reference proteome;
KW Ubl conjugation pathway.
FT CHAIN 1..107
FT /note="Anaphase-promoting complex subunit 14"
FT /id="PRO_0000058047"
SQ SEQUENCE 107 AA; 12192 MW; F2DDD34689012489 CRC64;
MDPFAGTGQS KSYRTFGNVF QRLSMSGNPK PLAKKPLLLP EASKAIEFWN YRDVIGGEEA
EQERNERASR IAISRIASSR SSIPEYRQAI MQHLTKHVQQ LDQLAEW