SWM1_YEAST
ID SWM1_YEAST Reviewed; 170 AA.
AC Q12379; D6VSP0;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Anaphase-promoting complex subunit SWM1;
DE AltName: Full=Anaphase-promoting complex subunit 13;
DE AltName: Full=Spore wall maturation protein 1;
GN Name=SWM1; Synonyms=APC13; OrderedLocusNames=YDR260C;
GN ORFNames=YD9320A.11, YD9320A.11c;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
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).
RN [5]
RP SUBUNIT, AND INTERACTION WITH APC5 AND CDC23.
RX PubMed=12609981; DOI=10.1074/jbc.m213109200;
RA Hall M.C., Torres M.P., Schroeder G.K., Borchers C.H.;
RT "Mnd2 and Swm1 are core subunits of the Saccharomyces cerevisiae anaphase-
RT promoting complex.";
RL J. Biol. Chem. 278:16698-16705(2003).
RN [6]
RP FUNCTION, AND SUBUNIT.
RX PubMed=15060174; DOI=10.1128/mcb.24.8.3562-3576.2004;
RA Schwickart M., Havlis J., Habermann B., Bogdanova A., Camasses A.,
RA Oelschlaegel T., Shevchenko A., Zachariae W.;
RT "Swm1/Apc13 is an evolutionarily conserved subunit of the anaphase-
RT promoting complex stabilizing the association of Cdc16 and Cdc27.";
RL Mol. Cell. Biol. 24:3562-3576(2004).
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. In early mitosis, the APC/C is
CC activated by CDC20 and targets securin PDS1, the B-type cyclin CLB5,
CC and other anaphase inhibitory proteins for proteolysis, thereby
CC triggering the separation of sister chromatids at the metaphase-to-
CC anaphase transition. In late mitosis and in G1, degradation of CLB5
CC allows activation of the APC/C by CDH1, which is needed to destroy
CC CDC20 and the B-type cyclin CLB2 to allow exit from mitosis and
CC creating the low CDK state necessary for cytokinesis and for reforming
CC prereplicative complexes in G1 prior to another round of replication.
CC SWM1 is required for APC/C activity in meiosis.
CC {ECO:0000269|PubMed:15060174}.
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: APC1, APC2, APC4, APC5,
CC APC9, APC11, CDC16, CDC23, CDC26, CDC27, DOC1, MND2 and SWM1. SWM1
CC interacts directly with CDC23 and APC5, and is required to tether APC9,
CC CDC16, CDC26 and CDC27 to the complex. {ECO:0000269|PubMed:12477395,
CC ECO:0000269|PubMed:12609981, ECO:0000269|PubMed:15060174}.
CC -!- INTERACTION:
CC Q12379; Q04601: APC4; NbExp=5; IntAct=EBI-33330, EBI-32842;
CC Q12379; Q08683: APC5; NbExp=4; IntAct=EBI-33330, EBI-35371;
CC Q12379; P16522: CDC23; NbExp=5; IntAct=EBI-33330, EBI-4216;
CC -!- SIMILARITY: Belongs to the APC13 family. {ECO:0000305}.
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DR EMBL; Z70202; CAA94099.1; -; Genomic_DNA.
DR EMBL; Z68329; CAA92718.1; -; Genomic_DNA.
DR EMBL; AY557727; AAS56053.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12100.1; -; Genomic_DNA.
DR PIR; S67318; S67318.
DR RefSeq; NP_010546.1; NM_001180568.1.
DR AlphaFoldDB; Q12379; -.
DR BioGRID; 32310; 165.
DR ComplexPortal; CPX-756; Anaphase-Promoting core complex.
DR ComplexPortal; CPX-760; Anaphase-Promoting Complex, CDC20 variant.
DR ComplexPortal; CPX-761; Anaphase-Promoting Complex, CDH1 variant.
DR ComplexPortal; CPX-762; Anaphase-Promoting complex AMA1 variant.
DR DIP; DIP-4818N; -.
DR IntAct; Q12379; 32.
DR STRING; 4932.YDR260C; -.
DR PaxDb; Q12379; -.
DR PRIDE; Q12379; -.
DR EnsemblFungi; YDR260C_mRNA; YDR260C; YDR260C.
DR GeneID; 851847; -.
DR KEGG; sce:YDR260C; -.
DR SGD; S000002668; SWM1.
DR VEuPathDB; FungiDB:YDR260C; -.
DR eggNOG; ENOG502S9HM; Eukaryota.
DR HOGENOM; CLU_150173_0_0_1; -.
DR InParanoid; Q12379; -.
DR OMA; SSHHALY; -.
DR BioCyc; YEAST:G3O-29831-MON; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q12379; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q12379; protein.
DR GO; GO:0005680; C:anaphase-promoting complex; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:1904824; P:anaphase-promoting complex assembly; IMP:SGD.
DR GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; IDA:ComplexPortal.
DR GO; GO:0030476; P:ascospore wall assembly; IMP:SGD.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IDA:ComplexPortal.
DR GO; GO:0051445; P:regulation of meiotic cell cycle; IC:ComplexPortal.
DR GO; GO:0007346; P:regulation of mitotic cell cycle; IC:ComplexPortal.
DR GO; GO:0030071; P:regulation of mitotic metaphase/anaphase transition; IMP:SGD.
DR InterPro; IPR008401; Apc13.
DR Pfam; PF05839; Apc13p; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Meiosis; Mitosis; Reference proteome;
KW Ubl conjugation pathway.
FT CHAIN 1..170
FT /note="Anaphase-promoting complex subunit SWM1"
FT /id="PRO_0000072352"
FT REGION 48..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 122..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..64
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..81
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 170 AA; 19356 MW; 7DD5FC4CBDE8BF19 CRC64;
MSSSSYRDSY FQYRHLPAPH HILYAEWNQD ILALPDEVAN ITMAMKDNTR TDAEEGRAPQ
DGERNSNVRE SAQGKALMTS EQNSNRYWNS FHDEDDWNLF NGMELESNGV VTFAGQAFDH
SLNGGTNSRN DGANEPRKET ITGSIFDRRI TQLAYARNNG WHELALPQSR
