CENPO_YEAST
ID CENPO_YEAST Reviewed; 368 AA.
AC Q06675; D6VSU9;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Inner kinetochore subunit MCM21 {ECO:0000305};
DE AltName: Full=CENP-O homolog {ECO:0000303|PubMed:22561346};
DE AltName: Full=Chromosome transmission fidelity protein 5;
DE AltName: Full=Constitutive centromere-associated network protein MCM21 {ECO:0000305};
DE AltName: Full=Minichromosome maintenance protein 21;
GN Name=MCM21; Synonyms=CTF5; OrderedLocusNames=YDR318W;
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] OF 118-368.
RC STRAIN=ATCC 204508 / S288c;
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 REVISION OF GENE MODEL, INTERACTION WITH CTF19 AND OKP1, AND SUBCELLULAR
RP LOCATION.
RX PubMed=10323865; DOI=10.1101/gad.13.9.1140;
RA Ortiz J., Stemmann O., Rank S., Lechner J.;
RT "A putative protein complex consisting of Ctf19, Mcm21, and Okp1 represents
RT a missing link in the budding yeast kinetochore.";
RL Genes Dev. 13:1140-1155(1999).
RN [5]
RP FUNCTION.
RX PubMed=9987135; DOI=10.1046/j.1365-2958.1999.01179.x;
RA Poddar A., Roy N., Sinha P.;
RT "MCM21 and MCM22, two novel genes of the yeast Saccharomyces cerevisiae are
RT required for chromosome transmission.";
RL Mol. Microbiol. 31:349-360(1999).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND COMPONENT OF CTF19 COMPLEX.
RX PubMed=12408861; DOI=10.1016/s0092-8674(02)00973-x;
RA Cheeseman I.M., Anderson S., Jwa M., Green E.M., Kang J.-S.,
RA Yates J.R. III, Chan C.S.M., Drubin D.G., Barnes G.;
RT "Phospho-regulation of kinetochore-microtubule attachments by the Aurora
RT kinase Ipl1p.";
RL Cell 111:163-172(2002).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND COMPONENT OF COMA COMPLEX.
RX PubMed=14633972; DOI=10.1101/gad.1144403;
RA De Wulf P., McAinsh A.D., Sorger P.K.;
RT "Hierarchical assembly of the budding yeast kinetochore from multiple
RT subcomplexes.";
RL Genes Dev. 17:2902-2921(2003).
RN [8]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [9]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-88, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [11]
RP IDENTIFICATION IN CCAN, AND SUBUNIT.
RX PubMed=22561346; DOI=10.1038/ncb2493;
RA Schleiffer A., Maier M., Litos G., Lampert F., Hornung P., Mechtler K.,
RA Westermann S.;
RT "CENP-T proteins are conserved centromere receptors of the Ndc80 complex.";
RL Nat. Cell Biol. 14:604-613(2012).
RN [12]
RP SUBCELLULAR LOCATION.
RX PubMed=29046335; DOI=10.15252/embj.201796636;
RA Schmitzberger F., Richter M.M., Gordiyenko Y., Robinson C.V., Dadlez M.,
RA Westermann S.;
RT "Molecular basis for inner kinetochore configuration through RWD domain-
RT peptide interactions.";
RL EMBO J. 36:3458-3482(2017).
CC -!- FUNCTION: Component of the kinetochore, a multiprotein complex that
CC assembles on centromeric DNA and attaches chromosomes to spindle
CC microtubules, mediating chromosome segregation and sister chromatid
CC segregation during meiosis and mitosis. Component of the inner
CC kinetochore COMA complex, which connects centromere-associated proteins
CC and the outer kinetochore. COMA interacts with other inner kinetochore
CC proteins to form the inner kinetochore constitutive centromere-
CC associated network (CCAN), which serves as a structural platform for
CC outer kinetochore assembly. {ECO:0000269|PubMed:9987135}.
CC -!- SUBUNIT: Component of the heterotetrameric kinetochore subcomplex COMA,
CC which consists of AME1, CTF19, MCM21 and OKP1 (PubMed:10323865,
CC PubMed:14633972). The COMA subcomplex is part of a larger constitutive
CC centromere-associated network (CCAN) (also known as central kinetochore
CC CTF19 complex in yeast), which is composed of at least AME1, CHL4,
CC CNN1, CTF3, CTF19, IML3, MCM16, MCM21, MCM22, MHF1, MHF2, MIF2, NKP1,
CC NKP2, OKP1 and WIP1 (PubMed:12408861, PubMed:22561346). COMA binds the
CC centromeric nucleosome-binding protein MIF2, and to the outer
CC kinetochore MIND subcomplex (By similarity).
CC {ECO:0000250|UniProtKB:Q6CRN7, ECO:0000269|PubMed:10323865,
CC ECO:0000269|PubMed:12408861, ECO:0000269|PubMed:14633972,
CC ECO:0000269|PubMed:22561346}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:29046335}.
CC Chromosome, centromere, kinetochore {ECO:0000269|PubMed:29046335}.
CC -!- MISCELLANEOUS: Present with 952 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the CENP-O/MCM21 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB64754.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; U32517; AAB64754.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AY557737; AAS56063.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12159.1; -; Genomic_DNA.
DR PIR; S59784; S59784.
DR RefSeq; NP_010604.4; NM_001180626.3.
DR PDB; 6NUW; EM; 4.25 A; C=1-368.
DR PDB; 6QLD; EM; 4.15 A; O=153-364.
DR PDB; 6QLE; EM; 3.55 A; O=1-368.
DR PDB; 6QLF; EM; 3.45 A; O=1-368.
DR PDBsum; 6NUW; -.
DR PDBsum; 6QLD; -.
DR PDBsum; 6QLE; -.
DR PDBsum; 6QLF; -.
DR AlphaFoldDB; Q06675; -.
DR SMR; Q06675; -.
DR BioGRID; 32374; 229.
DR ComplexPortal; CPX-1187; COMA complex.
DR DIP; DIP-2240N; -.
DR IntAct; Q06675; 42.
DR MINT; Q06675; -.
DR STRING; 4932.YDR318W; -.
DR iPTMnet; Q06675; -.
DR MaxQB; Q06675; -.
DR PaxDb; Q06675; -.
DR PRIDE; Q06675; -.
DR EnsemblFungi; YDR318W_mRNA; YDR318W; YDR318W.
DR GeneID; 851916; -.
DR KEGG; sce:YDR318W; -.
DR SGD; S000002726; MCM21.
DR VEuPathDB; FungiDB:YDR318W; -.
DR eggNOG; ENOG502RXWX; Eukaryota.
DR HOGENOM; CLU_068734_0_0_1; -.
DR InParanoid; Q06675; -.
DR OMA; FEKPHYI; -.
DR BioCyc; YEAST:G3O-29876-MON; -.
DR PRO; PR:Q06675; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q06675; protein.
DR GO; GO:0000817; C:COMA complex; IDA:SGD.
DR GO; GO:0000776; C:kinetochore; IDA:SGD.
DR GO; GO:0008608; P:attachment of spindle microtubules to kinetochore; IC:ComplexPortal.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0034508; P:centromere complex assembly; IEA:InterPro.
DR GO; GO:0034087; P:establishment of mitotic sister chromatid cohesion; IMP:SGD.
DR GO; GO:1905262; P:negative regulation of meiotic DNA double-strand break formation involved in reciprocal meiotic recombination; IMP:SGD.
DR GO; GO:0071459; P:protein localization to chromosome, centromeric region; IMP:SGD.
DR InterPro; IPR018464; CENP-O.
DR Pfam; PF09496; CENP-O; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Centromere; Chromosome;
KW Coiled coil; Kinetochore; Meiosis; Mitosis; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..368
FT /note="Inner kinetochore subunit MCM21"
FT /id="PRO_0000096282"
FT COILED 1..43
FT /evidence="ECO:0000255"
FT MOD_RES 88
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT HELIX 156..171
FT /evidence="ECO:0007829|PDB:6QLF"
FT STRAND 174..180
FT /evidence="ECO:0007829|PDB:6QLF"
FT STRAND 183..188
FT /evidence="ECO:0007829|PDB:6QLF"
FT STRAND 190..192
FT /evidence="ECO:0007829|PDB:6QLF"
FT STRAND 195..199
FT /evidence="ECO:0007829|PDB:6QLF"
FT STRAND 201..206
FT /evidence="ECO:0007829|PDB:6QLF"
FT STRAND 211..213
FT /evidence="ECO:0007829|PDB:6QLF"
FT STRAND 220..226
FT /evidence="ECO:0007829|PDB:6QLF"
FT TURN 228..230
FT /evidence="ECO:0007829|PDB:6QLF"
FT STRAND 233..238
FT /evidence="ECO:0007829|PDB:6QLF"
FT HELIX 246..252
FT /evidence="ECO:0007829|PDB:6QLF"
FT HELIX 253..256
FT /evidence="ECO:0007829|PDB:6QLF"
FT HELIX 261..290
FT /evidence="ECO:0007829|PDB:6QLF"
FT STRAND 305..309
FT /evidence="ECO:0007829|PDB:6QLF"
FT STRAND 314..320
FT /evidence="ECO:0007829|PDB:6QLF"
FT STRAND 323..330
FT /evidence="ECO:0007829|PDB:6QLF"
FT HELIX 340..348
FT /evidence="ECO:0007829|PDB:6QLF"
FT HELIX 353..359
FT /evidence="ECO:0007829|PDB:6QLF"
SQ SEQUENCE 368 AA; 42971 MW; B01FA87E25D426F3 CRC64;
MSRIDDLQQD IESLLSEINS LEESREKLKA KIKDKRKNEE SANPIVQEFE DLFDQFPQLN
NFLFNEHPEL EETDDKDISR AQADIPATPI PYEPKKRAKL ENEEILPEQE WVLKTQPMVQ
HQMFDPGVAD LLDTDILTSP SKRKRKLKID DISTSDRSEL EDYIVLENVY RMFGITFFPL
VDPIDLKIKD ASGEIFVDRE MLGIRLEVFS ERTSQFEKPH YVLLKKRIKS NSWFLFKHTI
PSFIDVQGIF DDTNGGLVIS HDDAYLFAKR VFLQLVEVQK RRQIFKDLEA KKIIHDLDLD
LESSMVSFFV KDIKVELFVK QNEIVSCSIL DDIHDFSQNN KSKWEIALLG SLDDLELKLN
HSFATIFK
