CENPP_YEAST
ID CENPP_YEAST Reviewed; 369 AA.
AC Q02732; D6W3Z4;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Inner kinetochore subunit CTF19 {ECO:0000305};
DE AltName: Full=CENP-P homolog {ECO:0000303|PubMed:22561346};
DE AltName: Full=Chromosome transmission fidelity protein 19;
DE AltName: Full=Constitutive centromere-associated network protein CTF19 {ECO:0000305};
DE AltName: Full=Minichromosome maintenance protein 18;
GN Name=CTF19; Synonyms=MCM18; OrderedLocusNames=YPL018W; ORFNames=LPB13W;
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 [GENOMIC DNA], AND SUBCELLULAR LOCATION.
RX PubMed=10189365; DOI=10.1083/jcb.145.1.15;
RA Hyland K.M., Kingsbury J., Koshland D., Hieter P.;
RT "Ctf19p: a novel kinetochore protein in Saccharomyces cerevisiae and a
RT potential link between the kinetochore and mitotic spindle.";
RL J. Cell Biol. 145:15-28(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [3]
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 [4]
RP INTERACTION WITH CBF2; MCM21 AND OKP1, AND SUBCELLULAR 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 INTERACTION WITH CSE4, AND SUBCELLULAR LOCATION.
RX PubMed=10958698; DOI=10.1128/mcb.20.18.7037-7048.2000;
RA Chen Y., Baker R.E., Keith K.C., Harris K., Stoler S., Fitzgerald-Hayes M.;
RT "The N-terminus of the centromere H3-like protein Cse4p performs an
RT essential function distinct from that of the histone fold domain.";
RL Mol. Cell. Biol. 20:7037-7048(2000).
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 INTERACTION WITH CTF3; MCM16 AND MCM22, AND SUBCELLULAR LOCATION.
RX PubMed=11782448; DOI=10.1101/gad.949302;
RA Measday V., Hailey D.W., Pot I., Givan S.A., Hyland K.M., Cagney G.,
RA Fields S., Davis T.N., Hieter P.;
RT "Ctf3p, the Mis6 budding yeast homolog, interacts with Mcm22p and Mcm16p at
RT the yeast outer kinetochore.";
RL Genes Dev. 16:101-113(2002).
RN [8]
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 [9]
RP INTERACTION WITH CHL4; CTF3 AND IML3, AND SUBCELLULAR LOCATION.
RX PubMed=12589047; DOI=10.1091/mbc.e02-08-0517;
RA Pot I., Measday V., Snydsman B., Cagney G., Fields S., Davis T.N.,
RA Muller E.G.D., Hieter P.;
RT "Chl4p and Iml3p are two new members of the budding yeast outer
RT kinetochore.";
RL Mol. Biol. Cell 14:460-476(2003).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=14690591; DOI=10.1016/s1097-2765(03)00476-3;
RA Hazbun T.R., Malmstroem L., Anderson S., Graczyk B.J., Fox B., Riffle M.,
RA Sundin B.A., Aranda J.D., McDonald W.H., Chiu C.-H., Snydsman B.E.,
RA Bradley P., Muller E.G.D., Fields S., Baker D., Yates J.R. III, Davis T.N.;
RT "Assigning function to yeast proteins by integration of technologies.";
RL Mol. Cell 12:1353-1365(2003).
RN [11]
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 [12]
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 [13]
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:10323865,
CC ECO:0000269|PubMed:14633972}.
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). CTF19 interacts with the
CC CTF3 complex subunits CTF3, MCM16 and MCM22 as well as CHL4 and IML3
CC (PubMed:11782448, PubMed:12589047). Interacts with the N-terminal
CC domain of centromeric nucleosome protein CSE4 and with the CBF3 complex
CC subunit A (CBF2) (PubMed:10958698). {ECO:0000250|UniProtKB:Q6CRN7,
CC ECO:0000269|PubMed:10323865, ECO:0000269|PubMed:10958698,
CC ECO:0000269|PubMed:11782448, ECO:0000269|PubMed:12408861,
CC ECO:0000269|PubMed:12589047, ECO:0000269|PubMed:14633972,
CC ECO:0000269|PubMed:22561346}.
CC -!- INTERACTION:
CC Q02732; Q12748: CTF3; NbExp=3; IntAct=EBI-5199, EBI-30457;
CC Q02732; P53267: DAM1; NbExp=2; IntAct=EBI-5199, EBI-23268;
CC Q02732; Q12262: MCM16; NbExp=2; IntAct=EBI-5199, EBI-31487;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:29046335}.
CC Chromosome, centromere, kinetochore {ECO:0000269|PubMed:29046335}.
CC -!- MISCELLANEOUS: Present with 1254 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the CENP-P/CTF19 family. {ECO:0000305}.
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DR EMBL; U72265; AAB17275.1; -; Genomic_DNA.
DR EMBL; U36624; AAB68169.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11410.1; -; Genomic_DNA.
DR PIR; S63464; S63464.
DR RefSeq; NP_015307.1; NM_001183832.1.
DR PDB; 5W94; X-ray; 3.19 A; E/H=1-6.
DR PDB; 6NUW; EM; 4.25 A; D=1-369.
DR PDB; 6QLD; EM; 4.15 A; P=97-366.
DR PDB; 6QLE; EM; 3.55 A; P=1-369.
DR PDB; 6QLF; EM; 3.45 A; P=1-369.
DR PDBsum; 5W94; -.
DR PDBsum; 6NUW; -.
DR PDBsum; 6QLD; -.
DR PDBsum; 6QLE; -.
DR PDBsum; 6QLF; -.
DR AlphaFoldDB; Q02732; -.
DR SMR; Q02732; -.
DR BioGRID; 36159; 315.
DR ComplexPortal; CPX-1187; COMA complex.
DR DIP; DIP-3009N; -.
DR IntAct; Q02732; 16.
DR MINT; Q02732; -.
DR STRING; 4932.YPL018W; -.
DR MaxQB; Q02732; -.
DR PaxDb; Q02732; -.
DR PRIDE; Q02732; -.
DR EnsemblFungi; YPL018W_mRNA; YPL018W; YPL018W.
DR GeneID; 856089; -.
DR KEGG; sce:YPL018W; -.
DR SGD; S000005939; CTF19.
DR VEuPathDB; FungiDB:YPL018W; -.
DR eggNOG; ENOG502S47W; Eukaryota.
DR HOGENOM; CLU_062277_0_0_1; -.
DR InParanoid; Q02732; -.
DR OMA; THHAGEA; -.
DR BioCyc; YEAST:G3O-33937-MON; -.
DR PRO; PR:Q02732; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q02732; protein.
DR GO; GO:0000817; C:COMA complex; IDA:SGD.
DR GO; GO:0000776; C:kinetochore; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0008608; P:attachment of spindle microtubules to kinetochore; IDA:SGD.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007059; P:chromosome segregation; IMP:SGD.
DR GO; GO:0034087; P:establishment of mitotic sister chromatid cohesion; IMP:SGD.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; IMP:SGD.
DR GO; GO:0071459; P:protein localization to chromosome, centromeric region; IMP:SGD.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Centromere; Chromosome;
KW Coiled coil; Kinetochore; Meiosis; Mitosis; Nucleus; Reference proteome.
FT CHAIN 1..369
FT /note="Inner kinetochore subunit CTF19"
FT /id="PRO_0000079492"
FT COILED 51..87
FT /evidence="ECO:0000255"
FT STRAND 125..128
FT /evidence="ECO:0007829|PDB:6QLF"
FT HELIX 134..139
FT /evidence="ECO:0007829|PDB:6QLF"
FT HELIX 150..159
FT /evidence="ECO:0007829|PDB:6QLF"
FT STRAND 168..172
FT /evidence="ECO:0007829|PDB:6QLF"
FT STRAND 182..189
FT /evidence="ECO:0007829|PDB:6QLF"
FT STRAND 192..195
FT /evidence="ECO:0007829|PDB:6QLF"
FT STRAND 197..204
FT /evidence="ECO:0007829|PDB:6QLF"
FT STRAND 207..209
FT /evidence="ECO:0007829|PDB:6QLF"
FT STRAND 215..220
FT /evidence="ECO:0007829|PDB:6QLF"
FT HELIX 227..230
FT /evidence="ECO:0007829|PDB:6QLF"
FT HELIX 231..233
FT /evidence="ECO:0007829|PDB:6QLF"
FT HELIX 237..263
FT /evidence="ECO:0007829|PDB:6QLF"
FT TURN 264..268
FT /evidence="ECO:0007829|PDB:6QLF"
FT STRAND 269..272
FT /evidence="ECO:0007829|PDB:6QLF"
FT TURN 275..278
FT /evidence="ECO:0007829|PDB:6QLF"
FT STRAND 279..284
FT /evidence="ECO:0007829|PDB:6QLF"
FT STRAND 294..303
FT /evidence="ECO:0007829|PDB:6QLF"
FT STRAND 318..326
FT /evidence="ECO:0007829|PDB:6QLF"
FT STRAND 328..331
FT /evidence="ECO:0007829|PDB:6QLF"
FT HELIX 334..347
FT /evidence="ECO:0007829|PDB:6QLF"
FT HELIX 353..362
FT /evidence="ECO:0007829|PDB:6QLF"
SQ SEQUENCE 369 AA; 42782 MW; 23B4CBD6AE26E793 CRC64;
MDFTSDTTNS HDTSNSHLSL EDAVGTHHAG EADVNIDGDE KQQLSLLDDD QVRALKLQEE
KDALLTRRNT LLQEIQTYQN ILMKENNSKT KNGDILQNDI TQDFLNLISI SSSNPNSAIS
DRKRVERING LTNLQKELVT KYDTLPLLNM NLRLSYLRDH TYPHLQVSVQ SRDRVHNDGI
EVLVVNYKFC RNTMNPFEIQ FKMFYKFEDS TLLKWEILRI STNVRLKAKQ LLATRNFQKC
LLSLYEFDKI KSKKTGIFQN LINLLKRKTR CYLMNNSDSL IVERVIREGR LTTIKLQINF
IITMPGERGK PRNCFLPMSK ISIALWKGGE RFNQIDLDEI CYGLIKEYGV KTGLKEICNV
CLFPDMYAR
