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 27-MAR-2024, entry version 174. 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; GN 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 PDB; 8OVW; EM; 3.40 A; P=1-369. DR PDB; 8OVX; EM; 3.40 A; P=1-369. DR PDB; 8OW0; EM; 3.40 A; P=1-369. DR PDB; 8OW1; EM; 3.70 A; P/PP=1-369. DR PDBsum; 5W94; -. DR PDBsum; 6NUW; -. DR PDBsum; 6QLD; -. DR PDBsum; 6QLE; -. DR PDBsum; 6QLF; -. DR PDBsum; 8OVW; -. DR PDBsum; 8OVX; -. DR PDBsum; 8OW0; -. DR PDBsum; 8OW1; -. DR AlphaFoldDB; Q02732; -. DR EMDB; EMD-0523; -. DR EMDB; EMD-17224; -. DR EMDB; EMD-17225; -. DR EMDB; EMD-17226; -. DR EMDB; EMD-17227; -. DR EMDB; EMD-4579; -. DR EMDB; EMD-4580; -. DR EMDB; EMD-4581; -. DR SMR; Q02732; -. DR BioGRID; 36159; 320. DR ComplexPortal; CPX-1187; COMA complex. DR ComplexPortal; CPX-2533; Kinetochore CCAN complex. DR DIP; DIP-3009N; -. DR IntAct; Q02732; 16. DR MINT; Q02732; -. DR STRING; 4932.YPL018W; -. DR MaxQB; Q02732; -. DR PaxDb; 4932-YPL018W; -. DR PeptideAtlas; Q02732; -. DR EnsemblFungi; YPL018W_mRNA; YPL018W; YPL018W. DR GeneID; 856089; -. DR KEGG; sce:YPL018W; -. DR AGR; SGD:S000005939; -. 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 OrthoDB; 2029234at2759; -. DR BioCyc; YEAST:G3O-33937-MONOMER; -. DR BioGRID-ORCS; 856089; 1 hit in 10 CRISPR screens. 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 //