CENPI_YEAST
ID CENPI_YEAST Reviewed; 733 AA.
AC Q12748; D6VZ16; Q7LHY6;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Inner kinetochore subunit CTF3 {ECO:0000305};
DE AltName: Full=CENP-I homolog {ECO:0000303|PubMed:22561346};
DE AltName: Full=Chromosome loss protein 3;
DE AltName: Full=Chromosome transmission fidelity protein 3;
DE AltName: Full=Constitutive centromere-associated network protein CTF3 {ECO:0000305};
GN Name=CTF3; Synonyms=CHL3; OrderedLocusNames=YLR381W;
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=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(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 538-733.
RC STRAIN=AB1-4A/8/55;
RX PubMed=3034607; DOI=10.1002/j.1460-2075.1987.tb04812.x;
RA Labouesse M., Herbert C.J., Dujardin G., Slonimski P.P.;
RT "Three suppressor mutations which cure a mitochondrial RNA maturase
RT deficiency occur at the same codon in the open reading frame of the nuclear
RT NAM2 gene.";
RL EMBO J. 6:713-721(1987).
RN [4]
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 [5]
RP INTERACTION WITH CTF19; 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 [6]
RP INTERACTION WITH CHL4 AND CTF19, 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 [7]
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 [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 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 [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Component of the central kinetochore, which mediates the
CC attachment of the centromere to the mitotic spindle by forming
CC essential interactions between the microtubule-associated outer
CC kinetochore proteins and the centromere-associated inner kinetochore
CC proteins. Required for establishing bipolar spindle-microtubule
CC attachments and proper chromosome segregation.
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 constitutive centromere-associated network (CCAN), which
CC serves as a structural platform for outer kinetochore assembly.
CC {ECO:0000269|PubMed:12408861}.
CC -!- SUBUNIT: Component of the heterotrimeric kinetochore subcomplex CTF3,
CC which consists of CTF3, MCM16 and MCM22 (PubMed:11782448). The CTF3
CC subcomplex is part of a larger constitutive centromere-associated
CC network (CCAN) (also known as central kinetochore CTF19 complex in
CC yeast), which is composed of at least AME1, CHL4, CNN1, CTF3, CTF19,
CC IML3, MCM16, MCM21, MCM22, MHF1, MHF2, MIF2, NKP1, NKP2, OKP1 and WIP1
CC (PubMed:12408861, PubMed:22561346). Interacts with CTF19
CC (PubMed:11782448, PubMed:12589047). Interacts with CHL4
CC (PubMed:12589047). {ECO:0000269|PubMed:11782448,
CC ECO:0000269|PubMed:12408861, ECO:0000269|PubMed:12589047,
CC ECO:0000269|PubMed:22561346}.
CC -!- INTERACTION:
CC Q12748; Q02732: CTF19; NbExp=3; IntAct=EBI-30457, EBI-5199;
CC Q12748; Q12262: MCM16; NbExp=3; IntAct=EBI-30457, EBI-31487;
CC Q12748; P47167: MCM22; NbExp=2; IntAct=EBI-30457, EBI-25691;
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome, centromere, kinetochore.
CC Note=Associated with kinetochores.
CC -!- MISCELLANEOUS: Present with 319 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the CENP-I/CTF3 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; U19104; AAB67274.1; -; Genomic_DNA.
DR EMBL; X05143; CAA28792.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09682.1; -; Genomic_DNA.
DR PIR; S51468; S51468.
DR RefSeq; NP_013485.1; NM_001182270.1.
DR PDB; 6NUW; EM; 4.25 A; H/Y=1-733.
DR PDB; 6OUA; EM; 4.18 A; I=1-733.
DR PDB; 6QLD; EM; 4.15 A; I=321-728.
DR PDB; 6QLE; EM; 3.55 A; I=335-733.
DR PDB; 6WUC; EM; 3.23 A; I=1-733.
DR PDB; 6YPC; X-ray; 2.90 A; I=1-245.
DR PDB; 7L7Q; EM; 3.70 A; I=1-733.
DR PDBsum; 6NUW; -.
DR PDBsum; 6OUA; -.
DR PDBsum; 6QLD; -.
DR PDBsum; 6QLE; -.
DR PDBsum; 6WUC; -.
DR PDBsum; 6YPC; -.
DR PDBsum; 7L7Q; -.
DR AlphaFoldDB; Q12748; -.
DR SMR; Q12748; -.
DR BioGRID; 31640; 155.
DR ComplexPortal; CPX-1156; Central kinetochore CTF19 complex.
DR DIP; DIP-4647N; -.
DR IntAct; Q12748; 13.
DR MINT; Q12748; -.
DR STRING; 4932.YLR381W; -.
DR iPTMnet; Q12748; -.
DR MaxQB; Q12748; -.
DR PaxDb; Q12748; -.
DR PRIDE; Q12748; -.
DR EnsemblFungi; YLR381W_mRNA; YLR381W; YLR381W.
DR GeneID; 851097; -.
DR KEGG; sce:YLR381W; -.
DR SGD; S000004373; CTF3.
DR VEuPathDB; FungiDB:YLR381W; -.
DR eggNOG; ENOG502QS8Q; Eukaryota.
DR HOGENOM; CLU_022668_0_0_1; -.
DR InParanoid; Q12748; -.
DR OMA; NYLWRNK; -.
DR BioCyc; YEAST:G3O-32447-MON; -.
DR PRO; PR:Q12748; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q12748; protein.
DR GO; GO:0000776; C:kinetochore; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0007059; P:chromosome segregation; IMP:SGD.
DR GO; GO:0006270; P:DNA replication initiation; 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.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cell cycle; Cell division; Centromere;
KW Chromosome; Kinetochore; Meiosis; Mitosis; Nucleus; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..733
FT /note="Inner kinetochore subunit CTF3"
FT /id="PRO_0000079493"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT HELIX 4..14
FT /evidence="ECO:0007829|PDB:6YPC"
FT HELIX 21..38
FT /evidence="ECO:0007829|PDB:6YPC"
FT HELIX 42..54
FT /evidence="ECO:0007829|PDB:6YPC"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:6YPC"
FT HELIX 60..70
FT /evidence="ECO:0007829|PDB:6YPC"
FT STRAND 73..76
FT /evidence="ECO:0007829|PDB:6YPC"
FT HELIX 79..86
FT /evidence="ECO:0007829|PDB:6YPC"
FT HELIX 94..96
FT /evidence="ECO:0007829|PDB:6WUC"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:6WUC"
FT HELIX 104..116
FT /evidence="ECO:0007829|PDB:6YPC"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:6YPC"
FT HELIX 126..140
FT /evidence="ECO:0007829|PDB:6YPC"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:6YPC"
FT HELIX 146..156
FT /evidence="ECO:0007829|PDB:6YPC"
FT TURN 160..162
FT /evidence="ECO:0007829|PDB:6YPC"
FT HELIX 165..176
FT /evidence="ECO:0007829|PDB:6YPC"
FT HELIX 178..180
FT /evidence="ECO:0007829|PDB:6WUC"
FT HELIX 183..198
FT /evidence="ECO:0007829|PDB:6YPC"
FT HELIX 202..210
FT /evidence="ECO:0007829|PDB:6YPC"
FT HELIX 217..222
FT /evidence="ECO:0007829|PDB:6YPC"
FT HELIX 228..240
FT /evidence="ECO:0007829|PDB:6YPC"
FT HELIX 248..264
FT /evidence="ECO:0007829|PDB:6WUC"
FT TURN 265..267
FT /evidence="ECO:0007829|PDB:6WUC"
FT HELIX 296..301
FT /evidence="ECO:0007829|PDB:6WUC"
FT HELIX 312..315
FT /evidence="ECO:0007829|PDB:6WUC"
FT TURN 333..347
FT /evidence="ECO:0007829|PDB:6WUC"
FT HELIX 355..368
FT /evidence="ECO:0007829|PDB:6WUC"
FT HELIX 375..386
FT /evidence="ECO:0007829|PDB:6WUC"
FT HELIX 390..400
FT /evidence="ECO:0007829|PDB:6WUC"
FT STRAND 401..403
FT /evidence="ECO:0007829|PDB:6WUC"
FT HELIX 404..408
FT /evidence="ECO:0007829|PDB:6WUC"
FT HELIX 410..420
FT /evidence="ECO:0007829|PDB:6WUC"
FT STRAND 421..423
FT /evidence="ECO:0007829|PDB:6WUC"
FT HELIX 432..447
FT /evidence="ECO:0007829|PDB:6WUC"
FT HELIX 458..474
FT /evidence="ECO:0007829|PDB:6WUC"
FT HELIX 479..490
FT /evidence="ECO:0007829|PDB:6WUC"
FT TURN 491..494
FT /evidence="ECO:0007829|PDB:6WUC"
FT TURN 496..498
FT /evidence="ECO:0007829|PDB:6WUC"
FT STRAND 501..503
FT /evidence="ECO:0007829|PDB:6WUC"
FT TURN 506..511
FT /evidence="ECO:0007829|PDB:6WUC"
FT HELIX 512..524
FT /evidence="ECO:0007829|PDB:6WUC"
FT HELIX 532..534
FT /evidence="ECO:0007829|PDB:6WUC"
FT TURN 539..541
FT /evidence="ECO:0007829|PDB:6WUC"
FT HELIX 542..546
FT /evidence="ECO:0007829|PDB:6WUC"
FT HELIX 551..562
FT /evidence="ECO:0007829|PDB:6WUC"
FT TURN 566..568
FT /evidence="ECO:0007829|PDB:6WUC"
FT STRAND 569..571
FT /evidence="ECO:0007829|PDB:6WUC"
FT HELIX 576..588
FT /evidence="ECO:0007829|PDB:6WUC"
FT TURN 590..593
FT /evidence="ECO:0007829|PDB:6WUC"
FT TURN 597..599
FT /evidence="ECO:0007829|PDB:6WUC"
FT STRAND 603..606
FT /evidence="ECO:0007829|PDB:6WUC"
FT HELIX 608..614
FT /evidence="ECO:0007829|PDB:6WUC"
FT TURN 627..629
FT /evidence="ECO:0007829|PDB:6WUC"
FT STRAND 630..632
FT /evidence="ECO:0007829|PDB:6WUC"
FT TURN 633..635
FT /evidence="ECO:0007829|PDB:6WUC"
FT TURN 637..639
FT /evidence="ECO:0007829|PDB:6WUC"
FT HELIX 640..654
FT /evidence="ECO:0007829|PDB:6WUC"
FT HELIX 667..676
FT /evidence="ECO:0007829|PDB:6WUC"
FT HELIX 678..683
FT /evidence="ECO:0007829|PDB:6WUC"
FT STRAND 684..686
FT /evidence="ECO:0007829|PDB:6WUC"
FT HELIX 693..704
FT /evidence="ECO:0007829|PDB:6WUC"
FT HELIX 712..722
FT /evidence="ECO:0007829|PDB:6WUC"
FT STRAND 723..725
FT /evidence="ECO:0007829|PDB:6WUC"
SQ SEQUENCE 733 AA; 84252 MW; 38DB89EE32C44AC6 CRC64;
MSLILDDIIL SLTNANERTP PQALKTTLSL LYEKSKQYGL SSPQLQALVR LLCETSIIDT
VTKVYIVENC FLPDGYLTKE LLLEIINHLG TPTVFSRYRI QTPPVLQSAL CKWLVHVYFL
FPVHSEREHN ISSSIWLHLW QFSFLQKWIT PLVIWQATTP VDVKPWKLSI IKRCAMHPGY
RDAPGSATLI LQRFQCLVGA SSQITESIIT INCNRKTLKS HRNLKLDAHF LSILKRILSR
AHPANFPADT VQNTIDMYLS EIHQLGADSI YPLRLQSLPE YVPSDSTVSL WDVTSLEQLA
QNWPQLHIPN DVDYMMKPSL NSNVLLPRKV MSRDSLKHLY SSIILIKNSR DESSSPYEWC
IWQLKRCFAH QIETPQEVIP IIISVSSMDN KLSSRIIQTF CNLKYLKLDE LTLKKVCGGI
LPLWKPELIS GTREFFVKFM ASIFMWSTRD GHDNNCTFSE TCFYVLQMIT NWVLDDKLIA
LGLTLLHDMQ SLLTLDKIFN NATSNRFSTM AFISSLDILT QLSKQTKSDY AIQYLIVGPD
IMNKVFSSDD PLLLSAACRY LVATKNKLMQ YPSTNKFVRM QNQYIMDLTN YLYRNKVLSS
KSLFGVSPDF FKQILENLYI PTADFKNAKF FTITGIPALS YICIIILRRL ETAENTKIKF
TSGIINEETF NNFFRVHHDE IGQHGWIKGV NNIHDLRVKI LMHLSNTANP YRDIAAFLFT
YLKSLSKYSV QNS
