CENPN_YEAST
ID CENPN_YEAST Reviewed; 458 AA.
AC P38907; D6VSN4;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Inner kinetochore subunit CHL4 {ECO:0000305};
DE AltName: Full=CENP-N homolog {ECO:0000303|PubMed:22561346};
DE AltName: Full=Chromosome loss protein 4;
DE AltName: Full=Chromosome transmission fidelity protein 17;
DE AltName: Full=Constitutive centromere-associated network protein CHL4 {ECO:0000305};
DE AltName: Full=Minichromosome maintenance protein 17;
GN Name=CHL4; Synonyms=CTF17, MCM17; OrderedLocusNames=YDR254W;
GN ORFNames=YD9320A.04;
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.
RC STRAIN=YNK50;
RX PubMed=8316241;
RA Kouprina N.Y., Kroll E.S., Koryabin M.Y., Bannikov V.M., Kirillov A.V.,
RA Zakharyev V.M., Larionov V.L.;
RT "Stable maintenance of dicentric mini-chromosomes in CHL4 mutants in
RT yeast.";
RL Mol. Biol. (Mosk.) 27:589-607(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Z4221-3C1;
RX PubMed=8243998; DOI=10.1093/genetics/135.2.327;
RA Kouprina N.Y., Kirillov A.V., Kroll E.S., Koryabin M.Y., Shestopalov B.,
RA Bannikov V.M., Zakharyev V.M., Larionov V.L.;
RT "Identification and cloning of the CHL4 gene controlling chromosome
RT segregation in yeast.";
RL Genetics 135:327-341(1993).
RN [3]
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 [4]
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 [5]
RP FUNCTION.
RX PubMed=9339342; DOI=10.1007/s002940050264;
RA Roy N., Poddar A., Lohia A., Sinha P.;
RT "The mcm17 mutation of yeast shows a size-dependent segregational defect of
RT a mini-chromosome.";
RL Curr. Genet. 32:182-189(1997).
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; CTF19 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 [8]
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 [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 X-RAY CRYSTALLOGRAPHY (2.28 ANGSTROMS) OF 361-458 IN COMPLEX WITH IML3.
RX PubMed=24075991; DOI=10.1016/j.celrep.2013.08.036;
RA Hinshaw S.M., Harrison S.C.;
RT "An Iml3-Chl4 heterodimer links the core centromere to factors required for
RT accurate chromosome segregation.";
RL Cell Rep. 5:29-36(2013).
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:9339342}.
CC -!- SUBUNIT: Forms a heterodimer with IML3 (PubMed:12589047,
CC PubMed:24075991). CHL4-IML3 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). Interacts with
CC CTF3 and CTF19 (PubMed:12589047). {ECO:0000269|PubMed:12408861,
CC ECO:0000269|PubMed:12589047, ECO:0000269|PubMed:22561346,
CC ECO:0000269|PubMed:24075991}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12589047}.
CC Chromosome, centromere, kinetochore {ECO:0000269|PubMed:12589047}.
CC Note=Associated with kinetochores.
CC -!- MISCELLANEOUS: Present with 606 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the CENP-N/CHL4 family. {ECO:0000305}.
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DR EMBL; S63181; AAB27309.1; -; Genomic_DNA.
DR EMBL; M92290; AAA16452.1; -; Unassigned_DNA.
DR EMBL; Z70202; CAA94093.1; -; Genomic_DNA.
DR EMBL; Z68329; CAA92711.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12094.1; -; Genomic_DNA.
DR PIR; S52594; S52594.
DR RefSeq; NP_010540.3; NM_001180562.3.
DR PDB; 4JE3; X-ray; 2.28 A; B=361-458.
DR PDB; 6NUW; EM; 4.25 A; E=1-458.
DR PDB; 6QLD; EM; 4.15 A; N=5-451.
DR PDB; 6QLE; EM; 3.55 A; N=1-458.
DR PDB; 6QLF; EM; 3.45 A; N=1-458.
DR PDBsum; 4JE3; -.
DR PDBsum; 6NUW; -.
DR PDBsum; 6QLD; -.
DR PDBsum; 6QLE; -.
DR PDBsum; 6QLF; -.
DR AlphaFoldDB; P38907; -.
DR SMR; P38907; -.
DR BioGRID; 32304; 219.
DR ComplexPortal; CPX-1156; Central kinetochore CTF19 complex.
DR DIP; DIP-5659N; -.
DR IntAct; P38907; 7.
DR MINT; P38907; -.
DR STRING; 4932.YDR254W; -.
DR MaxQB; P38907; -.
DR PaxDb; P38907; -.
DR PRIDE; P38907; -.
DR EnsemblFungi; YDR254W_mRNA; YDR254W; YDR254W.
DR GeneID; 851841; -.
DR KEGG; sce:YDR254W; -.
DR SGD; S000002662; CHL4.
DR VEuPathDB; FungiDB:YDR254W; -.
DR eggNOG; ENOG502QVRZ; Eukaryota.
DR HOGENOM; CLU_031572_0_0_1; -.
DR InParanoid; P38907; -.
DR OMA; DWRHGIT; -.
DR BioCyc; YEAST:G3O-29826-MON; -.
DR PRO; PR:P38907; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P38907; protein.
DR GO; GO:0000776; C:kinetochore; IPI:ComplexPortal.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000940; C:outer kinetochore; IDA:SGD.
DR GO; GO:0005198; F:structural molecule activity; IMP: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:0007059; P:chromosome segregation; IMP:SGD.
DR GO; GO:0034089; P:establishment of meiotic sister chromatid cohesion; IMP:SGD.
DR GO; GO:0034087; P:establishment of mitotic sister chromatid cohesion; IMP:SGD.
DR GO; GO:0051382; P:kinetochore assembly; IMP:SGD.
DR GO; GO:0034090; P:maintenance of meiotic sister chromatid cohesion; IMP:SGD.
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.
DR InterPro; IPR007902; Chl4/mis15/CENP-N.
DR Pfam; PF05238; CENP-N; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Centromere; Chromosome;
KW Kinetochore; Meiosis; Mitosis; Nucleus; Reference proteome.
FT CHAIN 1..458
FT /note="Inner kinetochore subunit CHL4"
FT /id="PRO_0000089646"
FT HELIX 17..24
FT /evidence="ECO:0007829|PDB:6QLF"
FT HELIX 29..42
FT /evidence="ECO:0007829|PDB:6QLF"
FT TURN 53..55
FT /evidence="ECO:0007829|PDB:6QLF"
FT HELIX 56..64
FT /evidence="ECO:0007829|PDB:6QLF"
FT HELIX 68..76
FT /evidence="ECO:0007829|PDB:6QLF"
FT HELIX 86..99
FT /evidence="ECO:0007829|PDB:6QLF"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:6QLF"
FT STRAND 106..113
FT /evidence="ECO:0007829|PDB:6QLF"
FT TURN 114..116
FT /evidence="ECO:0007829|PDB:6QLF"
FT HELIX 127..137
FT /evidence="ECO:0007829|PDB:6QLF"
FT STRAND 140..146
FT /evidence="ECO:0007829|PDB:6QLF"
FT STRAND 150..163
FT /evidence="ECO:0007829|PDB:6QLF"
FT STRAND 200..207
FT /evidence="ECO:0007829|PDB:6QLF"
FT STRAND 209..214
FT /evidence="ECO:0007829|PDB:6QLF"
FT HELIX 219..231
FT /evidence="ECO:0007829|PDB:6QLF"
FT STRAND 234..236
FT /evidence="ECO:0007829|PDB:6QLF"
FT STRAND 238..242
FT /evidence="ECO:0007829|PDB:6QLF"
FT HELIX 251..258
FT /evidence="ECO:0007829|PDB:6QLF"
FT STRAND 259..261
FT /evidence="ECO:0007829|PDB:6QLF"
FT HELIX 262..264
FT /evidence="ECO:0007829|PDB:6QLF"
FT HELIX 269..272
FT /evidence="ECO:0007829|PDB:6QLF"
FT TURN 273..276
FT /evidence="ECO:0007829|PDB:6QLF"
FT HELIX 290..293
FT /evidence="ECO:0007829|PDB:6QLF"
FT STRAND 295..298
FT /evidence="ECO:0007829|PDB:6QLF"
FT HELIX 319..333
FT /evidence="ECO:0007829|PDB:6QLF"
FT STRAND 383..393
FT /evidence="ECO:0007829|PDB:4JE3"
FT STRAND 396..408
FT /evidence="ECO:0007829|PDB:4JE3"
FT HELIX 409..418
FT /evidence="ECO:0007829|PDB:4JE3"
FT HELIX 424..426
FT /evidence="ECO:0007829|PDB:4JE3"
FT TURN 429..437
FT /evidence="ECO:0007829|PDB:4JE3"
FT STRAND 440..443
FT /evidence="ECO:0007829|PDB:4JE3"
FT STRAND 446..449
FT /evidence="ECO:0007829|PDB:4JE3"
SQ SEQUENCE 458 AA; 52672 MW; 7C8A62C1313DCD60 CRC64;
MSNELRLEDN YVPTSDTLVV FKQLMKLPVT VLYDLTLSWF AKFGGSFDGD IYLLTETLDL
LIEKGVRRNV IVNRILYVYW PDGLNVFQLA EIDCHLMISK PEKFKWLPSK ALRGDGKPYV
VKLQPAKFIE NLQTDLAKIY HCHVYMFKHP SLPVLITRIQ LFDSNNLFLS TPNIGSINKE
SLYNKLDKFQ GKPLISRRPY YVAFPLNSPI IFHSVDKDIY ARLVLQSISR TISERETIIF
KPVQKIPVKS IHNIMTLLGP SRFAESMGPW ECYASANFER SPLHDYKKHQ GLTGKKVMVR
EFDDSFLNDD ENFYGKEEPE IRRLRLEKNM IKFKGSANGV MDQKYNDLKE FNEHVHNIRN
GKKNEDSGEP VYISRYSSLV PIEKVGFTLK NEINSRIITI KLKFNGNDIF GGLHELCDKN
LINIDKVPGW LAGENGSFSG TIMNGDFQRE QVAKGGLL
