CENPO_KLULA
ID CENPO_KLULA Reviewed; 293 AA.
AC Q6CVQ9;
DT 13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT 04-NOV-2008, sequence version 2.
DT 25-MAY-2022, entry version 80.
DE RecName: Full=Inner kinetochore subunit MCM21;
DE AltName: Full=CENP-O homolog;
DE AltName: Full=Constitutive centromere-associated network protein MCM21;
DE AltName: Full=Minichromosome maintenance protein 21;
GN Name=MCM21; OrderedLocusNames=KLLA0B10142g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (3.7 ANGSTROMS) IN COMPLEX WITH CTF19, DOMAIN, AND
RP INTERACTION WITH AME1 AND OKP1.
RX PubMed=22322944; DOI=10.1038/embor.2012.1;
RA Schmitzberger F., Harrison S.C.;
RT "RWD domain: a recurring module in kinetochore architecture shown by a
RT Ctf19-Mcm21 complex structure.";
RL EMBO Rep. 13:216-222(2012).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 108-293 IN COMPLEX WITH CTF19 AND
RP OKP1, AND SUBUNIT.
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 (By similarity). Component of
CC the inner kinetochore COMA subcomplex, which connects centromere-
CC associated proteins and the outer kinetochore (PubMed:29046335). COMA
CC interacts with other inner kinetochore proteins to form the inner
CC kinetochore constitutive centromere-associated network (CCAN), which
CC serves as a structural platform for outer kinetochore assembly (By
CC similarity). {ECO:0000250|UniProtKB:Q06675,
CC ECO:0000269|PubMed:29046335}.
CC -!- SUBUNIT: Component of the heterotetrameric kinetochore subcomplex COMA,
CC which consists of AME1, CTF19, MCM21 and OKP1 (PubMed:22322944,
CC PubMed:29046335). 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 CTF3, CTF19, IML3, MCM16, MCM21, MCM22, NKP1, NKP2 and OKP1 (By
CC similarity). COMA binds the centromeric nucleosome-binding protein
CC MIF2, and to the outer kinetochore MIND subcomplex (PubMed:29046335).
CC {ECO:0000250|UniProtKB:Q06675, ECO:0000269|PubMed:22322944,
CC ECO:0000269|PubMed:29046335}.
CC -!- INTERACTION:
CC Q6CVQ9; Q6CRN7: CTF19; NbExp=3; IntAct=EBI-7692022, EBI-7692007;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q06675}.
CC Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q06675}.
CC -!- DOMAIN: The D-RWD region contains a double-RWD domain which is involved
CC in the interaction with other kinetochore proteins.
CC {ECO:0000269|PubMed:22322944}.
CC -!- SIMILARITY: Belongs to the CENP-O/MCM21 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; CR382122; CAH02373.2; -; Genomic_DNA.
DR RefSeq; XP_451980.2; XM_451980.2.
DR PDB; 3ZXU; X-ray; 3.90 A; A/C=1-293.
DR PDB; 5MU3; X-ray; 2.10 A; A/D=108-293.
DR PDBsum; 3ZXU; -.
DR PDBsum; 5MU3; -.
DR AlphaFoldDB; Q6CVQ9; -.
DR SMR; Q6CVQ9; -.
DR IntAct; Q6CVQ9; 3.
DR MINT; Q6CVQ9; -.
DR STRING; 28985.XP_451980.2; -.
DR EnsemblFungi; CAH02373; CAH02373; KLLA0_B10142g.
DR GeneID; 2897499; -.
DR KEGG; kla:KLLA0_B10142g; -.
DR eggNOG; ENOG502RXWX; Eukaryota.
DR HOGENOM; CLU_068734_0_0_1; -.
DR InParanoid; Q6CVQ9; -.
DR Proteomes; UP000000598; Chromosome B.
DR GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0034508; P:centromere complex assembly; IEA:InterPro.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
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; Reference proteome.
FT CHAIN 1..293
FT /note="Inner kinetochore subunit MCM21"
FT /id="PRO_0000417589"
FT REGION 107..293
FT /note="D-RWD"
FT COILED 1..31
FT /evidence="ECO:0000255"
FT HELIX 109..118
FT /evidence="ECO:0007829|PDB:5MU3"
FT STRAND 121..129
FT /evidence="ECO:0007829|PDB:5MU3"
FT STRAND 132..139
FT /evidence="ECO:0007829|PDB:5MU3"
FT TURN 144..147
FT /evidence="ECO:0007829|PDB:5MU3"
FT STRAND 153..159
FT /evidence="ECO:0007829|PDB:5MU3"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:5MU3"
FT STRAND 167..172
FT /evidence="ECO:0007829|PDB:5MU3"
FT HELIX 180..188
FT /evidence="ECO:0007829|PDB:5MU3"
FT TURN 189..191
FT /evidence="ECO:0007829|PDB:5MU3"
FT HELIX 195..221
FT /evidence="ECO:0007829|PDB:5MU3"
FT TURN 222..224
FT /evidence="ECO:0007829|PDB:5MU3"
FT STRAND 230..237
FT /evidence="ECO:0007829|PDB:5MU3"
FT STRAND 243..248
FT /evidence="ECO:0007829|PDB:5MU3"
FT STRAND 251..258
FT /evidence="ECO:0007829|PDB:5MU3"
FT TURN 259..262
FT /evidence="ECO:0007829|PDB:5MU3"
FT STRAND 263..269
FT /evidence="ECO:0007829|PDB:5MU3"
FT HELIX 281..286
FT /evidence="ECO:0007829|PDB:5MU3"
FT TURN 287..289
FT /evidence="ECO:0007829|PDB:5MU3"
SQ SEQUENCE 293 AA; 33521 MW; 7932BDB56BCC3691 CRC64;
MEETEAVQQD IEALEREIQT IKIQIANAHS GASKDEVKIP DAYKQFLSEN INFSNLMRKD
ENTTLSINLS PRKPGTTTGQ IQGIDSSIRS NFGVSSGHNE VAGFKSITDF VQWENSVRLI
GVSLFPVNYD NIEFMGIRLE LFDELSLKYD PPFYVILKPS VKRLGIWELF KHNLPKYINI
HQHWQLITKD TDTSDSNIMK FANLCYKDLL KVHSRVQFFR KLEGNYVNDK QYSLLHIDNM
GLNVSFRLGA DIIKIKVDDG DDEIIDCTFN GEKNISLLGS IYGITNRFQS IIM
