CENPQ_KLULA
ID CENPQ_KLULA Reviewed; 383 AA.
AC Q6CJY0;
DT 31-JAN-2018, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 77.
DE RecName: Full=Inner kinetochore subunit OKP1;
DE AltName: Full=CENP-Q homolog;
DE AltName: Full=Constitutive centromere-associated network protein OKP1;
GN Name=OKP1; OrderedLocusNames=KLLA0F15136g;
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 (2.10 ANGSTROMS) OF 295-360 IN COMPLEX WITH CTF19 AND
RP MCM21, INTERACTION WITH AME1; NKP1 AND NKP2, SUBUNIT, SUBCELLULAR LOCATION,
RP AND FUNCTION.
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). Through its multiple protein-protein interactions, OKP1
CC acts as a molecular nexus for inner kinetochore organization
CC (PubMed:29046335). {ECO:0000250|UniProtKB:P53298,
CC ECO:0000269|PubMed:29046335}.
CC -!- SUBUNIT: Component of the heterotetrameric kinetochore subcomplex COMA,
CC which consists of AME1, CTF19, MCM21 and OKP1 (PubMed:29046335). The
CC COMA subcomplex is part of a larger constitutive centromere-associated
CC network (CCAN) (also known as central kinetochore CTF19 complex in
CC yeast) (By similarity). COMA binds the centromeric nucleosome-binding
CC protein MIF2, and to the outer kinetochore MIND subcomplex. OKP1
CC interacts directly with AME1, with an NKP1-NKP2 dimer, and with CTF19-
CC MCM21 (PubMed:29046335). {ECO:0000250|UniProtKB:P53298,
CC ECO:0000269|PubMed:29046335}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P53298}.
CC Chromosome, centromere, kinetochore {ECO:0000269|PubMed:29046335}.
CC -!- SIMILARITY: Belongs to the CENP-Q/OKP1 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; CR382126; CAG98467.1; -; Genomic_DNA.
DR RefSeq; XP_455759.1; XM_455759.1.
DR PDB; 5MU3; X-ray; 2.10 A; C/F=295-360.
DR PDBsum; 5MU3; -.
DR AlphaFoldDB; Q6CJY0; -.
DR SMR; Q6CJY0; -.
DR IntAct; Q6CJY0; 1.
DR MINT; Q6CJY0; -.
DR STRING; 28985.XP_455759.1; -.
DR EnsemblFungi; CAG98467; CAG98467; KLLA0_F15136g.
DR GeneID; 2896047; -.
DR KEGG; kla:KLLA0_F15136g; -.
DR eggNOG; ENOG502S031; Eukaryota.
DR HOGENOM; CLU_058662_0_0_1; -.
DR InParanoid; Q6CJY0; -.
DR OMA; GHDIDSE; -.
DR Proteomes; UP000000598; Chromosome F.
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:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
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..383
FT /note="Inner kinetochore subunit OKP1"
FT /id="PRO_0000443076"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 77..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 234..264
FT /note="Interaction with AME1"
FT /evidence="ECO:0000269|PubMed:29046335"
FT REGION 318..337
FT /note="CTF19-MCM21 binding motif"
FT /evidence="ECO:0000269|PubMed:29046335"
FT REGION 350..383
FT /note="Interaction with NKP1-NKP2"
FT /evidence="ECO:0000269|PubMed:29046335"
FT COILED 244..274
FT /evidence="ECO:0000255"
FT COMPBIAS 77..91
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 320..329
FT /evidence="ECO:0007829|PDB:5MU3"
SQ SEQUENCE 383 AA; 44886 MW; 48BD096F97D21E48 CRC64;
MSKRYLDDVL SPDTGTSDSD SSIENLNADN YRIDIVNDNA RRDDIDRIQS SNLNHEPPYN
LEGVFAIDDD EHGDEMVRKD SDRRQDITED NDDSFVPDIT TPPRERKRVR FGINEKGGDE
EFNNVSPWDF KRLIRKFYKE QLPDTYQIRN WKRPSKDMLT NFIDLIENNI ELASEEVFKQ
YHQELNQLYP DSEEQAKLKD SLENKVFDTT YNIKKRLKRT KVPSKIWVDN LNMEYIYAKG
ESIKKRYKSE LDRAEAIERQ LIREEEHLKS LQEKGETQAK KRKQVLSKEL SELSKTMHPS
LSVALSNTFG LIKDDKMSNE IYQQDKIDFN LKLKTDFSKP LISEKEENSL NGLTNAMDNN
RELVNEIFGK ISALLQPKKN SNE
