CENPP_KLULA
ID CENPP_KLULA Reviewed; 270 AA.
AC Q6CRN7;
DT 13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 63.
DE RecName: Full=Inner kinetochore subunit CTF19;
DE AltName: Full=CENP-P homolog;
DE AltName: Full=Constitutive centromere-associated network protein CTF19;
GN Name=CTF19; OrderedLocusNames=KLLA0D07612g;
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 MCM21, 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 106-270 IN COMPLEX WITH MCM21 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:Q02732,
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:Q02732, ECO:0000269|PubMed:22322944,
CC ECO:0000269|PubMed:29046335}.
CC -!- INTERACTION:
CC Q6CRN7; Q6CVQ9: MCM21; NbExp=3; IntAct=EBI-7692007, EBI-7692022;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q02732}.
CC Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q02732}.
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-P/CTF19 family. {ECO:0000305}.
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DR EMBL; CR382124; CAH00498.1; -; Genomic_DNA.
DR RefSeq; XP_453402.1; XM_453402.1.
DR PDB; 3ZXU; X-ray; 3.90 A; B/D=1-270.
DR PDB; 5MU3; X-ray; 2.10 A; B/E=106-270.
DR PDBsum; 3ZXU; -.
DR PDBsum; 5MU3; -.
DR AlphaFoldDB; Q6CRN7; -.
DR SMR; Q6CRN7; -.
DR IntAct; Q6CRN7; 1.
DR MINT; Q6CRN7; -.
DR STRING; 28985.XP_453402.1; -.
DR EnsemblFungi; CAH00498; CAH00498; KLLA0_D07612g.
DR GeneID; 2893227; -.
DR KEGG; kla:KLLA0_D07612g; -.
DR HOGENOM; CLU_1030821_0_0_1; -.
DR InParanoid; Q6CRN7; -.
DR Proteomes; UP000000598; Chromosome D.
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..270
FT /note="Inner kinetochore subunit CTF19"
FT /id="PRO_0000417588"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 107..270
FT /note="D-RWD"
FT COILED 31..63
FT /evidence="ECO:0000255"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..30
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 108..119
FT /evidence="ECO:0007829|PDB:5MU3"
FT STRAND 123..127
FT /evidence="ECO:0007829|PDB:5MU3"
FT STRAND 130..135
FT /evidence="ECO:0007829|PDB:5MU3"
FT STRAND 138..147
FT /evidence="ECO:0007829|PDB:5MU3"
FT STRAND 150..160
FT /evidence="ECO:0007829|PDB:5MU3"
FT HELIX 162..175
FT /evidence="ECO:0007829|PDB:5MU3"
FT HELIX 178..205
FT /evidence="ECO:0007829|PDB:5MU3"
FT STRAND 212..218
FT /evidence="ECO:0007829|PDB:5MU3"
FT STRAND 221..228
FT /evidence="ECO:0007829|PDB:5MU3"
FT STRAND 237..244
FT /evidence="ECO:0007829|PDB:5MU3"
FT HELIX 246..256
FT /evidence="ECO:0007829|PDB:5MU3"
FT HELIX 258..267
FT /evidence="ECO:0007829|PDB:5MU3"
SQ SEQUENCE 270 AA; 30805 MW; 2B86807BAE9F2850 CRC64;
MDFTSSSGVL DSERNTGSND SDEPSSHSDV IETEELKLIK LQEHKNNLLR QRSELLDQLS
QTRVVEPRSV QLDDKLLLKL LRRNDNAVSD SSQSSNNPLP RVLPSLNIEQ RKKYLDITLN
DVTVTCEKDM ILLRKGSFTA SFRIAVENES IRSMAIDLNA FEVELQPIIQ YAEDTQNVNV
AMMAVVQFLR IKELHEQMIS KIVEASKFIR ASNNTITLND LEVSFHCYWN LPSPYPETLI
LTNKVQKILD FLIYQYGIQL GVIKYGSTII
