DAD2_KLULA
ID DAD2_KLULA Reviewed; 132 AA.
AC Q6CXI8;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 85.
DE RecName: Full=DASH complex subunit DAD2;
DE AltName: Full=Outer kinetochore protein DAD2;
GN Name=DAD2; OrderedLocusNames=KLLA0A07887g;
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).
CC -!- FUNCTION: Component of the DASH complex, a microtubule-binding
CC subcomplex of the outer kinetochore that is essential for proper
CC chromosome segregation. The DASH complex mediates the formation and
CC maintenance of bipolar kinetochore-microtubule attachments by forming
CC closed rings around spindle microtubules and establishing interactions
CC with proteins from the central kinetochore (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: The DASH complex oligomerizes to form rings that encircle the
CC microtubules. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm, cytoskeleton,
CC spindle {ECO:0000250}. Chromosome, centromere, kinetochore
CC {ECO:0000250}. Note=Associates with the mitotic spindle and the
CC kinetochore. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DASH complex DAD2 family. {ECO:0000305}.
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DR EMBL; CR382121; CAH02939.1; -; Genomic_DNA.
DR RefSeq; XP_451351.1; XM_451351.1.
DR AlphaFoldDB; Q6CXI8; -.
DR SMR; Q6CXI8; -.
DR STRING; 28985.XP_451351.1; -.
DR EnsemblFungi; CAH02939; CAH02939; KLLA0_A07887g.
DR GeneID; 2896437; -.
DR KEGG; kla:KLLA0_A07887g; -.
DR eggNOG; ENOG502S93M; Eukaryota.
DR HOGENOM; CLU_138063_1_0_1; -.
DR InParanoid; Q6CXI8; -.
DR OMA; DYEVGVW; -.
DR Proteomes; UP000000598; Chromosome A.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0042729; C:DASH complex; IEA:EnsemblFungi.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0072686; C:mitotic spindle; IEA:InterPro.
DR GO; GO:0051010; F:microtubule plus-end binding; IEA:EnsemblFungi.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:1990758; P:mitotic sister chromatid biorientation; IEA:EnsemblFungi.
DR GO; GO:0051987; P:positive regulation of attachment of spindle microtubules to kinetochore; IEA:EnsemblFungi.
DR GO; GO:0031116; P:positive regulation of microtubule polymerization; IEA:EnsemblFungi.
DR InterPro; IPR013963; DASH_Dad2.
DR PANTHER; PTHR28036; PTHR28036; 1.
DR Pfam; PF08654; DASH_Dad2; 1.
PE 3: Inferred from homology;
KW Cell cycle; Cell division; Centromere; Chromosome; Chromosome partition;
KW Coiled coil; Cytoplasm; Cytoskeleton; Kinetochore; Microtubule; Mitosis;
KW Nucleus; Reference proteome.
FT CHAIN 1..132
FT /note="DASH complex subunit DAD2"
FT /id="PRO_0000211595"
FT REGION 81..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 21..50
FT /evidence="ECO:0000255"
FT COMPBIAS 81..95
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 132 AA; 14980 MW; 4F7B2F9C797A0076 CRC64;
MAFETEIETK RRELNYLKHV SALTQKLKAQ LDELSVQVAQ MNSNAVTVKD VMANWDSVLR
SISQASISLL QYTENDYETG KWASKEEHRN QQGAEDESAA SESSEDNQQR QQDQLPPLPE
TLVRVKVADD VE