DAD2_ASHGO
ID DAD2_ASHGO Reviewed; 111 AA.
AC Q759Q6;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 87.
DE RecName: Full=DASH complex subunit DAD2;
DE AltName: Full=Outer kinetochore protein DAD2;
GN Name=DAD2; OrderedLocusNames=ADR217C;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
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; AE016817; AAS52137.1; -; Genomic_DNA.
DR RefSeq; NP_984313.1; NM_209666.2.
DR AlphaFoldDB; Q759Q6; -.
DR SMR; Q759Q6; -.
DR STRING; 33169.AAS52137; -.
DR EnsemblFungi; AAS52137; AAS52137; AGOS_ADR217C.
DR GeneID; 4620475; -.
DR KEGG; ago:AGOS_ADR217C; -.
DR eggNOG; ENOG502S93M; Eukaryota.
DR HOGENOM; CLU_138063_1_0_1; -.
DR InParanoid; Q759Q6; -.
DR OMA; DYEVGVW; -.
DR Proteomes; UP000000591; Chromosome IV.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0042729; C:DASH complex; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:1990023; C:mitotic spindle midzone; IBA:GO_Central.
DR GO; GO:0044732; C:mitotic spindle pole body; IBA:GO_Central.
DR GO; GO:0051010; F:microtubule plus-end binding; IEA:EnsemblFungi.
DR GO; GO:0008608; P:attachment of spindle microtubules to kinetochore; IBA:GO_Central.
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..111
FT /note="DASH complex subunit DAD2"
FT /id="PRO_0000211591"
FT REGION 80..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 17..48
FT /evidence="ECO:0000255"
SQ SEQUENCE 111 AA; 12479 MW; DED9D54724E23025 CRC64;
MVPEDVYQSK KSELLYLQKV TGLTDTLKAQ LDELSKQVHQ MHDNAECVSS VLKNWDSILN
SISQATLSLL QYTENDYEVG AWSNGSRPEA DKEPPLPETL VRVNVANESQ E