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Database: UniProt
Entry: DAM1_YARLI
LinkDB: DAM1_YARLI
Original site: DAM1_YARLI 
ID   DAM1_YARLI              Reviewed;         223 AA.
AC   Q6C2T8;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   24-JAN-2024, entry version 88.
DE   RecName: Full=DASH complex subunit DAM1;
DE   AltName: Full=Outer kinetochore protein DAM1;
GN   Name=DAM1; OrderedLocusNames=YALI0F05236g;
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150;
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 that connects microtubules with
CC       kinetochores and couples microtubule depolymerisation to chromosome
CC       movement; it is involved in retrieving kinetochores to the spindle
CC       poles before their re-orientation on the spindle in early mitosis and
CC       allows microtubule depolymerization to pull chromosomes apart and
CC       resist detachment during anaphase. Kinetochores, consisting of a
CC       centromere-associated inner segment and a microtubule-contacting outer
CC       segment, play a crucial role in chromosome segregation by mediating the
CC       physical connection between centromeric DNA and microtubules.
CC       Kinetochores also serve as an input point for the spindle assembly
CC       checkpoint, which delays anaphase until all chromosomes have bioriented
CC       on the mitotic spindle. {ECO:0000250|UniProtKB:P53267}.
CC   -!- SUBUNIT: Component of the DASH complex consisting of ASK1, DAD1, DAD2,
CC       DAD3, DAD4, DAM1, DUO1, HSK3, SPC19 and SPC34, with a stoichiometry of
CC       one copy of each subunit per complex. Multiple DASH complexes
CC       oligomerize to form a ring that encircles spindle microtubules and
CC       organizes the rod-like NDC80 complexes of the outer kinetochore. DASH
CC       complex oligomerization strengthens microtubule attachments. Within the
CC       complex, DAM1 and DUO1 may form the microtubule connections (By
CC       similarity). On cytoplasmic microtubules, DASH complexes appear to form
CC       patches instead of rings (By similarity). Interacts with the outer
CC       kinetochore component NDC80; the interaction is direct (By similarity).
CC       {ECO:0000250|UniProtKB:P53267, ECO:0000250|UniProtKB:Q9HDZ6}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P53267}.
CC       Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:P53267}.
CC       Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:P53267}.
CC   -!- SIMILARITY: Belongs to the DASH complex DAM1 family. {ECO:0000305}.
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DR   EMBL; CR382132; CAG77831.1; -; Genomic_DNA.
DR   RefSeq; XP_505024.1; XM_505024.1.
DR   AlphaFoldDB; Q6C2T8; -.
DR   SMR; Q6C2T8; -.
DR   STRING; 284591.Q6C2T8; -.
DR   EnsemblFungi; CAG77831; CAG77831; YALI0_F05236g.
DR   GeneID; 2908164; -.
DR   KEGG; yli:YALI0F05236g; -.
DR   VEuPathDB; FungiDB:YALI0_F05236g; -.
DR   HOGENOM; CLU_083960_0_0_1; -.
DR   InParanoid; Q6C2T8; -.
DR   OMA; AHGYGNS; -.
DR   OrthoDB; 1463832at2759; -.
DR   Proteomes; UP000001300; Chromosome F.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0042729; C:DASH complex; ISS:UniProtKB.
DR   GO; GO:1990537; C:mitotic spindle polar microtubule; IBA:GO_Central.
DR   GO; GO:0044732; C:mitotic spindle pole body; IBA:GO_Central.
DR   GO; GO:0008608; P:attachment of spindle microtubules to kinetochore; ISS:UniProtKB.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:1990758; P:mitotic sister chromatid biorientation; ISS:UniProtKB.
DR   GO; GO:1990976; P:protein transport along microtubule to mitotic spindle pole body; ISS:UniProtKB.
DR   InterPro; IPR013962; DASH_Dam1.
DR   PANTHER; PTHR28113; DASH COMPLEX SUBUNIT DAM1; 1.
DR   PANTHER; PTHR28113:SF1; DASH COMPLEX SUBUNIT DAM1; 1.
DR   Pfam; PF08653; DASH_Dam1; 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..223
FT                   /note="DASH complex subunit DAM1"
FT                   /id="PRO_0000127662"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          114..223
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          94..125
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        117..174
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   223 AA;  25253 MW;  539E2BB26DB87305 CRC64;
     MQRPTTPLRR SNSRQSDHEE HYPIVESVLD MAIGEQMAEL ADGMSALDRN LKDLQVIHTN
     LNNFNESFST LIYGLQMNAW CAEFHNGPRS CDFARRKEVE EMEERARRAQ MQAERDRMAM
     QQIQETPTRL PSEPSDGDVT YMRNDNSFII QPPSSYQSQL PSRIPQSSRA SRIRPPNSLR
     PPRGRGLYLR GGSRGVTGGR GSYTGVGRGS GRPASEGTTR RWL
//
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