SPC34_KLULA
ID SPC34_KLULA Reviewed; 275 AA.
AC Q6CJ49;
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 SPC34;
DE AltName: Full=Outer kinetochore protein SPC34;
GN Name=SPC34; OrderedLocusNames=KLLA0F21428g;
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 SPC34 family. {ECO:0000305}.
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DR EMBL; CR382126; CAG98748.1; -; Genomic_DNA.
DR RefSeq; XP_456040.1; XM_456040.1.
DR AlphaFoldDB; Q6CJ49; -.
DR SMR; Q6CJ49; -.
DR STRING; 28985.XP_456040.1; -.
DR EnsemblFungi; CAG98748; CAG98748; KLLA0_F21428g.
DR GeneID; 2895447; -.
DR KEGG; kla:KLLA0_F21428g; -.
DR eggNOG; ENOG502QSS0; Eukaryota.
DR HOGENOM; CLU_970457_0_0_1; -.
DR InParanoid; Q6CJ49; -.
DR OMA; LIRDCNP; -.
DR Proteomes; UP000000598; Chromosome F.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0042729; C:DASH complex; IEA:EnsemblFungi.
DR GO; GO:0005876; C:spindle microtubule; 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; IPR013966; Spc34.
DR Pfam; PF08657; DASH_Spc34; 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..275
FT /note="DASH complex subunit SPC34"
FT /id="PRO_0000211552"
FT COILED 203..275
FT /evidence="ECO:0000255"
SQ SEQUENCE 275 AA; 31796 MW; AA9C45436F40AE64 CRC64;
MSGSLDYCLD QISKSAESIS TLYFKPPGIF RNAIVPGNSK VYSDLIVKLI RDGDSIEEMS
LYSTDNDGNM KRKDGKVGIY DHLLEREATL KRNRALCLPD PRPITYIPKG FYLSQNDHVI
RKKQKPARDF IFEGSNSDEL GIYDVLLKKF SKDEQIKQFL HALRNGSVIT GEDVSRRKTL
FVEDFPISII LSVFREIIDQ WPLTEYKEKF EKLMQIYNGL QADINELQKK VEIQELDFQH
EALPEKTSIS SLIDKEEKEI QKLEKQLDLL EGRNK