CIN8_CANGA
ID CIN8_CANGA Reviewed; 988 AA.
AC Q6FXI5;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Kinesin-like protein CIN8;
GN Name=CIN8; OrderedLocusNames=CAGL0B03641g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
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: Required for assembly of the mitotic spindle. Interacts with
CC spindle microtubules to produce an outwardly directed force acting upon
CC the poles. Following spindle assembly, CIN8 and KIP1 apparently act to
CC oppose a force that draws separated poles back together. This force
CC seems to be mediated by KAR3 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle {ECO:0000250}.
CC Note=Spindle microtubules that lie between the poles. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. BimC subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00283}.
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DR EMBL; CR380948; CAG58030.1; -; Genomic_DNA.
DR RefSeq; XP_445130.1; XM_445130.1.
DR AlphaFoldDB; Q6FXI5; -.
DR SMR; Q6FXI5; -.
DR STRING; 5478.XP_445130.1; -.
DR EnsemblFungi; CAG58030; CAG58030; CAGL0B03641g.
DR GeneID; 2886646; -.
DR KEGG; cgr:CAGL0B03641g; -.
DR CGD; CAL0127858; CAGL0B03641g.
DR VEuPathDB; FungiDB:CAGL0B03641g; -.
DR eggNOG; KOG0243; Eukaryota.
DR HOGENOM; CLU_001485_33_3_1; -.
DR InParanoid; Q6FXI5; -.
DR OMA; QMNSKTY; -.
DR Proteomes; UP000002428; Chromosome B.
DR GO; GO:0000235; C:astral microtubule; IEA:EnsemblFungi.
DR GO; GO:0000776; C:kinetochore; IEA:EnsemblFungi.
DR GO; GO:0005828; C:kinetochore microtubule; IEA:EnsemblFungi.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR GO; GO:0008569; F:minus-end-directed microtubule motor activity; IEA:EnsemblFungi.
DR GO; GO:0008574; F:plus-end-directed microtubule motor activity; IEA:EnsemblFungi.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0000073; P:initial mitotic spindle pole body separation; IEA:EnsemblFungi.
DR GO; GO:0045144; P:meiotic sister chromatid segregation; IEA:EnsemblFungi.
DR GO; GO:0007019; P:microtubule depolymerization; IEA:EnsemblFungi.
DR GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR GO; GO:0033047; P:regulation of mitotic sister chromatid segregation; IEA:EnsemblFungi.
DR Gene3D; 3.40.850.10; -; 2.
DR InterPro; IPR019821; Kinesin_motor_CS.
DR InterPro; IPR001752; Kinesin_motor_dom.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00225; Kinesin; 2.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00129; KISc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell cycle; Cell division; Coiled coil; Cytoplasm;
KW Cytoskeleton; Microtubule; Mitosis; Motor protein; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..988
FT /note="Kinesin-like protein CIN8"
FT /id="PRO_0000125366"
FT DOMAIN 33..470
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 206..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 965..988
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 514..619
FT /evidence="ECO:0000255"
FT COILED 707..769
FT /evidence="ECO:0000255"
FT COMPBIAS 206..235
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..301
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 125..132
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 988 AA; 111387 MW; 77BC1A5B97CEFEBC CRC64;
MVVTTEAVTS RSERDAEPVQ EPLVEKLATE ELNILVAVRC RGRNEREIKA KSSVVVDVPD
NGVTNEVSIN TTDDVGIAAK MNSKTYTVDK VFGPSASQKL VYEEIAEPLF QDFIKGYNCT
ILVYGMTSTG KTYTMTGDEK LHNGELGDAA GIIPRVLFEL FDTLEANKDD YLVKCSFVEL
YNEELKDLLD STNTATNSDN KKLRIFDSNV NGTSASGSSS RSSSRNNSPR SAPDNSRAQM
LRRKLGRHNT TGNSKISNNN HNKFSRFKQT SQESTRAHAS NNHQNVHIPN NNSNNTNQQQ
SPIDQSASIY IQNLEEFHIT SAMEGLQLLQ KGLKQRQVAS TKMNDFSSRS HSIFTITLYK
EQNGELFRVS KMNLVDLAGS ENISRSGAMN QRAKEAGSIN QSLLTLGRVI NSLADKSEHI
PFRESKLTRL LQDSLGGNTK TALIATISPA KMTSEETCST LEYASKAKNI KNKPQLGAFI
MKDILVRSIT SELAKIKSDL LSTKSKEGVY MSHEHYKDLH YDIECYKTEL EESKRAIESL
TAQNAMLQQE RLSLKDDNAC YKANIASLKD NVVTLQSSLK EQITKETNIR SLLKDVQGAN
EEMKKTIHLF EFKQQELQQS ISTFISDEIS NIRDTLKKHI EYLQNNGDLK DTEISGNLMR
LEKEVVKVIK AAEEEASKSY GECVKMMLKE TPRLFESVSG RLDNISKLAE ENHSKIAETL
SDVSEEYNNL KQYLTNNFFK NNHEELLSHH VQNTYAQLEE NSAQLMQNFT MMLDKHIQEN
KRHMLENILG VTDEVINNEL QMFGEQRAKW EKSSALINQC DSVNHSFHQA LGSNLVEIRD
VVSSSRDNIG ATISSIQSRT RNRQSIEEMI QGNDVIRQQI TRIKQKNKSL SLFKEHSTET
ATTSIGSVNK VEGNLKVIMD KVLNDPQLSR GKAEVPDEEL HRLEKIPLGI TNKENVVDLQ
HRYPALQEKR KPEDEVLLQA KLQRRNPD
