KLP6_SCHPO
ID KLP6_SCHPO Reviewed; 784 AA.
AC O59751; Q9UTZ7;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Kinesin-like protein 6;
GN Name=klp6; ORFNames=SPBC1685.15c, SPBC649.01c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INTERACTION WITH KLP5, AND
RP SUBCELLULAR LOCATION.
RX PubMed=11967147; DOI=10.1016/s0960-9822(02)00761-3;
RA Garcia M.A., Koonrugsa N., Toda T.;
RT "Two kinesin-like Kin I family proteins in fission yeast regulate the
RT establishment of metaphase and the onset of anaphase A.";
RL Curr. Biol. 12:610-621(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 233-464.
RC STRAIN=ATCC 38364 / 968;
RX PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA Hiraoka Y.;
RT "Large-scale screening of intracellular protein localization in living
RT fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL Genes Cells 5:169-190(2000).
CC -!- FUNCTION: Has a role in establishing metaphase during mitosis. Required
CC for chromosome segregation where it generates tension during
CC kinetochore capturing. {ECO:0000269|PubMed:11967147}.
CC -!- SUBUNIT: Heterodimer with klp5.
CC -!- INTERACTION:
CC O59751; O14343: klp5; NbExp=3; IntAct=EBI-1561745, EBI-1561765;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11967147}.
CC Cytoplasm, cytoskeleton {ECO:0000269|PubMed:11967147}. Chromosome,
CC centromere, kinetochore {ECO:0000269|PubMed:11967147}. Cytoplasm,
CC cytoskeleton, spindle {ECO:0000269|PubMed:11967147}. Note=Cytoplasmic
CC microtubules in interphase, mitotic kinetochores in metaphase and
CC spindle midzone in anaphase and telophase.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. Kinesin II subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00283}.
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DR EMBL; AB072925; BAB69886.1; -; Genomic_DNA.
DR EMBL; CU329671; CAA20063.1; -; Genomic_DNA.
DR EMBL; AB027906; BAA87210.1; -; Genomic_DNA.
DR PIR; T40594; T40594.
DR RefSeq; XP_001713122.1; XM_001713070.2.
DR AlphaFoldDB; O59751; -.
DR SMR; O59751; -.
DR BioGRID; 276253; 142.
DR IntAct; O59751; 1.
DR STRING; 4896.SPBC1685.15c.1; -.
DR iPTMnet; O59751; -.
DR MaxQB; O59751; -.
DR PaxDb; O59751; -.
DR PRIDE; O59751; -.
DR EnsemblFungi; SPBC1685.15c.1; SPBC1685.15c.1:pep; SPBC1685.15c.
DR PomBase; SPBC1685.15c; klp6.
DR VEuPathDB; FungiDB:SPBC1685.15c; -.
DR eggNOG; KOG0242; Eukaryota.
DR HOGENOM; CLU_001485_21_1_1; -.
DR InParanoid; O59751; -.
DR OMA; EYVRVIY; -.
DR PhylomeDB; O59751; -.
DR PRO; PR:O59751; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0055028; C:cortical microtubule; IDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:1904511; C:cytoplasmic microtubule plus-end; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR GO; GO:0016938; C:kinesin I complex; IPI:PomBase.
DR GO; GO:0000776; C:kinetochore; IDA:PomBase.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:PomBase.
DR GO; GO:0072686; C:mitotic spindle; IDA:PomBase.
DR GO; GO:0061673; C:mitotic spindle astral microtubule; IDA:PomBase.
DR GO; GO:1990023; C:mitotic spindle midzone; IDA:PomBase.
DR GO; GO:0044732; C:mitotic spindle pole body; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0005873; C:plus-end kinesin complex; IPI:PomBase.
DR GO; GO:1990295; C:post-anaphase microtubule array; IDA:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:PomBase.
DR GO; GO:0008017; F:microtubule binding; IDA:PomBase.
DR GO; GO:0003777; F:microtubule motor activity; IBA:GO_Central.
DR GO; GO:0008574; F:plus-end-directed microtubule motor activity; IDA:PomBase.
DR GO; GO:0010938; P:cytoplasmic microtubule depolymerization; IMP:PomBase.
DR GO; GO:1902426; P:deactivation of mitotic spindle assembly checkpoint; IMP:PomBase.
DR GO; GO:0007019; P:microtubule depolymerization; IMP:PomBase.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:1903475; P:mitotic actomyosin contractile ring assembly; IMP:PomBase.
DR GO; GO:0007079; P:mitotic chromosome movement towards spindle pole; EXP:PomBase.
DR GO; GO:1990942; P:mitotic metaphase chromosome recapture; IMP:PomBase.
DR GO; GO:1990758; P:mitotic sister chromatid biorientation; IMP:PomBase.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; IMP:PomBase.
DR GO; GO:0007052; P:mitotic spindle organization; IMP:PomBase.
DR GO; GO:0070462; P:plus-end specific microtubule depolymerization; IDA:PomBase.
DR GO; GO:0140210; P:protein transport along microtubule to kinetochore; IMP:PomBase.
DR GO; GO:0032888; P:regulation of mitotic spindle elongation; IMP:PomBase.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR027640; Kinesin-like_fam.
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 PANTHER; PTHR24115; PTHR24115; 1.
DR Pfam; PF00225; Kinesin; 1.
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 1: Evidence at protein level;
KW ATP-binding; Cell cycle; Cell division; Centromere; Chromosome;
KW Chromosome partition; Coiled coil; Cytoplasm; Cytoskeleton; Kinetochore;
KW Microtubule; Mitosis; Motor protein; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..784
FT /note="Kinesin-like protein 6"
FT /id="PRO_0000125389"
FT DOMAIN 6..389
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 677..715
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 405..440
FT /evidence="ECO:0000255"
FT COILED 463..483
FT /evidence="ECO:0000255"
FT COMPBIAS 691..708
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 134..141
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 784 AA; 87796 MW; EBE985FF79C18BB6 CRC64;
MKEGSSISVA VRVRPFTERE KGLLAETPKS KEFLGDGSLA VSNTSSNTFC TNGIRKIVRV
LDDNVLIFDP PEENPLAKVQ KSLLPAGKRF RDVRYAFDRL FGEEASQEDV YKGTTEPLLD
SVLQGYNATV FAYGATGCGK THTISGRPDD PGIIFLTMRA LLDRVEGLKR TMNVDISVSY
LEIYNEKIRD LLVQDPLSME KPKSLNICED AEQNVSVPGL SYFTPTNLEE VMEIIIRGNS
NRTMSPTEAN AVSSRSHAVL QIYITQTPKS GEKQEESESQ NSHKVRSVFS FIDLAGSERA
SATKNRGKRL VEGANINRSL LALGNCINSL CEPRRRQHVP YRDSKLTRLL KFSLGGNCRT
CMIVCISPSS EHYDETHNTL KYGNRAKNIK TKVSRNVVSV DRHVSEYVRT IYELRQKVSI
LQKRIAEESK QLALNKEVRK ISSREIKMLD ARSMLKNSFD GSRDLQKSLI EHVRTLRRIE
DEITLTKMWI SIAKESDAMS GHNIKSVETR LAKLYDQRSL ITAKVNPEEI CKTFQNSISH
IVSSFKGEGA DMYADMLQDD VDLLKSIIEN QILDAKHESE TFSSTSRKLI QNLFLLFPLL
PGNAIDVNES LARAFDQLVG IVPSEPTIQV PNLIEKGKAP LLSMFEIPRS PSRFKARSPS
KAARVLKKPL KKRVRFSEVP TTSSVPPVEI KNKDSKPKVE KSLDKHNMNN DRSFLVPSRD
ARNSLTSLSL HSNVAKNKSS HSSKWPTHTL SPIITTALKQ PVRRISLVSQ PLQKTGGTEN
TPNA
