KLP5_SCHPO
ID KLP5_SCHPO Reviewed; 883 AA.
AC O14343;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Kinesin-like protein 5;
GN Name=klp5; ORFNames=SPBC2F12.13;
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 KLP6, 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).
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 klp6.
CC -!- INTERACTION:
CC O14343; O59751: klp6; NbExp=3; IntAct=EBI-1561765, EBI-1561745;
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; AB072924; BAB69885.1; -; Genomic_DNA.
DR EMBL; CU329671; CAB10160.1; -; Genomic_DNA.
DR PIR; T40128; T40128.
DR RefSeq; NP_595703.1; NM_001021600.2.
DR AlphaFoldDB; O14343; -.
DR SMR; O14343; -.
DR BioGRID; 276890; 64.
DR IntAct; O14343; 2.
DR STRING; 4896.SPBC2F12.13.1; -.
DR iPTMnet; O14343; -.
DR MaxQB; O14343; -.
DR PaxDb; O14343; -.
DR PRIDE; O14343; -.
DR EnsemblFungi; SPBC2F12.13.1; SPBC2F12.13.1:pep; SPBC2F12.13.
DR GeneID; 2540361; -.
DR KEGG; spo:SPBC2F12.13; -.
DR PomBase; SPBC2F12.13; klp5.
DR VEuPathDB; FungiDB:SPBC2F12.13; -.
DR eggNOG; KOG0242; Eukaryota.
DR HOGENOM; CLU_001485_21_1_1; -.
DR InParanoid; O14343; -.
DR OMA; RNMISVD; -.
DR PhylomeDB; O14343; -.
DR PRO; PR:O14343; -.
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:0005829; C:cytosol; TAS:Reactome.
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:0051301; P:cell division; IEA:UniProtKB-KW.
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:0099607; P:lateral attachment of mitotic spindle microtubules to kinetochore; 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: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..883
FT /note="Kinesin-like protein 5"
FT /id="PRO_0000125388"
FT DOMAIN 6..390
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 755..785
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 396..435
FT /evidence="ECO:0000255"
FT COILED 563..588
FT /evidence="ECO:0000255"
FT COMPBIAS 767..781
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 144..151
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 883 AA; 99059 MW; BB8A60E22DA397E8 CRC64;
MSRQSSITVT VRVRPFSTAE SANLIASSDR LSFGTSSSLR NPGSGRQIRR VVKVLDGRVL
VFDPPDETTA TLSATNRRLS TSQQSLARLS RKSNNSAGFG RDLRYAFDRV FDETATQQQV
YERTARPLLD NILDGFNATI FAYGATGCGK THTISGTMQD PGLIYLTLKE LFERMDHLRD
EKIFDLRLSY LEIYNETIRD LLVSPTPNQA KPLNLREDAD RRITVPGLTS LSPESLEEII
DIIMKGNANR TMSPTEANAA SSRSHAVLQV TLIQKPRTAG INEDHTLATL SIIDLAGSER
ATATKLRGSR LFEGANINKS LLALGNCINA LCDPHRRAHV PYRDSKLTRL LKFSLGGNCR
TVMIVCVSPS SVHYEETHNT LKYANRAKNI KTEVLRNMIS VDRHVSQYVK AIVELREQIS
ELENRLAQID LSSQSNGSDQ DAVTQSFAHE SKLAEARNLL RMTFEETLPL QNDTINKVEK
VKHFDDSIRV LKYWLSCYER ILPNSADERV FLVRSKLESL LTRRAEIIAD IDPELVYQKF
QRSVSHIINT YKQEGATMYA DVLQDEVDLL KSIIENQVLD AQNKVDEFTP VLESLLRSSF
KASSLLKEGG MQELFSILEK WLLGIGLGEK PNISVLSESY KLNSTSDDSR TINRDRVHSF
PTQPLLNNNL PRMFFVKSPK KPVVFSKRSP KKRVRFDDSM STSDSGASAY NSPIQTSKLK
NMNFFNTMHM PSTPAHKRPE NKNQIDVEIN LTSPVSPMLE DKPEPGLLIK SPLEKKQEVN
SESTQLDQLL AEDSSTDDVS LPHLDTIDLD GSPVPKVPDL NFSRANMDSP TFILNNEAIH
NFDFSKPKTR QSLSSLTTLH LSNPANIIRK SLSMAENEEE KAT
