KLP2_SCHPO
ID KLP2_SCHPO Reviewed; 817 AA.
AC Q9US03;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Kinesin-like protein 2;
GN Name=klp2; ORFNames=SPAC664.10;
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 / MRNA], FUNCTION, AND SUBCELLULAR
RP LOCATION.
RX PubMed=11694582; DOI=10.1091/mbc.12.11.3476;
RA Troxell C.L., Sweezy M.A., West R.R., Reed K.D., Carson B.D., Pidoux A.L.,
RA Cande W.Z., McIntosh J.R.;
RT "pkl1(+)and klp2(+): two kinesins of the Kar3 subfamily in fission yeast
RT perform different functions in both mitosis and meiosis.";
RL Mol. Biol. Cell 12:3476-3488(2001).
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 FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16002618; DOI=10.1126/science.1113465;
RA Carazo-Salas R.E., Antony C., Nurse P.;
RT "The kinesin Klp2 mediates polarization of interphase microtubules in
RT fission yeast.";
RL Science 309:297-300(2005).
CC -!- FUNCTION: Microtubule-dependent motor that is involved in microtubule
CC organization in the mitotic spindle. Required for the polarization of
CC interphase microtubules where it orients the microtubule plus ends
CC toward the cell ends and the minus ends toward the cell center.
CC Mediates minus end-directed sliding of cytoplasmic microtubules
CC relative to each other, thereby promoting mitotic spindle disassembly.
CC {ECO:0000269|PubMed:11694582, ECO:0000269|PubMed:16002618}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Nucleus. Note=During
CC interphase. When in the nucleus, it associates with chromatin.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. NCD subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00283}.
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DR EMBL; CU329670; CAB65811.1; -; Genomic_DNA.
DR PIR; T50240; T50240.
DR RefSeq; NP_593458.1; NM_001018891.2.
DR AlphaFoldDB; Q9US03; -.
DR SMR; Q9US03; -.
DR BioGRID; 279782; 16.
DR STRING; 4896.SPAC664.10.1; -.
DR iPTMnet; Q9US03; -.
DR MaxQB; Q9US03; -.
DR PaxDb; Q9US03; -.
DR PRIDE; Q9US03; -.
DR EnsemblFungi; SPAC664.10.1; SPAC664.10.1:pep; SPAC664.10.
DR GeneID; 2543360; -.
DR KEGG; spo:SPAC664.10; -.
DR PomBase; SPAC664.10; klp2.
DR VEuPathDB; FungiDB:SPAC664.10; -.
DR eggNOG; KOG0239; Eukaryota.
DR HOGENOM; CLU_001485_12_1_1; -.
DR InParanoid; Q9US03; -.
DR OMA; WEYRMEG; -.
DR PhylomeDB; Q9US03; -.
DR PRO; PR:Q9US03; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0000235; C:astral microtubule; IDA:PomBase.
DR GO; GO:0055028; C:cortical microtubule; IDA:PomBase.
DR GO; GO:0005881; C:cytoplasmic microtubule; IDA:PomBase.
DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR GO; GO:0000776; C:kinetochore; IDA:PomBase.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0015630; C:microtubule cytoskeleton; HDA:PomBase.
DR GO; GO:0036449; C:microtubule minus-end; IDA:PomBase.
DR GO; GO:0005815; C:microtubule organizing center; IBA:GO_Central.
DR GO; GO:0035371; C:microtubule plus-end; IDA:PomBase.
DR GO; GO:0005872; C:minus-end kinesin complex; IDA:PomBase.
DR GO; GO:0072686; C:mitotic spindle; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0005524; F:ATP binding; ISM:PomBase.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0008017; F:microtubule binding; IDA:PomBase.
DR GO; GO:0003777; F:microtubule motor activity; IBA:GO_Central.
DR GO; GO:0008569; F:minus-end-directed microtubule motor activity; IDA:PomBase.
DR GO; GO:0008574; F:plus-end-directed microtubule motor activity; IDA:PomBase.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; IMP:PomBase.
DR GO; GO:0030951; P:establishment or maintenance of microtubule cytoskeleton polarity; IMP:PomBase.
DR GO; GO:0000742; P:karyogamy involved in conjugation with cellular fusion; IGI:PomBase.
DR GO; GO:1990571; P:meiotic centromere clustering; IMP:PomBase.
DR GO; GO:0140642; P:meiotic spindle formation (spindle phase two); IMP:PomBase.
DR GO; GO:1990810; P:microtubule anchoring at mitotic spindle pole body; IGI:PomBase.
DR GO; GO:0001578; P:microtubule bundle formation; IDA:PomBase.
DR GO; GO:0051012; P:microtubule sliding; IMP:PomBase.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0031534; P:minus-end directed microtubule sliding; IMP:PomBase.
DR GO; GO:1990942; P:mitotic metaphase chromosome recapture; IMP:PomBase.
DR GO; GO:0090307; P:mitotic spindle assembly; IBA:GO_Central.
DR GO; GO:0000022; P:mitotic spindle elongation; IMP:PomBase.
DR GO; GO:0140641; P:mitotic spindle formation (spindle phase two); IMP:PomBase.
DR GO; GO:0051256; P:mitotic spindle midzone assembly; IDA:PomBase.
DR GO; GO:0090561; P:nuclear migration during mitotic telophase; IGI:PomBase.
DR GO; GO:0031535; P:plus-end directed microtubule sliding; IDA:PomBase.
DR Gene3D; 3.40.850.10; -; 1.
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; 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 3: Inferred from homology;
KW ATP-binding; Coiled coil; Cytoplasm; Cytoskeleton; Microtubule;
KW Motor protein; Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..817
FT /note="Kinesin-like protein 2"
FT /id="PRO_0000125386"
FT DOMAIN 473..807
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 1..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 155..242
FT /evidence="ECO:0000255"
FT COMPBIAS 10..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..136
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 563..570
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 817 AA; 91043 MW; 804677851AF1A52D CRC64;
MEEEGHKSLT SHLPQSSSSL SQSREIAKEF TSNIPPPTIK TNSSSSNILK PRLSLQNEVN
QLKPAKFPSK MLPPGSLASV KSSSLAKKAR PFTASSNPRM PKSAHPISSR SVSASSHFGR
PASAVSSSLN SSDDVRSMSD ESMESYNDEK SVNASALRTT EDRLRSMEMA YAQLSAKVIP
SPSKRPANYK FYEQRIAMLE ESLEVERSRT SELQEQFSVA LREKAEAEAN KIVSQKGMES
LEIMLNSMKS ENHQRMAMLE ENHARVMETA ELQHQAELQD FASNIEQKAN SLIMEYKNEL
QSAEEHFSHK IKELTSENEL KISRLQEEKD SLLKKVQEGA SLAMQRVQNK HDLEKKRLQS
AIQPLQEENN SLKQQIEQLQ RELASETVVK ENLKSSLDQQ SANVQKLEST NRALESTIKT
LEEDVYTMKN KIIELEGILK SANVERDGLV EKLIAEETLR RKLHNTIQEL KGNIRVFCRV
RPPLGDGESA QIAFPDQNSE ASTIEIVAQA PGSSLTGNGI KQYAFNFDRV FSPETTNEDV
FNELSQLIQS AMDGYNVCIF AYGQTGSGKT HTMSSNTGMI PSSVRMIYNR STSLKERGWE
YRMEGQFLEI YNETIIDLLA SGNEEEKGKK KLEIYHDTKA GRTTITNITS EPLDTPEQVT
WLLDQASKNR SVAATNANEH SSRSHSVFML HLNGSNSTTG ETCRSTLNLI DLAGSERLSS
SQSVGERLKE TQAINKSLSC LGDVIHALGS GKEGTYIPYR NSKLTNLLQY SLGGNSKTLM
FVNISPLKQH VPETLCSLRF ATKVNNTQIG TARKVTK
