KLP1_SCHPO
ID KLP1_SCHPO Reviewed; 832 AA.
AC Q92376; O42669;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Kinesin-like protein 1;
GN Name=klp1; Synonyms=pkl1; ORFNames=SPAC3A11.14c;
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 [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=972 / ATCC 24843;
RX PubMed=8898367; DOI=10.1091/mbc.7.10.1639;
RA Pidoux A.L., Ledizet M., Cande W.Z.;
RT "Fission yeast pkl1 is a kinesin-related protein involved in mitotic
RT spindle function.";
RL Mol. Biol. Cell 7:1639-1655(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBCELLULAR 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 [3]
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: Microtubule-dependent motor that is involved in microtubule
CC organization in the mitotic spindle. {ECO:0000269|PubMed:8898367}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytoskeleton {ECO:0000305}.
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; U63916; AAB88235.1; -; mRNA.
DR EMBL; CU329670; CAB16597.1; -; Genomic_DNA.
DR PIR; T38749; T38749.
DR RefSeq; NP_594189.1; NM_001019613.2.
DR AlphaFoldDB; Q92376; -.
DR SMR; Q92376; -.
DR BioGRID; 279109; 14.
DR STRING; 4896.SPAC3A11.14c.1; -.
DR iPTMnet; Q92376; -.
DR MaxQB; Q92376; -.
DR PaxDb; Q92376; -.
DR PRIDE; Q92376; -.
DR EnsemblFungi; SPAC3A11.14c.1; SPAC3A11.14c.1:pep; SPAC3A11.14c.
DR GeneID; 2542655; -.
DR KEGG; spo:SPAC3A11.14c; -.
DR PomBase; SPAC3A11.14c; -.
DR VEuPathDB; FungiDB:SPAC3A11.14c; -.
DR eggNOG; KOG0239; Eukaryota.
DR HOGENOM; CLU_001485_12_1_1; -.
DR InParanoid; Q92376; -.
DR PhylomeDB; Q92376; -.
DR PRO; PR:Q92376; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0000776; C:kinetochore; IDA:PomBase.
DR GO; GO:0090619; C:meiotic spindle pole; EXP:PomBase.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0072686; C:mitotic spindle; IDA:PomBase.
DR GO; GO:0044732; C:mitotic spindle pole body; IDA:PomBase.
DR GO; GO:1990811; C:MWP complex; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008017; F:microtubule binding; IDA:PomBase.
DR GO; GO:0003777; F:microtubule motor activity; IDA:PomBase.
DR GO; GO:0008569; F:minus-end-directed microtubule motor activity; IDA:PomBase.
DR GO; GO:0000742; P:karyogamy involved in conjugation with cellular fusion; IGI:PomBase.
DR GO; GO:1990810; P:microtubule anchoring at mitotic spindle pole body; IMP:PomBase.
DR GO; GO:0001578; P:microtubule bundle formation; IDA:PomBase.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; IGI:PomBase.
DR GO; GO:0090307; P:mitotic spindle assembly; IGI:PomBase.
DR GO; GO:1990976; P:protein transport along microtubule to mitotic spindle pole body; 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 2: Evidence at transcript level;
KW ATP-binding; Coiled coil; Cytoplasm; Cytoskeleton; Microtubule;
KW Motor protein; Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..832
FT /note="Kinesin-like protein 1"
FT /id="PRO_0000125385"
FT DOMAIN 479..822
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT COILED 193..266
FT /evidence="ECO:0000255"
FT COILED 284..305
FT /evidence="ECO:0000255"
FT COILED 344..481
FT /evidence="ECO:0000255"
FT BINDING 575..582
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT CONFLICT 343
FT /note="E -> D (in Ref. 1; AAB88235)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 832 AA; 96337 MW; 870CF74224B9F3E4 CRC64;
MVIENTKDIS INTGYKRQED ALNTDSEDLI YRPKKIIKTN QEDAVHDLKY ENFVSKNHVL
QSDINGKKRD SNRDKAAVVT APIASTHESN YEESVSKFKE SWLPQLKDLI ESHKTICEST
LAYESDQAMA SSNTLKRIKD LKSKPKNIIQ LERLHMLSNG EHRLLSKDET DDIESAYLNL
RSHLQVQEQV YAEKDHEYSL QLQSYREAAE KAKQDILETK ENLSSELSIS NIQLKEAKER
LEAANASYQK LRREHKELAL YHEKKTHSLV CNLNGERKSF GDFVENEVKS YKHEYANICE
SLRRALVLIQ GSCTEKILRF KEKILDLLEM KQQEENDRIS HIEYENDLTV KKLKRRISEL
EMAVKEYESE KSYSEKEYEE KISSLRIELE DKLAEIDMLR NKLLKEEHKH HSTSEKLEEL
SKYVASIQDK ERNNGQNALE LQARIQQLER RNEDMYNKLL AEEIIRRKLH NDIQELKGNI
RVFCRVRPLL PSEESEYCIA DVLQFPDKDA LEPQKLILKG PNVESSLGHT YDRNYEFSFD
RVFAPESDNS SVFEEISQLI QSAIDGYNVS IFAYGQTGSG KTYTMSSQDG MIAMSIKHIF
NYLSTLREKG WVYKLRGQFL EIYNETIYDL LNKAEMLKNP KHDIHHDEKE RRTTVDNVSI
IDFNEEDTVY KMLNRAGENR FIAATKANER SSRSHTVFML YIDGENSRTK QICKGTLNLV
DLAGSERLSY SQAVGDRLRE TQAINKSLSC LGDVIHALGN ASNSTTKEKS HIPYRNSKLT
YLLKYSLGKG AKTLMFVNVS PLKSQFMDTL NSLRFATKVN DTKVGSIKHY KR
