KLP9_SCHPO
ID KLP9_SCHPO Reviewed; 633 AA.
AC Q1MTQ7;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 2.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Kinesin-like motor protein 9;
GN Name=klp9; ORFNames=SPBC15D4.01c, SPBC2D10.21c;
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 [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 [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-605; SER-611 AND SER-613, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, AND INTERACTION WITH ASE1.
RX PubMed=19686686; DOI=10.1016/j.devcel.2009.06.012;
RA Fu C., Ward J.J., Loiodice I., Velve-Casquillas G., Nedelec F.J.,
RA Tran P.T.;
RT "Phospho-regulated interaction between kinesin-6 Klp9p and microtubule
RT bundler Ase1p promotes spindle elongation.";
RL Dev. Cell 17:257-267(2009).
CC -!- FUNCTION: Kinesin-like motor protein involved in anaphase B spindle
CC elongation. {ECO:0000269|PubMed:19686686}.
CC -!- SUBUNIT: Interacts with ase1. {ECO:0000269|PubMed:19686686}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytoskeleton, microtubule
CC organizing center, spindle pole body. Cytoplasm, cytoskeleton.
CC -!- PTM: Phosphorylated by cdc2 and dephosphorylated by clp1.
CC Dephosphorylation is required for the interaction with ase1.
CC {ECO:0000269|PubMed:18257517, ECO:0000269|PubMed:19686686}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. {ECO:0000255|PROSITE-ProRule:PRU00283}.
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DR EMBL; CU329671; CAA21179.2; -; Genomic_DNA.
DR RefSeq; XP_001713140.1; XM_001713088.2.
DR AlphaFoldDB; Q1MTQ7; -.
DR SMR; Q1MTQ7; -.
DR BioGRID; 276328; 9.
DR STRING; 4896.SPBC15D4.01c.1; -.
DR iPTMnet; Q1MTQ7; -.
DR MaxQB; Q1MTQ7; -.
DR PaxDb; Q1MTQ7; -.
DR PRIDE; Q1MTQ7; -.
DR EnsemblFungi; SPBC15D4.01c.1; SPBC15D4.01c.1:pep; SPBC15D4.01c.
DR PomBase; SPBC15D4.01c; klp9.
DR VEuPathDB; FungiDB:SPBC15D4.01c; -.
DR eggNOG; KOG0242; Eukaryota.
DR HOGENOM; CLU_429034_0_0_1; -.
DR InParanoid; Q1MTQ7; -.
DR OMA; IDGDHTF; -.
DR PhylomeDB; Q1MTQ7; -.
DR Reactome; R-SPO-68884; Mitotic Telophase/Cytokinesis.
DR PRO; PR:Q1MTQ7; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR GO; GO:1990385; C:meiotic spindle midzone; EXP:PomBase.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:1990023; C:mitotic spindle midzone; IDA:PomBase.
DR GO; GO:0005654; C:nucleoplasm; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:1990295; C:post-anaphase microtubule array; IDA:PomBase.
DR GO; GO:0005816; C:spindle pole body; IEA:UniProtKB-SubCell.
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; IBA:GO_Central.
DR GO; GO:0003777; F:microtubule motor activity; IMP:PomBase.
DR GO; GO:0008574; F:plus-end-directed microtubule motor activity; IDA:PomBase.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:1990758; P:mitotic sister chromatid biorientation; IGI:PomBase.
DR GO; GO:0000022; P:mitotic spindle elongation; IMP:PomBase.
DR GO; GO:0061805; P:mitotic spindle elongation (spindle phase three); IMP:PomBase.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR027640; Kinesin-like_fam.
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; PS50067; KINESIN_MOTOR_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Coiled coil; Cytoplasm; Cytoskeleton; Microtubule;
KW Motor protein; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..633
FT /note="Kinesin-like motor protein 9"
FT /id="PRO_0000353837"
FT DOMAIN 1..392
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 393..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 531..556
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 575..633
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 417..541
FT /evidence="ECO:0000255"
FT COMPBIAS 397..423
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 575..593
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 616..633
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 94..101
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT MOD_RES 605
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 611
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 613
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 633 AA; 71452 MW; 16EE7C0E5F557695 CRC64;
MIQIFLRVKK AQPSSDASNK YGFLTVLNDY EILLESPEDS HAYRVSKSKT LEKASFTKVF
PPSCTQLDVF STICAPLIAD SLVNMNDTLL FTLGVSGAGK TYTLFGPSDR PGVAFLALDA
LFYAIKGREA SPQTVEFLRS QLEKCKIVEA SKFLRGEAPL DIKVPNTEYY ASHFPKIEEK
NYQYAIYLSF AEIYNDRIFD LLEKASFFGH RHALSLKKSS TSDKKSIAGI QKVFVSNTTE
AYKLIQKVLQ LRKSTSTKSN SVSSRSHLIM SIELFKVCTK SNKFESCQID LVDLAGSERT
RSAETSGLLL REGASINRSL LTLGQCLEAL RRKHEGKQHI IPFRQSKLTE LLFHSGHLSG
LAGINMLVNI DPFGSFDENA QVMRYSANAR EILPPPLNEN SGSQSPSHSL LQKSKNTSST
KALTSHLEQL QQENQQLRML LADADSEMMN LEYEIRQQMT REMEERVSEV ERTFLTKLLE
ESAQGIEYTD QKLEKMGGWM KKLQDENSEK TETIAQLEQI IEELHEELRS LEEESIKESS
ATQQNENQHK RSSRKLLYED KQAIQEAHTI NTKRKLWPQS TLIQAPNSDD EENVPSPSPK
KKVVSPIKPL SPSRRPPLTS LYSGTTDIDI NEL
