KLP3_SCHPO
ID KLP3_SCHPO Reviewed; 554 AA.
AC Q9US60; Q9US61;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Kinesin-like protein 3;
DE AltName: Full=Kinesin-related protein 1;
GN Name=klp3; Synonyms=krp1; ORFNames=SPAC1834.07;
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=10641037;
RX DOI=10.1002/(sici)1097-0061(20000130)16:2<149::aid-yea514>3.0.co;2-c;
RA Brazer S.-C.W., Williams H.P., Chappell T.G., Cande W.Z.;
RT "A fission yeast kinesin affects Golgi membrane recycling.";
RL Yeast 16:149-166(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=12132578;
RA Jeong J.W., Rhee D.K., Cho S.Y., Hae K.L., Kim D.U., Won M., Kim H.B.;
RT "Cloning and characterization of the kinesin-related protein, Krp1p, in
RT Schizosaccharomyces pombe.";
RL Mol. Cells 13:389-398(2002).
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: Cytoplasmic motor that could play a role in Golgi membrane
CC recycling. {ECO:0000269|PubMed:10641037}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:10641037}.
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; AF154055; AAF14525.1; -; mRNA.
DR EMBL; AF156966; AAF22609.1; -; mRNA.
DR EMBL; AF247188; AAF81205.1; -; Genomic_DNA.
DR EMBL; CU329670; CAB75775.1; -; Genomic_DNA.
DR PIR; T50118; T50118.
DR RefSeq; NP_594686.1; NM_001020115.2.
DR AlphaFoldDB; Q9US60; -.
DR SMR; Q9US60; -.
DR BioGRID; 278670; 20.
DR STRING; 4896.SPAC1834.07.1; -.
DR iPTMnet; Q9US60; -.
DR MaxQB; Q9US60; -.
DR PaxDb; Q9US60; -.
DR PRIDE; Q9US60; -.
DR EnsemblFungi; SPAC1834.07.1; SPAC1834.07.1:pep; SPAC1834.07.
DR GeneID; 2542195; -.
DR KEGG; spo:SPAC1834.07; -.
DR PomBase; SPAC1834.07; klp3.
DR VEuPathDB; FungiDB:SPAC1834.07; -.
DR eggNOG; KOG0240; Eukaryota.
DR HOGENOM; CLU_001485_2_1_1; -.
DR InParanoid; Q9US60; -.
DR OMA; EVKVSYM; -.
DR PhylomeDB; Q9US60; -.
DR PRO; PR:Q9US60; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005938; C:cell cortex; HDA:PomBase.
DR GO; GO:0005881; C:cytoplasmic microtubule; IDA:CACAO.
DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; IBA:GO_Central.
DR GO; GO:0008574; F:plus-end-directed microtubule motor activity; IBA:GO_Central.
DR GO; GO:0030705; P:cytoskeleton-dependent intracellular transport; IBA:GO_Central.
DR GO; GO:0071963; P:establishment or maintenance of cell polarity regulating cell shape; IMP:PomBase.
DR GO; GO:0006887; P:exocytosis; ISO:PomBase.
DR GO; GO:0006886; P:intracellular protein transport; IC:PomBase.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0000301; P:retrograde transport, vesicle recycling within Golgi; IMP:PomBase.
DR GO; GO:0010970; P:transport along microtubule; ISM: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; Reference proteome.
FT CHAIN 1..554
FT /note="Kinesin-like protein 3"
FT /id="PRO_0000125387"
FT DOMAIN 3..325
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT COILED 446..473
FT /evidence="ECO:0000255"
FT BINDING 84..91
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT BINDING 233..240
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT CONFLICT 57
FT /note="Q -> L (in Ref. 1; AAF14525)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 554 AA; 61938 MW; B4533BD095C49CBD CRC64;
MTSIKVVCRI RPTNQLEQDL GGNNVIYPLN DSTVHIETSD YSGNFVFDRV FHPSSTQNDI
FSYSIESTVD DLFLGYNGTV LAYGQTGSGK TYTMMGIENN FEKEGMTPRM LRRIFDKIRD
SPSTTEYEVK VSYMEIYMEK IHDLLSEKND RLTVHEDKLQ GVYVQGLKTI YVSSETEALD
ILNKGMGSRA VASTSMNAQS SRSHSIFVLE VVQTDTESGE TRRGRLFLVD LAGSESVGKS
GAVGQTLEEA KKINRSLSTL GMVINSLTDS KLSHVPYRDS KLTRILKESL GGNSRTTLII
NCSPDSYNAT ETLSTLRFGH RAKSIKNKAV VNSELSVDEM KRQLYIYKDA LSRCVCGARI
NNNLDYNNCH SNVWSGEHSL TLSNLAEKSN LKEAEIIQGN RTIQESNNDR DESTVASIHR
HNFDSDSINR LYAEAQLELK QRDGVLSSTK QQLSDLMTAL GDAQERYVEL VKNHRVNSNL
TANNSLNDKP GFTIEQKDKN FSINNERNNF LQKLSTLDSS LAALVNVQRK LIKALISKER
PQNGTVIKKI QGGT
