TEA2_SCHPO
ID TEA2_SCHPO Reviewed; 628 AA.
AC Q1MTQ1; O94732;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Kinesin-like protein tea2;
DE AltName: Full=Kinesin-like protein 4;
DE AltName: Full=Tip elongation aberrant protein 2;
GN Name=tea2 {ECO:0000312|EMBL:CAA22353.1};
GN Synonyms=klp4 {ECO:0000312|EMBL:CAA22353.1}; ORFNames=SPBC1604.20c;
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] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, AND SUBCELLULAR
RP LOCATION.
RX PubMed=11018050; DOI=10.1083/jcb.151.1.15;
RA Browning H., Hayles J., Mata J., Aveline L., Nurse P., McIntosh J.R.;
RT "Tea2p is a kinesin-like protein required to generate polarized growth in
RT fission yeast.";
RL J. Cell Biol. 151:15-28(2000).
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] {ECO:0000305, ECO:0000312|EMBL:BAA87207.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 339-545, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=ATCC 38364 / 968 {ECO:0000312|EMBL:BAA87207.1};
RX PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA Hiraoka Y.;
RT "Large-scale screening of intracellular protein localization in living
RT fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL Genes Cells 5:169-190(2000).
RN [4]
RP FUNCTION, INTERACTION WITH MAL3 AND TIP1, AND SUBCELLULAR LOCATION.
RX PubMed=15177031; DOI=10.1016/j.devcel.2004.05.008;
RA Busch K.E., Hayles J., Nurse P., Brunner D.;
RT "Tea2p kinesin is involved in spatial microtubule organization by
RT transporting tip1p on microtubules.";
RL Dev. Cell 6:831-843(2004).
RN [5] {ECO:0000305}
RP FUNCTION, AND INTERACTION WITH MAL3.
RX PubMed=15665379; DOI=10.1074/jbc.m413620200;
RA Browning H., Hackney D.D.;
RT "The EB1 homolog Mal3 stimulates the ATPase of the kinesin Tea2 by
RT recruiting it to the microtubule.";
RL J. Biol. Chem. 280:12299-12304(2005).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82, AND IDENTIFICATION BY
RP 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).
CC -!- FUNCTION: Promotes microtubule growth, possibly through interactions
CC with the microtubule end, and is important for establishing and
CC maintaining polarized growth along the long axis of the cell. Acts as a
CC kinesin motor protein that moves along microtubules and is required for
CC proper localization of tea1 and tip1 to the cell tips and microtubules,
CC respectively. ATPase activity stimulated via interaction with mal3.
CC {ECO:0000269|PubMed:11018050, ECO:0000269|PubMed:15177031,
CC ECO:0000269|PubMed:15665379}.
CC -!- SUBUNIT: Interacts with mal3 and tip1. {ECO:0000269|PubMed:15177031,
CC ECO:0000269|PubMed:15665379}.
CC -!- INTERACTION:
CC Q1MTQ1; Q10113: mal3; NbExp=3; IntAct=EBI-1107767, EBI-1002268;
CC Q1MTQ1; P79065: tip1; NbExp=6; IntAct=EBI-1107767, EBI-1102463;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:11018050,
CC ECO:0000269|PubMed:15177031}. Note=Localized in large clusters at cell
CC tips and also in punctate dots within the cell that are coincident with
CC the ends of cytoplasmic microtubules.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. {ECO:0000255|PROSITE-ProRule:PRU00283}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CU329671; CAA22353.1; -; Genomic_DNA.
DR EMBL; AB027903; BAA87207.1; -; Genomic_DNA.
DR PIR; T39494; T39494.
DR RefSeq; NP_596620.1; NM_001022541.2.
DR AlphaFoldDB; Q1MTQ1; -.
DR SMR; Q1MTQ1; -.
DR BioGRID; 276404; 129.
DR DIP; DIP-35717N; -.
DR IntAct; Q1MTQ1; 4.
DR STRING; 4896.SPBC1604.20c.1; -.
DR iPTMnet; Q1MTQ1; -.
DR MaxQB; Q1MTQ1; -.
DR PaxDb; Q1MTQ1; -.
DR PRIDE; Q1MTQ1; -.
DR EnsemblFungi; SPBC1604.20c.1; SPBC1604.20c.1:pep; SPBC1604.20c.
DR GeneID; 2539857; -.
DR KEGG; spo:SPBC1604.20c; -.
DR PomBase; SPBC1604.20c; tea2.
DR VEuPathDB; FungiDB:SPBC1604.20c; -.
DR eggNOG; KOG0242; Eukaryota.
DR HOGENOM; CLU_001485_24_1_1; -.
DR InParanoid; Q1MTQ1; -.
DR OMA; DTFQIRI; -.
DR PhylomeDB; Q1MTQ1; -.
DR PRO; PR:Q1MTQ1; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0051285; C:cell cortex of cell tip; IDA:PomBase.
DR GO; GO:0051286; C:cell tip; IDA:PomBase.
DR GO; GO:1903754; C:cortical microtubule plus-end; IDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0005881; C:cytoplasmic microtubule; IDA:PomBase.
DR GO; GO:1904511; C:cytoplasmic microtubule plus-end; IDA:PomBase.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:1990752; C:microtubule end; IDA:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
DR GO; GO:0008574; F:plus-end-directed microtubule motor activity; IDA:PomBase.
DR GO; GO:0071963; P:establishment or maintenance of cell polarity regulating cell shape; IMP:PomBase.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0099117; P:protein transport along microtubule to cell tip; 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 1: Evidence at protein level;
KW ATP-binding; Coiled coil; Cytoplasm; Cytoskeleton; Hydrolase; Microtubule;
KW Motor protein; Nucleotide-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..628
FT /note="Kinesin-like protein tea2"
FT /id="PRO_0000259608"
FT DOMAIN 132..460
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 2..122
FT /note="Interaction with mal3"
FT /evidence="ECO:0000269|PubMed:15665379"
FT REGION 21..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 588..628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 530..557
FT /evidence="ECO:0000255"
FT COMPBIAS 589..608
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 218..225
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT MOD_RES 82
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 628 AA; 70099 MW; 0C108D4B9690A6D3 CRC64;
MSSSSSKPVN TGLVTPRRYS TMTGIRTGPS QSGTGSIPYS PTSPLSRNFS NYSIPMLRSN
STQTNVNGPT AFDLGVTEKL MSPGTLDRYT RPALYPSKDL DYLKNEYVNY ESTTSQQTNS
KGLKESNFVG SGIITSIRIR PIGKNQGVWS HGKLSNDPYG REYIRQQTST SSSTIQQEYL
FNNVFGMESK NYDIYKRSVK SVVRNVFSGY NGIVFAYGMT GTGKTYSMQG TENEPGIIPL
AMNDLFEMVE NNSDDDTFQI RISYLEIYNE RIRDLIGNSD EEPRIRENAS GEVNVTPLTR
VLVTSPEEVS QVIEQCNAIR KTAATDFNTY SSRSHAILQV FLIRNNPTAH TSQISSLSLV
DLAGSERASA HHERRKEGAF INKSLLTLGT VISRLSAAAN PSLTSNSGHI PYRESKLTRL
LQQSLSGQSQ ISLLATISIE SNHTMETTNT LKFASRAQNL PQDIRQAEAV TNVQAELASL
HSALEKNAQE VEYYASLVKQ LTSDLEERDT YIAMLEAERS QGTAISRARL RMEELLSDHN
FEIADLRDEL QDKEQIIYAL RYAQKQRDIA DFNQSLAKFP HKILKKNVTR GSRSSSDQFS
NETKTEILPD DQQQSKKDSV TQETQLLS
