MYO2_SCHPO
ID MYO2_SCHPO Reviewed; 1526 AA.
AC Q9USI6; P78969;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Myosin type-2 heavy chain 1;
DE AltName: Full=Myosin type II heavy chain 1;
GN Name=myo2; ORFNames=SPCC645.05c;
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], AND FUNCTION.
RC STRAIN=972 / ATCC 24843;
RX PubMed=9415380;
RX DOI=10.1002/(sici)1097-0169(1997)38:4<385::aid-cm8>3.0.co;2-2;
RA May K.M., Watts F.Z., Jones N., Hyams J.S.;
RT "Type II myosin involved in cytokinesis in the fission yeast,
RT Schizosaccharomyces pombe.";
RL Cell Motil. Cytoskeleton 38:385-396(1997).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1044, 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: Required for cell division. It is a component of the cdc12
CC 'spot', a structure thought to mark the site of septation. May work in
CC conjunction with myo3. {ECO:0000269|PubMed:9415380}.
CC -!- SUBUNIT: Binds to cdc4 and rlc1.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000305}.
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DR EMBL; U75357; AAC49908.1; -; Genomic_DNA.
DR EMBL; CU329672; CAB39901.1; -; Genomic_DNA.
DR PIR; T41522; T41522.
DR RefSeq; NP_588114.1; NM_001023104.2.
DR AlphaFoldDB; Q9USI6; -.
DR SMR; Q9USI6; -.
DR BioGRID; 276075; 46.
DR STRING; 4896.SPCC645.05c.1; -.
DR iPTMnet; Q9USI6; -.
DR MaxQB; Q9USI6; -.
DR PaxDb; Q9USI6; -.
DR PRIDE; Q9USI6; -.
DR EnsemblFungi; SPCC645.05c.1; SPCC645.05c.1:pep; SPCC645.05c.
DR GeneID; 2539513; -.
DR KEGG; spo:SPCC645.05c; -.
DR PomBase; SPCC645.05c; myo2.
DR VEuPathDB; FungiDB:SPCC645.05c; -.
DR eggNOG; KOG0161; Eukaryota.
DR HOGENOM; CLU_000192_7_16_1; -.
DR InParanoid; Q9USI6; -.
DR OMA; TDTTQDK; -.
DR PhylomeDB; Q9USI6; -.
DR Reactome; R-SPO-5627123; RHO GTPases activate PAKs.
DR PRO; PR:Q9USI6; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0032153; C:cell division site; IDA:PomBase.
DR GO; GO:0030863; C:cortical cytoskeleton; IDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; IDA:PomBase.
DR GO; GO:0031097; C:medial cortex; IDA:PomBase.
DR GO; GO:0036391; C:medial cortex septin ring; IDA:PomBase.
DR GO; GO:0071341; C:medial cortical node; IDA:PomBase.
DR GO; GO:0110085; C:mitotic actomyosin contractile ring; IDA:PomBase.
DR GO; GO:0120106; C:mitotic actomyosin contractile ring, distal actin filament layer; IDA:PomBase.
DR GO; GO:0120105; C:mitotic actomyosin contractile ring, intermediate layer; IDA:PomBase.
DR GO; GO:0120104; C:mitotic actomyosin contractile ring, proximal layer; IDA:PomBase.
DR GO; GO:0032982; C:myosin filament; IBA:GO_Central.
DR GO; GO:0016460; C:myosin II complex; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; ISM:PomBase.
DR GO; GO:0030899; F:calcium-dependent ATPase activity; IDA:PomBase.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0000146; F:microfilament motor activity; IDA:PomBase.
DR GO; GO:1903478; P:actin filament bundle convergence involved in mitotic contractile ring assembly; IMP:PomBase.
DR GO; GO:1903475; P:mitotic actomyosin contractile ring assembly; IMP:PomBase.
DR GO; GO:1902404; P:mitotic actomyosin contractile ring contraction; IMP:PomBase.
DR GO; GO:1990274; P:mitotic actomyosin contractile ring disassembly; IMP:PomBase.
DR GO; GO:0000281; P:mitotic cytokinesis; IMP:PomBase.
DR Gene3D; 2.30.30.360; -; 1.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR004009; Myosin_N.
DR InterPro; IPR008989; Myosin_S1_N.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF02736; Myosin_N; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50096; IQ; 1.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS51844; SH3_LIKE; 1.
PE 1: Evidence at protein level;
KW Actin-binding; ATP-binding; Calmodulin-binding; Coiled coil; Motor protein;
KW Myosin; Nucleotide-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..1526
FT /note="Myosin type-2 heavy chain 1"
FT /id="PRO_0000123480"
FT DOMAIN 22..73
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01190"
FT DOMAIN 77..755
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 758..787
FT /note="IQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT REGION 634..656
FT /note="Actin-binding"
FT /evidence="ECO:0000250"
FT REGION 734..748
FT /note="Actin-binding"
FT /evidence="ECO:0000250"
FT COILED 875..1244
FT /evidence="ECO:0000255"
FT BINDING 170..177
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 1044
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT CONFLICT 1337
FT /note="S -> R (in Ref. 1; AAC49908)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1526 AA; 176432 MW; D71D51D6578192BA CRC64;
MTEVISNKIT AKDGATSLKD IDDKRWVWIS DPETAFTKAW IKEDLPDKKY VVRYNNSRDE
KIVGEDEIDP VNPAKFDRVN DMAELTYLNE PAVTYNLEQR YLSDQIYTYS GLFLVAVNPY
CGLPIYTKDI IQLYKDKTQE RKLPHVFAIA DLAYNNLLEN KENQSILVTG ESGAGKTENT
KRIIQYLAAI ASSTTVGSSQ VEEQIIKTNP VLESFGNART VRNNNSSRFG KFIKVEFSLS
GEISNAAIEW YLLEKSRVVH QNEFERNYHV FYQLLSGADT ALKNKLLLTD NCNDYRYLKD
SVHIIDGVDD KEEFKTLLAA FKTLGFDDKE NFDLFNILSI ILHMGNIDVG ADRSGIARLL
NPDEIDKLCH LLGVSPELFS QNLVRPRIKA GHEWVISARS QTQVISSIEA LAKAIYERNF
GWLVKRLNTS LNHSNAQSYF IGILDIAGFE IFEKNSFEQL CINYTNEKLQ QFFNHHMFVL
EQEEYMKEEI VWDFIDFGHD LQPTIDLIEK ANPIGILSCL DEECVMPKAT DATFTSKLDA
LWRNKSLKYK PFKFADQGFI LTHYAADVPY STEGWLEKNT DPLNENVAKL LAQSTNKHVA
TLFSDYQETE TKTVRGRTKK GLFRTVAQRH KEQLNQLMNQ FNSTQPHFIR CIVPNEEKKM
HTFNRPLVLG QLRCNGVLEG IRITRAGFPN RLPFNDFRVR YEIMAHLPTG TYVESRRASV
MILEELKIDE ASYRIGVSKI FFKAGVLAEL EERRVATLQR LMTMLQTRIR GFLQRKIFQK
RLKDIQAIKL LQANLQVYNE FRTFPWAKLF FNLRPLLSST QNDKQLKKRD AEIIELKYEL
KKQQNSKSEV ERDLVETNNS LTAVENLLTT ERAIALDKEE ILRRTQERLA NIEDSFSETK
QQNENLQRES ASLKQINNEL ESELLEKTSK VETLLSEQNE LKEKLSLEEK DLLDTKGELE
SLRENNATVL SEKAEFNEQC KSLQETIVTK DAELDKLTKY ISDYKTEIQE MRLTNQKMNE
KSIQQEGSLS ESLKRVKKLE RENSTLISDV SILKQQKEEL SVLKGVQELT INNLEEKVNY
LEADVKQLPK LKKELESLND KDQLYQLQAT KNKELEAKVK ECLNNIKSLT KELENKEEKC
QNLSDASLKY IELQEIHENL LLKVSDLENY KKKYEGLQLD LEGLKDVDTN FQELSKKHRD
LTFNHESLLR QSASYKEKLS LASSENKDLS NKVSSLTKQV NELSPKASKV PELERKITNL
MHEYSQLGKT FEDEKRKALI ASRDNEELRS LKSELESKRK LEVEYQKVLE EVKTTRSLRS
EVTLLRNKVA DHESIRSKLS EVEMKLVDTR KELNSALDSC KKREAEIHRL KEHRPSGKEN
NIPAVKTTEP VLKNIPQRKT IFDLQQRNAN QALYENLKRD YDRLNLEKHN LEKQVNELKG
AEVSPQPTGQ SLQHVNLAHA IELKALKDQI NSEKAKMFSV QVQYEKREQE LQKRIASLEK
VNKDSLIDVR ALRDRIASLE DELRAA
