MYO3_SCHPO
ID MYO3_SCHPO Reviewed; 2104 AA.
AC O14157; O42730; Q9UU49;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Myosin type-2 heavy chain 2;
DE AltName: Full=Myosin type II heavy chain 2;
GN Name=myo3; Synonyms=myp2; ORFNames=SPAC4A8.05c;
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].
RX PubMed=9459302; DOI=10.1016/s0014-5793(97)01510-x;
RA Motegi F., Nakano K., Kitayama C., Yamamoto M., Mabuchi I.;
RT "Identification of Myo3, a second type-II myosin heavy chain in the fission
RT yeast Schizosaccharomyces pombe.";
RL FEBS Lett. 420:161-166(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9398685; DOI=10.1091/mbc.8.12.2693;
RA Bezanilla M., Forsburg S.L., Pollard T.D.;
RT "Identification of a second myosin-II in Schizosaccharomyces pombe: Myp2p
RT is conditionally required for cytokinesis.";
RL Mol. Biol. Cell 8:2693-2705(1997).
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).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 1871-2078.
RC STRAIN=ATCC 38364 / 968;
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1421, 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: Stabilizes the F-actin cables forming the F-actin ring that
CC surrounds the nucleus during interphase. May work in conjunction with
CC myo2.
CC -!- SUBUNIT: Binds to cdc4 and rlc1.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000305}.
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; AB007633; BAA24579.1; -; Genomic_DNA.
DR EMBL; AF029788; AAC04615.1; -; Genomic_DNA.
DR EMBL; CU329670; CAB11475.1; -; Genomic_DNA.
DR EMBL; AB027812; BAA87116.1; -; Genomic_DNA.
DR PIR; T38774; T38774.
DR RefSeq; NP_593816.1; NM_001019246.2.
DR AlphaFoldDB; O14157; -.
DR SMR; O14157; -.
DR BioGRID; 279991; 62.
DR STRING; 4896.SPAC4A8.05c.1; -.
DR iPTMnet; O14157; -.
DR MaxQB; O14157; -.
DR PaxDb; O14157; -.
DR PRIDE; O14157; -.
DR EnsemblFungi; SPAC4A8.05c.1; SPAC4A8.05c.1:pep; SPAC4A8.05c.
DR GeneID; 2543576; -.
DR KEGG; spo:SPAC4A8.05c; -.
DR PomBase; SPAC4A8.05c; -.
DR VEuPathDB; FungiDB:SPAC4A8.05c; -.
DR eggNOG; KOG0161; Eukaryota.
DR HOGENOM; CLU_000192_5_3_1; -.
DR InParanoid; O14157; -.
DR OMA; TEFRSRY; -.
DR PhylomeDB; O14157; -.
DR Reactome; R-SPO-5627123; RHO GTPases activate PAKs.
DR PRO; PR:O14157; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0032153; C:cell division site; IDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0000930; C:gamma-tubulin complex; IMP:PomBase.
DR GO; GO:0031097; C:medial cortex; IDA:PomBase.
DR GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR GO; GO:0110085; C:mitotic actomyosin contractile ring; 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; IBA:GO_Central.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; ISM:PomBase.
DR GO; GO:0000146; F:microfilament motor activity; ISM: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:1902406; P:mitotic actomyosin contractile ring maintenance; IMP:PomBase.
DR GO; GO:0000281; P:mitotic cytokinesis; IMP:PomBase.
DR GO; GO:0090561; P:nuclear migration during mitotic telophase; IGI:PomBase.
DR Gene3D; 2.30.30.360; -; 1.
DR Gene3D; 3.40.850.10; -; 1.
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; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS51844; SH3_LIKE; 1.
PE 1: Evidence at protein level;
KW Actin-binding; ATP-binding; Coiled coil; Motor protein; Myosin;
KW Nucleotide-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..2104
FT /note="Myosin type-2 heavy chain 2"
FT /id="PRO_0000123481"
FT DOMAIN 35..85
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01190"
FT DOMAIN 89..767
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT REGION 646..660
FT /note="Actin-binding"
FT /evidence="ECO:0000255"
FT REGION 1245..1278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1398..1426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 829..2104
FT /evidence="ECO:0000255"
FT COMPBIAS 1258..1278
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1398..1424
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 182..189
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 1421
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT CONFLICT 1193
FT /note="D -> G (in Ref. 2; AAC04615)"
FT /evidence="ECO:0000305"
FT CONFLICT 1304
FT /note="E -> G (in Ref. 2; AAC04615)"
FT /evidence="ECO:0000305"
FT CONFLICT 1344
FT /note="E -> K (in Ref. 2; AAC04615)"
FT /evidence="ECO:0000305"
FT CONFLICT 1420
FT /note="G -> D (in Ref. 2; AAC04615)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2104 AA; 242572 MW; 3A0548594028D258 CRC64;
MSYLSKNGSN DNNNIIKKLV DAEKHCNAVK DASFDERTWI WIPDSKESFV KAWIVEDLGE
KYRVKLERDG SERIVDGFDA EKVNPPKFDM VDDMAALTCL NEPSVVNNLT QRYEKDLIYT
YSGLFLVAVN PYCHLPIYGD DVVRKYQSKQ FKETKPHIFG TADAAYRSLL ERRINQSILV
TGESGAGKTE TTKKVIQYLT SVTDASTSDS QQLEKKILET NPVLEAFGNA QTVRNNNSSR
FGKFIRIEFS NNGSIVGANL DWYLLEKSRV IHPSSNERNY HVFYQLLRGA DGSLLESLFL
DRYVDHYSYL KNGLKHINGV DDGKEFQKLC FGLRTLGFDN NEIHSLFLII ASILHIGNIE
VASDRSGQAR FPSLTQIDQL CHLLEIPVDG FVNAALHPKS KAGREWIVTA RTREQVVHTL
QSLAKGLYER NFAHLVKRLN QTMYYSQSEH DGFIGVLDIA GFEIFTFNSF EQLCINFTNE
KLQQFFNHYM FVLEQEEYTQ ERIEWDFIDY GNDLQPTIDA IEKSEPIGIF SCLDEDCVMP
MATDATFTEK LHLLFKGKSD IYRPKKFSSE GFVLKHYAGD VEYDTKDWLE KNKDPLNACL
AALMFKSTNS HVSSLFDDYS SNASGRDNIE KKGIFRTVSQ RHRRQLSSLM HQLEATQPHF
VRCIIPNNLK QPHNLDKSLV LHQLRCNGVL EGIRIAQTGF PNKLFYTEFR ARYGILSQSL
KRGYVEAKKA TITIINELKL PSTVYRLGET KVFFKASVLG SLEDRRNALL RVIFNSFSAR
IRGFLTRRRL YRFNHRQDAA ILLQHNLRQL KLLKPHPWWN LFLHLKPLLG TTQTDEYLRR
KDALINNLQN QLESTKEVAN ELTITKERVL QLTNDLQEEQ ALAHEKDILV ERANSRVEVV
HERLSSLENQ VTIADEKYEF LYAEKQSIEE DLANKQTEIS YLSDLSSTLE KKLSSIKKDE
QTISSKYKEL EKDYLNIMAD YQHSSQHLSN LEKAINEKNL NIRELNEKLM RLDDELLLKQ
RSYDTKVQEL REENASLKDQ CRTYESQLAS LVSKYSETES ELNKKEAELV IFQKEITEYR
DQLHKAFQNP EKTHNINDVK SGPLNSDENI YSTSSTTLSI LKDVQELKSL HTKEANQLSE
RIKEISEMLE QSIATEEKLR RKNSELCDII EALKYQIQDQ ETEIISLNAD NLDLKDTNGV
LEKNASDFID FQGIKSRYEH KISDLLNQLQ KERCKVGLLK QKTENRSVTQ HTLDGNSPHP
SFEEKHSGDP LKRIDGNNDD RKIDNKLLKT ISKSLDALQL TVEEELSNLY SLSKDLSFTD
ISGHIPNSIR KLEKGLSTLS ELKERLNASN SDRPSPDIFK DTQAIMNSRK LLSNPNSDAQ
SGLISSLQKK LYNPESNMEF TGLKPLSPSK ISNLPSSQPG SPSKRSGKME ALIRNFDQNS
SIPDPFIVNQ RNSVLQTEFE KINLKLKEAT KSGILDNKDL SKFSELIQSL LKENEELKNL
TTSNLGSDDK MLDFAPLLED VPNNTRNQIK GFVEKAISSK RAIAKLYSAS EEKLFSTEKA
LREITKERDR LLHGLQGPSV PTSPLKAPTA SQLIIPNFDG SITNYSGEEE TEWLQEEVNI
MKIKELTSTV NKYREQLAMV QSLNEHAESS LSKAERSKNY LTGRLQEVEE LARGFQTTNA
DLQNELADAV VKQKEYEVLY VEKSNDYNTL LLQKEKLMKQ IDEFHVIRVQ DLEEREKKDQ
LLFQRYQKEL NGFKVQLEEE REKNLRIRQD NRHMHAEIGD IRTKFDELVL EKTNLLKENS
ILQADLQSLS RVNNSSSTAQ QNAQSQLLSL TAQLQEVREA NQTLRKDQDT LLRENRNLER
KLHEVSEQLN KKFDSSARPF DEIEMEKEVL TLKSNLAQKD DLLSSLVERI KQIEMFALKT
QKDSNNHREE NLQLHRQLGV LQKEKKDLEL KLFDLDLKTY PISTSKDVRM LQKQISDLEA
SFAASDIERI KGIDECRNRD RTIRQLEAQI SKFDDDKKRI QSSVSRLEER NAQLRNQLED
VQASETQWKF ALRRTEHALQ EERERVKSLE TDFDKYRSLL EGQRVKRSES RLSMRSNRSP
SVLR
