MYO1_SCHPO
ID MYO1_SCHPO Reviewed; 1217 AA.
AC Q9Y7Z8;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Myosin-1;
DE AltName: Full=Class I unconventional myosin;
DE AltName: Full=Type I myosin;
GN Name=myo1; ORFNames=SPBC146.13c;
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 FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11076964; DOI=10.1083/jcb.151.4.789;
RA Lee W.-L., Bezanilla M., Pollard T.D.;
RT "Fission yeast myosin-I, Myo1p, stimulates actin assembly by Arp2/3 complex
RT and shares functions with WASp.";
RL J. Cell Biol. 151:789-800(2000).
RN [3]
RP INTERACTION WITH CAM2.
RX PubMed=15504913; DOI=10.1083/jcb.200404045;
RA Lord M., Pollard T.D.;
RT "UCS protein Rng3p activates actin filament gliding by fission yeast
RT myosin-II.";
RL J. Cell Biol. 167:315-325(2004).
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16051179; DOI=10.1016/j.cub.2005.07.009;
RA Takeda T., Chang F.;
RT "Role of fission yeast myosin I in organization of sterol-rich membrane
RT domains.";
RL Curr. Biol. 15:1331-1336(2005).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH VRP1.
RX PubMed=16087707; DOI=10.1083/jcb.200502053;
RA Sirotkin V., Beltzner C.C., Marchand J.-B., Pollard T.D.;
RT "Interactions of WASp, myosin-I, and verprolin with Arp2/3 complex during
RT actin patch assembly in fission yeast.";
RL J. Cell Biol. 170:637-648(2005).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-361; TYR-363; SER-742;
RP SER-782 AND SER-1211, AND 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).
CC -!- FUNCTION: Type-I myosin implicated in the organization of the actin
CC cytoskeleton. Required for proper actin cytoskeleton polarization. At
CC the cell cortex, assembles in patch-like structures together with
CC proteins from the actin-polymerizing machinery and promotes actin
CC assembly. Functions as actin nucleation-promoting factor (NPF) for the
CC Arp2/3 complex. Contributes to proper septation by transporting
CC vesicles containing septal material to the division site and is
CC involved in the formation of sterol-rich membrane domains at the cell
CC division site. Required also for mating. {ECO:0000269|PubMed:11076964,
CC ECO:0000269|PubMed:16051179, ECO:0000269|PubMed:16087707}.
CC -!- SUBUNIT: Interacts with cam2. Interacts (via SH3 domain) with vrp1.
CC {ECO:0000269|PubMed:15504913, ECO:0000269|PubMed:16087707}.
CC -!- INTERACTION:
CC Q9Y7Z8; Q09822: cdc15; NbExp=4; IntAct=EBI-1148082, EBI-1148185;
CC Q9Y7Z8; O36027: wsp1; NbExp=4; IntAct=EBI-1148082, EBI-1148109;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, actin patch
CC {ECO:0000269|PubMed:11076964, ECO:0000269|PubMed:16051179,
CC ECO:0000269|PubMed:16087707}. Note=Localizes to cortical patches at the
CC tips of growing cells and at sites of cell division.
CC -!- DOMAIN: The myosin motor domain displays actin-stimulated ATPase
CC activity and generates a mechanochemical force. {ECO:0000250}.
CC -!- DOMAIN: The tail domain participates in molecular interactions that
CC specify the role of the motor domain (By similarity). It is composed of
CC several tail homology (TH) domains, namely a putative phospholipid-
CC binding myosin tail domain (also named TH1), an Ala- and Pro-rich
CC domain (TH2), followed by an SH3 domain and a C-terminal acidic domain
CC (TH3). {ECO:0000250}.
CC -!- PTM: Phosphorylation of the TEDS site (Ser-361) is required for the
CC polarization of the actin cytoskeleton. Phosphorylation probably
CC activates the myosin-I ATPase activity (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000305}.
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DR EMBL; CU329671; CAB46766.1; -; Genomic_DNA.
DR PIR; T39427; T39427.
DR RefSeq; NP_595402.1; NM_001021309.2.
DR AlphaFoldDB; Q9Y7Z8; -.
DR SMR; Q9Y7Z8; -.
DR BioGRID; 276214; 28.
DR IntAct; Q9Y7Z8; 10.
DR STRING; 4896.SPBC146.13c.1; -.
DR iPTMnet; Q9Y7Z8; -.
DR MaxQB; Q9Y7Z8; -.
DR PaxDb; Q9Y7Z8; -.
DR PRIDE; Q9Y7Z8; -.
DR EnsemblFungi; SPBC146.13c.1; SPBC146.13c.1:pep; SPBC146.13c.
DR GeneID; 2539659; -.
DR KEGG; spo:SPBC146.13c; -.
DR PomBase; SPBC146.13c; myo1.
DR VEuPathDB; FungiDB:SPBC146.13c; -.
DR eggNOG; KOG0162; Eukaryota.
DR HOGENOM; CLU_000192_7_6_1; -.
DR InParanoid; Q9Y7Z8; -.
DR OMA; NGWWLCK; -.
DR PhylomeDB; Q9Y7Z8; -.
DR PRO; PR:Q9Y7Z8; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0030479; C:actin cortical patch; IDA:PomBase.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0051285; C:cell cortex of cell tip; IDA:PomBase.
DR GO; GO:0032153; C:cell division site; IDA:PomBase.
DR GO; GO:0051286; C:cell tip; IDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0043332; C:mating projection tip; IDA:PomBase.
DR GO; GO:0031097; C:medial cortex; IDA:PomBase.
DR GO; GO:0045160; C:myosin I complex; IPI:PomBase.
DR GO; GO:0005886; C:plasma membrane; EXP:PomBase.
DR GO; GO:0044853; C:plasma membrane raft; IDA:PomBase.
DR GO; GO:0005628; C:prospore membrane; IDA:PomBase.
DR GO; GO:0051015; F:actin filament binding; IDA:PomBase.
DR GO; GO:0071933; F:Arp2/3 complex binding; IDA:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0000146; F:microfilament motor activity; IDA:PomBase.
DR GO; GO:0005543; F:phospholipid binding; TAS:PomBase.
DR GO; GO:0000147; P:actin cortical patch assembly; IMP:PomBase.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0030989; P:dynein-driven meiotic oscillatory nuclear movement; EXP:PomBase.
DR GO; GO:0006897; P:endocytosis; IMP:PomBase.
DR GO; GO:0071963; P:establishment or maintenance of cell polarity regulating cell shape; IMP:PomBase.
DR GO; GO:0000281; P:mitotic cytokinesis; IMP:PomBase.
DR GO; GO:0044855; P:plasma membrane raft distribution; IMP:PomBase.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; IDA:PomBase.
DR GO; GO:0051127; P:positive regulation of actin nucleation; IDA:PomBase.
DR GO; GO:2000601; P:positive regulation of Arp2/3 complex-mediated actin nucleation; IDA:PomBase.
DR GO; GO:0030050; P:vesicle transport along actin filament; IBA:GO_Central.
DR CDD; cd01378; MYSc_Myo1; 1.
DR CDD; cd11858; SH3_Myosin-I_fungi; 1.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR035535; Fungal_myosin-I_SH3.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR010926; Myosin_TH1.
DR InterPro; IPR036072; MYSc_Myo1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF06017; Myosin_TH1; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00242; MYSc; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS50002; SH3; 1.
DR PROSITE; PS51757; TH1; 1.
PE 1: Evidence at protein level;
KW Actin-binding; ATP-binding; Cytoplasm; Cytoskeleton; Hydrolase;
KW Motor protein; Myosin; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Repeat; SH3 domain.
FT CHAIN 1..1217
FT /note="Myosin-1"
FT /id="PRO_0000123479"
FT DOMAIN 40..720
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 724..744
FT /note="IQ 1"
FT DOMAIN 745..770
FT /note="IQ 2"
FT DOMAIN 778..964
FT /note="TH1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01093"
FT DOMAIN 1106..1165
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 409..491
FT /note="Actin-binding"
FT /evidence="ECO:0000250"
FT REGION 961..1105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1013..1088
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1090..1105
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 17..24
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 133..140
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 361
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 363
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 742
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 782
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 1211
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 1217 AA; 135710 MW; 23851048FF5DEF0A CRC64;
MAILKRTNRA KAATAAAPNS TGKSNGIKKA VYTSTRKKTV GVDDLTLLSK ITDEEINKNL
ELRFRNGEIY TYIGHVLISV NPFRDLGIYT MDILKSYQGK NRLETSPHVY AIAENAYYQM
KSYHENQCII ISGESGAGKT EAAKRIMQYI THVSKSVGTE IERVSEIILA TNPLLESFGC
AKTLRNNNSS RHGKYLEMIF NSGGVPVGAK ITNYLLEKNR IVNQVRNERN FHIFYQFTKS
APQKYRDTYG IQGPENYVYT SACQCLSVDG ISDEKDFQGT MNAMKVIGIT EPEQDEIFRM
LSIILWLGNI QFQEGQDGGS VISDKSITEF LGYLIGVPVA AIERALTIRI MQTQHGARRG
SVYEVPLNPT QALAVRDALS MAIYNCLFDW IVERVNKALV TSDNSVSNSI GILDIYGFEI
FENNSFEQLC INYVNEKLQQ IFIELTLKTE QEEYVREQIA WTPIKYFNNK VVCDLIESKR
PPGLFAAMND AIATAHADSA AADSAFAQRL NFLSSNPHFE QRQNQFIVKH YAGDVTYSIT
GMTDKNKDQL ATDILNLIHS SNNEFMKSIF PVAEESNSRR RPPTAGDRIK TSANDLVETL
MKCQPSYIRT IKPNQTKSPN DYDQQMVLHQ IKYLGLQENI RIRRAGFAYR QAFDTFAQRF
AVLSGKTSYA GEYTWQGDDK SACEQILKDT NIPSSEYQMG TSKVFIKNPE TLFALEDMRD
KFWDTMATRI QRAWRSYVRR RSEAAACIQK LWNRNKVNME LERVRNEGTK LLQGKKQRRR
YSILGSRKFY GDYLSASKPN GTLWNTCGLS QNDHVIFSMR CEVLVHKLGR TSKPSPRQLV
LTKKNLYLVI TKIVDQKLTQ QVEKKFAVSS IDSVGLTNLQ DDWVAIRNKS SQNGDMFLRC
FFKTEFITTL KRINRNIQVI VGPTIQYCRK PGKVQTVKTA KDETTKDYDY YKSGTIHVGT
GLPPTSKSKP FPRLATGGST AAARGPRPVV QNKPAATKPV SMPAAKSKPA PMANPVSTAQ
QTQNRPPAPA MQARPNTTQA AAPVTSTTTT IKQATTVSAS KPAPSTVTSA ASSPSNISKP
SAPVANNVSK PSAVPPPPPP PPAEVEKKDL YLALYDFAGR SPNEMTIKKD EIIEIVQKEP
SGWWLALKNG AEGWVPATYV TEYKGSTPQT TASSTNVAAQ ANNNASPAEV NNLAGSLADA
LRMRASAVRG SDEEEDW
