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Protein

Myosin-1

Gene

myo1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Type-I myosin implicated in the organization of the actin cytoskeleton. Required for proper actin cytoskeleton polarization. At the cell cortex, assembles in patch-like structures together with proteins from the actin-polymerizing machinery and promotes actin assembly. Functions as actin nucleation-promoting factor (NPF) for the Arp2/3 complex. Contributes to proper septation by transporting vesicles containing septal material to the division site and is involved in the formation of sterol-rich membrane domains at the cell division site. Required also for mating.3 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi17 – 248ATPSequence analysis
Nucleotide bindingi133 – 1408ATPSequence analysis

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • microfilament motor activity Source: PomBase
  • phospholipid binding Source: PomBase

GO - Biological processi

  • actin cortical patch assembly Source: PomBase
  • actin cortical patch localization Source: PomBase
  • actin cytoskeleton organization Source: PomBase
  • actin filament organization Source: PomBase
  • actin nucleation Source: PomBase
  • endocytosis Source: PomBase
  • establishment or maintenance of cell polarity regulating cell shape Source: PomBase
  • plasma membrane raft distribution Source: PomBase
  • positive regulation of actin nucleation Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Motor protein, Myosin

Keywords - Ligandi

Actin-binding, ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Myosin-1
Alternative name(s):
Class I unconventional myosin
Type I myosin
Gene namesi
Name:myo1
ORF Names:SPBC146.13c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBC146.13c.
PomBaseiSPBC146.13c. myo1.

Subcellular locationi

GO - Cellular componenti

  • actin cortical patch Source: PomBase
  • actomyosin contractile ring Source: PomBase
  • cell division site Source: PomBase
  • cell tip Source: PomBase
  • cytoplasm Source: PomBase
  • mating projection tip Source: PomBase
  • medial cortex Source: PomBase
  • myosin I complex Source: PomBase
  • plasma membrane raft Source: PomBase
  • prospore membrane Source: PomBase
  • site of polarized growth Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12171217Myosin-1PRO_0000123479Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei361 – 3611Phosphoserine1 Publication
Modified residuei363 – 3631Phosphotyrosine1 Publication
Modified residuei742 – 7421Phosphoserine1 Publication
Modified residuei782 – 7821Phosphoserine1 Publication
Modified residuei1211 – 12111Phosphoserine1 Publication

Post-translational modificationi

Phosphorylation of the TEDS site (Ser-361) is required for the polarization of the actin cytoskeleton. Phosphorylation probably activates the myosin-I ATPase activity (By similarity).By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9Y7Z8.
PRIDEiQ9Y7Z8.

PTM databases

iPTMnetiQ9Y7Z8.

Interactioni

Subunit structurei

Interacts with cam2. Interacts (via SH3 domain) with vrp1.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
cdc15Q098224EBI-1148082,EBI-1148185
wsp1O360274EBI-1148082,EBI-1148109

Protein-protein interaction databases

BioGridi276214. 23 interactions.
IntActiQ9Y7Z8. 10 interactions.
MINTiMINT-4720405.

Structurei

3D structure databases

ProteinModelPortaliQ9Y7Z8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini40 – 720681Myosin motorAdd
BLAST
Domaini724 – 74421IQ 1Add
BLAST
Domaini745 – 77026IQ 2Add
BLAST
Domaini778 – 964187TH1PROSITE-ProRule annotationAdd
BLAST
Domaini1106 – 116560SH3PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni409 – 49183Actin-bindingBy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi963 – 1102140Pro-richAdd
BLAST
Compositional biasi1045 – 10506Poly-Thr

Domaini

The myosin motor domain displays actin-stimulated ATPase activity and generates a mechanochemical force.By similarity
The tail domain participates in molecular interactions that specify the role of the motor domain (By similarity). It is composed of several tail homology (TH) domains, namely a putative phospholipid-binding myosin tail domain (also named TH1), an Ala- and Pro-rich domain (TH2), followed by an SH3 domain and a C-terminal acidic domain (TH3).By similarity

Sequence similaritiesi

Contains 2 IQ domains.Curated
Contains 1 myosin motor domain.Curated
Contains 1 SH3 domain.PROSITE-ProRule annotation
Contains 1 TH1 (class I myosin tail homology) domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, SH3 domain

Phylogenomic databases

HOGENOMiHOG000260265.
InParanoidiQ9Y7Z8.
KOiK10356.
OMAiLKLRFEH.
OrthoDBiEOG7VDXXK.
PhylomeDBiQ9Y7Z8.

Family and domain databases

InterProiIPR001609. Myosin_head_motor_dom.
IPR010926. Myosin_TH1.
IPR027417. P-loop_NTPase.
IPR001452. SH3_domain.
[Graphical view]
PfamiPF00063. Myosin_head. 1 hit.
PF06017. Myosin_TH1. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSiPR00193. MYOSINHEAVY.
SMARTiSM00242. MYSc. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS51456. MYOSIN_MOTOR. 1 hit.
PS50002. SH3. 1 hit.
PS51757. TH1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9Y7Z8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAILKRTNRA KAATAAAPNS TGKSNGIKKA VYTSTRKKTV GVDDLTLLSK
60 70 80 90 100
ITDEEINKNL ELRFRNGEIY TYIGHVLISV NPFRDLGIYT MDILKSYQGK
110 120 130 140 150
NRLETSPHVY AIAENAYYQM KSYHENQCII ISGESGAGKT EAAKRIMQYI
160 170 180 190 200
THVSKSVGTE IERVSEIILA TNPLLESFGC AKTLRNNNSS RHGKYLEMIF
210 220 230 240 250
NSGGVPVGAK ITNYLLEKNR IVNQVRNERN FHIFYQFTKS APQKYRDTYG
260 270 280 290 300
IQGPENYVYT SACQCLSVDG ISDEKDFQGT MNAMKVIGIT EPEQDEIFRM
310 320 330 340 350
LSIILWLGNI QFQEGQDGGS VISDKSITEF LGYLIGVPVA AIERALTIRI
360 370 380 390 400
MQTQHGARRG SVYEVPLNPT QALAVRDALS MAIYNCLFDW IVERVNKALV
410 420 430 440 450
TSDNSVSNSI GILDIYGFEI FENNSFEQLC INYVNEKLQQ IFIELTLKTE
460 470 480 490 500
QEEYVREQIA WTPIKYFNNK VVCDLIESKR PPGLFAAMND AIATAHADSA
510 520 530 540 550
AADSAFAQRL NFLSSNPHFE QRQNQFIVKH YAGDVTYSIT GMTDKNKDQL
560 570 580 590 600
ATDILNLIHS SNNEFMKSIF PVAEESNSRR RPPTAGDRIK TSANDLVETL
610 620 630 640 650
MKCQPSYIRT IKPNQTKSPN DYDQQMVLHQ IKYLGLQENI RIRRAGFAYR
660 670 680 690 700
QAFDTFAQRF AVLSGKTSYA GEYTWQGDDK SACEQILKDT NIPSSEYQMG
710 720 730 740 750
TSKVFIKNPE TLFALEDMRD KFWDTMATRI QRAWRSYVRR RSEAAACIQK
760 770 780 790 800
LWNRNKVNME LERVRNEGTK LLQGKKQRRR YSILGSRKFY GDYLSASKPN
810 820 830 840 850
GTLWNTCGLS QNDHVIFSMR CEVLVHKLGR TSKPSPRQLV LTKKNLYLVI
860 870 880 890 900
TKIVDQKLTQ QVEKKFAVSS IDSVGLTNLQ DDWVAIRNKS SQNGDMFLRC
910 920 930 940 950
FFKTEFITTL KRINRNIQVI VGPTIQYCRK PGKVQTVKTA KDETTKDYDY
960 970 980 990 1000
YKSGTIHVGT GLPPTSKSKP FPRLATGGST AAARGPRPVV QNKPAATKPV
1010 1020 1030 1040 1050
SMPAAKSKPA PMANPVSTAQ QTQNRPPAPA MQARPNTTQA AAPVTSTTTT
1060 1070 1080 1090 1100
IKQATTVSAS KPAPSTVTSA ASSPSNISKP SAPVANNVSK PSAVPPPPPP
1110 1120 1130 1140 1150
PPAEVEKKDL YLALYDFAGR SPNEMTIKKD EIIEIVQKEP SGWWLALKNG
1160 1170 1180 1190 1200
AEGWVPATYV TEYKGSTPQT TASSTNVAAQ ANNNASPAEV NNLAGSLADA
1210
LRMRASAVRG SDEEEDW
Length:1,217
Mass (Da):135,710
Last modified:November 1, 1999 - v1
Checksum:i23851048FF5DEF0A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAB46766.1.
PIRiT39427.
RefSeqiNP_595402.1. NM_001021309.2.

Genome annotation databases

EnsemblFungiiSPBC146.13c.1; SPBC146.13c.1:pep; SPBC146.13c.
GeneIDi2539659.
KEGGispo:SPBC146.13c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAB46766.1.
PIRiT39427.
RefSeqiNP_595402.1. NM_001021309.2.

3D structure databases

ProteinModelPortaliQ9Y7Z8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi276214. 23 interactions.
IntActiQ9Y7Z8. 10 interactions.
MINTiMINT-4720405.

PTM databases

iPTMnetiQ9Y7Z8.

Proteomic databases

MaxQBiQ9Y7Z8.
PRIDEiQ9Y7Z8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC146.13c.1; SPBC146.13c.1:pep; SPBC146.13c.
GeneIDi2539659.
KEGGispo:SPBC146.13c.

Organism-specific databases

EuPathDBiFungiDB:SPBC146.13c.
PomBaseiSPBC146.13c. myo1.

Phylogenomic databases

HOGENOMiHOG000260265.
InParanoidiQ9Y7Z8.
KOiK10356.
OMAiLKLRFEH.
OrthoDBiEOG7VDXXK.
PhylomeDBiQ9Y7Z8.

Miscellaneous databases

PROiQ9Y7Z8.

Family and domain databases

InterProiIPR001609. Myosin_head_motor_dom.
IPR010926. Myosin_TH1.
IPR027417. P-loop_NTPase.
IPR001452. SH3_domain.
[Graphical view]
PfamiPF00063. Myosin_head. 1 hit.
PF06017. Myosin_TH1. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSiPR00193. MYOSINHEAVY.
SMARTiSM00242. MYSc. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS51456. MYOSIN_MOTOR. 1 hit.
PS50002. SH3. 1 hit.
PS51757. TH1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  2. "Fission yeast myosin-I, Myo1p, stimulates actin assembly by Arp2/3 complex and shares functions with WASp."
    Lee W.-L., Bezanilla M., Pollard T.D.
    J. Cell Biol. 151:789-800(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  3. "UCS protein Rng3p activates actin filament gliding by fission yeast myosin-II."
    Lord M., Pollard T.D.
    J. Cell Biol. 167:315-325(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CAM2.
  4. "Role of fission yeast myosin I in organization of sterol-rich membrane domains."
    Takeda T., Chang F.
    Curr. Biol. 15:1331-1336(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  5. "Interactions of WASp, myosin-I, and verprolin with Arp2/3 complex during actin patch assembly in fission yeast."
    Sirotkin V., Beltzner C.C., Marchand J.-B., Pollard T.D.
    J. Cell Biol. 170:637-648(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH VRP1.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-361; TYR-363; SER-742; SER-782 AND SER-1211, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiMYO1_SCHPO
AccessioniPrimary (citable) accession number: Q9Y7Z8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: November 1, 1999
Last modified: June 8, 2016
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.