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Protein

Myosin-2

Gene

MYO2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Myosin heavy chain that is required for the cell cycle-regulated transport of various organelles and proteins for their segregation. Functions by binding with its tail domain to receptor proteins on organelles and exerting force with its N-terminal motor domain against actin filaments, thereby transporting its cargo along polarized actin cables. Essential for the delivery of secretory vesicles to sites of active growth during bud emergence and cytokinesis. Required for segregation and inheritance of peroxisomes, late Golgi compartments, mitochondria and the vacuole to the daughter cell during cell division. Also required for correct alignment of the spindle during mitosis.8 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi164 – 171ATPBy similarity8

GO - Molecular functioni

  • actin filament binding Source: SGD
  • ATP binding Source: UniProtKB-KW
  • calmodulin binding Source: SGD
  • microfilament motor activity Source: SGD

GO - Biological processi

  • budding cell apical bud growth Source: SGD
  • establishment of mitotic spindle orientation Source: SGD
  • Golgi inheritance Source: SGD
  • membrane addition at site of cytokinesis Source: SGD
  • mitochondrion inheritance Source: SGD
  • peroxisome inheritance Source: SGD
  • protein transport Source: UniProtKB-KW
  • unidimensional cell growth Source: SGD
  • vacuole inheritance Source: SGD
  • vesicle docking involved in exocytosis Source: SGD
  • vesicle-mediated transport Source: SGD
  • vesicle transport along actin filament Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Motor protein, Myosin

Keywords - Biological processi

Cell cycle, Cell division, Protein transport, Transport

Keywords - Ligandi

Actin-binding, ATP-binding, Calmodulin-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-33803-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Myosin-2
Alternative name(s):
Cell division control protein 66
Class V unconventional myosin MYO2
Type V myosin heavy chain MYO2
Short name:
Myosin V MYO2
Gene namesi
Name:MYO2
Synonyms:CDC66
Ordered Locus Names:YOR326W
ORF Names:O6167
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XV

Organism-specific databases

EuPathDBiFungiDB:YOR326W.
SGDiS000005853. MYO2.

Subcellular locationi

  • Bud neck 1 Publication
  • Bud tip 1 Publication

  • Note: Concentrates to sites of polarized growth, namely to the bud tip during S and G2 phases of the cell cycle and to the bud neck during cytokinesis.

GO - Cellular componenti

  • actin filament bundle Source: SGD
  • cellular bud neck Source: SGD
  • cellular bud tip Source: SGD
  • filamentous actin Source: SGD
  • incipient cellular bud site Source: SGD
  • mating projection tip Source: SGD
  • Myo2p-Vac17p-Vac8p transport complex Source: SGD
  • myosin complex Source: UniProtKB-KW
  • transport vesicle Source: SGD
  • vesicle Source: SGD
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi511E → K in MYO2-66; disrupts actin binding. 1 Publication1
Mutagenesisi1189V → A in MYO2-573; causes a mitochondria inheritance defect; when associated with G-1288; M-1500; S-1529; G-1546 and R-1559. 1 Publication1
Mutagenesisi1247S → G: Intragenic suppressor of MYO2-2. 1 Publication1
Mutagenesisi1248G → D in MYO2-2; causes a vacuole inheritance defect. 1 Publication1
Mutagenesisi1262V → A: Intragenic suppressor of MYO2-2. 1 Publication1
Mutagenesisi1264F → S: Intragenic suppressor of MYO2-2. 1 Publication1
Mutagenesisi1268S → P: Intragenic suppressor of MYO2-2. 1 Publication1
Mutagenesisi1274T → M: Intragenic suppressor of MYO2-2. 1 Publication1
Mutagenesisi1275F → S: Intragenic suppressor of MYO2-2. 1 Publication1
Mutagenesisi1288V → A: Intragenic suppressor of MYO2-2. 2 Publications1
Mutagenesisi1288V → G in MYO2-573; causes a mitochondria inheritance defect; when associated with A-1189; M-1500; S-1529; G-1546 and R-1559. 2 Publications1
Mutagenesisi1297D → G, N or V: Causes a vacuole inheritance defect. 1 Publication1
Mutagenesisi1301L → P: Causes a vacuole inheritance defect. 1 Publication1
Mutagenesisi1304N → D or S: Causes a vacuole inheritance defect. 1 Publication1
Mutagenesisi1307N → D: Causes a vacuole inheritance defect. 1 Publication1
Mutagenesisi1474L → S in MYO2-338; abolishes interaction with YPT11; when associated with G-1484 and G-1511. 1 Publication1
Mutagenesisi1484E → G in MYO2-338; abolishes interaction with YPT11; when associated with S-1474 and G-1511. 1 Publication1
Mutagenesisi1500K → M in MYO2-573; causes a mitochondria inheritance defect; when associated with A-1189; G-1288; S-1529; G-1546 and R-1559. 1 Publication1
Mutagenesisi1511D → G in MYO2-338; abolishes interaction with YPT11; when associated with S-1474 and G-1484. 1 Publication1
Mutagenesisi1529P → S in MYO2-573; causes a mitochondria inheritance defect; when associated with A-1189; G-1288; M-1500; G-1546 and R-1559. 1 Publication1
Mutagenesisi1546E → G in MYO2-573; causes a mitochondria inheritance defect; when associated with A-1189; G-1288; M-1500; S-1529 and R-1559. 1 Publication1
Mutagenesisi1559K → R in MYO2-573; causes a mitochondria inheritance defect; when associated with A-1189; G-1288; M-1500; S-1529 and G-1546. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00001234892 – 1574Myosin-2Add BLAST1573

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineCombined sources1
Modified residuei1097PhosphothreonineCombined sources1
Modified residuei1121PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP19524.
PRIDEiP19524.

PTM databases

iPTMnetiP19524.

Interactioni

Subunit structurei

Homodimer. Interacts with calmodulin (CMD1) and the myosin light chain MLC1 through its IQ repeats. Binds to the membrane receptors SEC4 and VAC17 to transport secretory vesicles and the vacuole, respectively. Binds to KAR9, which transports BIM1-coated cytoplasmic microtubules that are attached to the spindle pole body into the emerging bud, thereby correctly orienting the mitotic spindle. Interacts with YPT11 and MMR1 to accelerate mitochondrial distribution to the bud. Interacts with SHE4 and localizes it to the bud tip. Interacts with RHO3 and SMY1, putative regulators of MYO2 function. Interacts with SRO7.14 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
INP2Q038243EBI-11659,EBI-27354
KAR9P325262EBI-11659,EBI-9516
SHE4P515343EBI-11659,EBI-17086

GO - Molecular functioni

  • actin filament binding Source: SGD
  • calmodulin binding Source: SGD

Protein-protein interaction databases

BioGridi34711. 220 interactors.
DIPiDIP-2308N.
IntActiP19524. 45 interactors.
MINTiMINT-440498.

Structurei

Secondary structure

11574
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi807 – 829Combined sources23
Helixi855 – 877Combined sources23
Helixi1153 – 1165Combined sources13
Helixi1167 – 1176Combined sources10
Turni1177 – 1181Combined sources5
Helixi1195 – 1198Combined sources4
Helixi1200 – 1214Combined sources15
Helixi1218 – 1237Combined sources20
Helixi1241 – 1243Combined sources3
Helixi1244 – 1271Combined sources28
Helixi1281 – 1325Combined sources45
Turni1332 – 1335Combined sources4
Helixi1355 – 1371Combined sources17
Helixi1376 – 1399Combined sources24
Helixi1407 – 1426Combined sources20
Helixi1432 – 1435Combined sources4
Helixi1437 – 1445Combined sources9
Helixi1453 – 1462Combined sources10
Turni1463 – 1465Combined sources3
Helixi1468 – 1477Combined sources10
Helixi1489 – 1504Combined sources16
Helixi1505 – 1507Combined sources3
Helixi1533 – 1536Combined sources4
Helixi1556 – 1567Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1M45X-ray1.65B806-830[»]
1M46X-ray2.10B854-878[»]
1N2DX-ray2.00C806-853[»]
2F6HX-ray2.25X1152-1570[»]
ProteinModelPortaliP19524.
SMRiP19524.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP19524.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini70 – 781Myosin motorAdd BLAST712
Domaini784 – 806IQ 1PROSITE-ProRule annotationAdd BLAST23
Domaini807 – 831IQ 2PROSITE-ProRule annotationAdd BLAST25
Domaini832 – 855IQ 3PROSITE-ProRule annotationAdd BLAST24
Domaini856 – 879IQ 4PROSITE-ProRule annotationAdd BLAST24
Domaini880 – 902IQ 5PROSITE-ProRule annotationAdd BLAST23
Domaini903 – 932IQ 6PROSITE-ProRule annotationAdd BLAST30
Domaini1226 – 1501DilutePROSITE-ProRule annotationAdd BLAST276

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni443 – 523Actin-bindingBy similarityAdd BLAST81
Regioni1087 – 1574Non alpha-helical, tail domainAdd BLAST488

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili933 – 1088Add BLAST156

Domaini

The myosin motor domain binds to actin.
The IQ domains provide the interaction surface for the myosin light chain MLC1.
The coiled-coiled domain is necessary for dimerization.
The tail domain is a globular cargo-binding domain involved in vectorial vesicle transport.

Sequence similaritiesi

Contains 1 dilute domain.PROSITE-ProRule annotation
Contains 6 IQ domains.PROSITE-ProRule annotation
Contains 1 myosin motor domain.Curated

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

GeneTreeiENSGT00840000129687.
HOGENOMiHOG000171839.
InParanoidiP19524.
KOiK10357.
OMAiHNDISAG.
OrthoDBiEOG092C04K7.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR002710. Dilute_dom.
IPR000048. IQ_motif_EF-hand-BS.
IPR001609. Myosin_head_motor_dom.
IPR008989. Myosin_S1_N.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF01843. DIL. 1 hit.
PF00063. Myosin_head. 1 hit.
[Graphical view]
PRINTSiPR00193. MYOSINHEAVY.
SMARTiSM01132. DIL. 1 hit.
SM00015. IQ. 4 hits.
SM00242. MYSc. 1 hit.
[Graphical view]
SUPFAMiSSF50084. SSF50084. 1 hit.
SSF52540. SSF52540. 2 hits.
PROSITEiPS51126. DILUTE. 1 hit.
PS50096. IQ. 1 hit.
PS51456. MYOSIN_MOTOR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P19524-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSFEVGTRCW YPHKELGWIG AEVIKNEFND GKYHLELQLE DDEIVSVDTK
60 70 80 90 100
DLNNDKDQSL PLLRNPPILE ATEDLTSLSY LNEPAVLHAI KQRYSQLNIY
110 120 130 140 150
TYSGIVLIAT NPFDRVDQLY TQDMIQAYAG KRRGELEPHL FAIAEEAYRL
160 170 180 190 200
MKNDKQNQTI VVSGESGAGK TVSAKYIMRY FASVEEENSA TVQHQVEMSE
210 220 230 240 250
TEQKILATNP IMEAFGNAKT TRNDNSSRFG KYLEILFDKD TSIIGARIRT
260 270 280 290 300
YLLERSRLVY QPPIERNYHI FYQLMAGLPA QTKEELHLTD ASDYFYMNQG
310 320 330 340 350
GDTKINGIDD AKEYKITVDA LTLVGITKET QHQIFKILAA LLHIGNIEIK
360 370 380 390 400
KTRNDASLSA DEPNLKLACE LLGIDAYNFA KWVTKKQIIT RSEKIVSNLN
410 420 430 440 450
YSQALVAKDS VAKFIYSALF DWLVENINTV LCNPAVNDQI SSFIGVLDIY
460 470 480 490 500
GFEHFEKNSF EQFCINYANE KLQQEFNQHV FKLEQEEYVK EEIEWSFIEF
510 520 530 540 550
NDNQPCIDLI ENKLGILSLL DEESRLPAGS DESWTQKLYQ TLDKSPTNKV
560 570 580 590 600
FSKPRFGQTK FIVSHYALDV AYDVEGFIEK NRDTVSDGHL EVLKASTNET
610 620 630 640 650
LINILEGLEK AAKKLEEAKK LELEQAGSKK PGPIRTVNRK PTLGSMFKQS
660 670 680 690 700
LIELMNTINS TNVHYIRCIK PNADKEAWQF DNLMVLSQLR ACGVLETIRI
710 720 730 740 750
SCAGFPSRWT FEEFVLRYYI LIPHEQWDLI FKKKETTEED IISVVKMILD
760 770 780 790 800
ATVKDKSKYQ IGNTKIFFKA GMLAYLEKLR SNKMHNSIVM IQKKIRAKYY
810 820 830 840 850
RKQYLQISQA IKYLQNNIKG FIIRQRVNDE MKVNCATLLQ AAYRGHSIRA
860 870 880 890 900
NVFSVLRTIT NLQKKIRKEL KQRQLKQEHE YNAAVTIQSK VRTFEPRSRF
910 920 930 940 950
LRTKKDTVVV QSLIRRRAAQ RKLKQLKADA KSVNHLKEVS YKLENKVIEL
960 970 980 990 1000
TQNLASKVKE NKEMTERIKE LQVQVEESAK LQETLENMKK EHLIDIDNQK
1010 1020 1030 1040 1050
SKDMELQKTI ENNLQSTEQT LKDAQLELED MVKQHDELKE ESKKQLEELE
1060 1070 1080 1090 1100
QTKKTLVEYQ TLNGDLQNEV KSLKEEIARL QTAMSLGTVT TSVLPQTPLK
1110 1120 1130 1140 1150
DVMGGGASNF NNMMLENSDL SPNDLNLKSR STPSSGNNHI DSLSVDRENG
1160 1170 1180 1190 1200
VNATQINEEL YRLLEDTEIL NQEITEGLLK GFEVPDAGVA IQLSKRDVVY
1210 1220 1230 1240 1250
PARILIIVLS EMWRFGLTKQ SESFLAQVLT TIQKVVTQLK GNDLIPSGVF
1260 1270 1280 1290 1300
WLANVRELYS FVVFALNSIL TEETFKNGMT DEEYKEYVSL VTELKDDFEA
1310 1320 1330 1340 1350
LSYNIYNIWL KKLQKQLQKK AINAVVISES LPGFSAGETS GFLNKIFANT
1360 1370 1380 1390 1400
EEYTMDDILT FFNSIYWCMK SFHIENEVFH AVVTTLLNYV DAICFNELIM
1410 1420 1430 1440 1450
KRNFLSWKRG LQLNYNVTRL EEWCKTHGLT DGTECLQHLI QTAKLLQVRK
1460 1470 1480 1490 1500
YTIEDIDILR GICYSLTPAQ LQKLISQYQV ADYESPIPQE ILRYVADIVK
1510 1520 1530 1540 1550
KEAALSSSGN DSKGHEHSSS IFITPETGPF TDPFSLIKTR KFDQVEAYIP
1560 1570
AWLSLPSTKR IVDLVAQQVV QDGH
Length:1,574
Mass (Da):180,680
Last modified:February 1, 1991 - v1
Checksum:i1F7E2887C1E59D54
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M35532 Genomic DNA. Translation: AAA34810.1.
Z75234 Genomic DNA. Translation: CAA99646.1.
Z75235 Genomic DNA. Translation: CAA99648.1.
X90565 Genomic DNA. Translation: CAA62184.1.
Z49821 Genomic DNA. Translation: CAA89973.1.
BK006948 Genomic DNA. Translation: DAA11089.1.
PIRiA38454.
RefSeqiNP_014971.1. NM_001183746.1.

Genome annotation databases

EnsemblFungiiYOR326W; YOR326W; YOR326W.
GeneIDi854504.
KEGGisce:YOR326W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M35532 Genomic DNA. Translation: AAA34810.1.
Z75234 Genomic DNA. Translation: CAA99646.1.
Z75235 Genomic DNA. Translation: CAA99648.1.
X90565 Genomic DNA. Translation: CAA62184.1.
Z49821 Genomic DNA. Translation: CAA89973.1.
BK006948 Genomic DNA. Translation: DAA11089.1.
PIRiA38454.
RefSeqiNP_014971.1. NM_001183746.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1M45X-ray1.65B806-830[»]
1M46X-ray2.10B854-878[»]
1N2DX-ray2.00C806-853[»]
2F6HX-ray2.25X1152-1570[»]
ProteinModelPortaliP19524.
SMRiP19524.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34711. 220 interactors.
DIPiDIP-2308N.
IntActiP19524. 45 interactors.
MINTiMINT-440498.

PTM databases

iPTMnetiP19524.

Proteomic databases

MaxQBiP19524.
PRIDEiP19524.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYOR326W; YOR326W; YOR326W.
GeneIDi854504.
KEGGisce:YOR326W.

Organism-specific databases

EuPathDBiFungiDB:YOR326W.
SGDiS000005853. MYO2.

Phylogenomic databases

GeneTreeiENSGT00840000129687.
HOGENOMiHOG000171839.
InParanoidiP19524.
KOiK10357.
OMAiHNDISAG.
OrthoDBiEOG092C04K7.

Enzyme and pathway databases

BioCyciYEAST:G3O-33803-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP19524.
PROiP19524.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR002710. Dilute_dom.
IPR000048. IQ_motif_EF-hand-BS.
IPR001609. Myosin_head_motor_dom.
IPR008989. Myosin_S1_N.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF01843. DIL. 1 hit.
PF00063. Myosin_head. 1 hit.
[Graphical view]
PRINTSiPR00193. MYOSINHEAVY.
SMARTiSM01132. DIL. 1 hit.
SM00015. IQ. 4 hits.
SM00242. MYSc. 1 hit.
[Graphical view]
SUPFAMiSSF50084. SSF50084. 1 hit.
SSF52540. SSF52540. 2 hits.
PROSITEiPS51126. DILUTE. 1 hit.
PS50096. IQ. 1 hit.
PS51456. MYOSIN_MOTOR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMYO2_YEAST
AccessioniPrimary (citable) accession number: P19524
Secondary accession number(s): D6W323
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: November 30, 2016
This is version 185 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 4339 molecules/cell in log phase SD medium.1 Publication
Moves with an average velocity of 3 um/s along actin cables.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XV
    Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

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.