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Protein

Myosin-6

Gene

Myh6

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Muscle contraction.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi177 – 184ATP8

GO - Molecular functioni

  • ATP binding Source: RGD
  • calcium-dependent ATPase activity Source: RGD
  • identical protein binding Source: IntAct
  • microfilament motor activity Source: RGD
  • protein heterodimerization activity Source: RGD
  • protein homodimerization activity Source: RGD

GO - Biological processi

  • muscle contraction Source: RGD
  • response to heat Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Motor protein, Muscle protein, Myosin

Keywords - Ligandi

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

Names & Taxonomyi

Protein namesi
Recommended name:
Myosin-6
Alternative name(s):
Myosin heavy chain 6
Myosin heavy chain, cardiac muscle alpha isoform
Short name:
MyHC-alpha
Gene namesi
Name:Myh6
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi62029. Myh6.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: RGD
  • mitochondrion Source: RGD
  • muscle myosin complex Source: RGD
  • myofibril Source: RGD
  • myosin filament Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Thick filament

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001234041 – 1938Myosin-6Add BLAST1938

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei128N6,N6,N6-trimethyllysineSequence analysis1
Modified residuei378PhosphothreonineCombined sources1
Modified residuei416PhosphoserineCombined sources1
Modified residuei1089PhosphoserineCombined sources1
Modified residuei1138PhosphoserineCombined sources1
Modified residuei1260PhosphotyrosineCombined sources1
Modified residuei1270PhosphoserineCombined sources1
Modified residuei1276PhosphothreonineCombined sources1
Modified residuei1283PhosphothreonineCombined sources1
Modified residuei1308PhosphoserineCombined sources1
Modified residuei1309PhosphotyrosineCombined sources1
Modified residuei1310PhosphothreonineCombined sources1
Modified residuei1511PhosphoserineCombined sources1
Modified residuei1514PhosphothreonineCombined sources1
Modified residuei1680PhosphothreonineCombined sources1

Keywords - PTMi

Methylation, Phosphoprotein

Proteomic databases

PaxDbiP02563.
PeptideAtlasiP02563.
PRIDEiP02563.

PTM databases

iPTMnetiP02563.
PhosphoSitePlusiP02563.

Interactioni

Subunit structurei

Muscle myosin is a hexameric protein that consists of 2 heavy chain subunits (MHC), 2 alkali light chain subunits (MLC) and 2 regulatory light chain subunits (MLC-2).

Binary interactionsi

WithEntry#Exp.IntActNotes
itself6EBI-6122328,EBI-6122328

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • protein heterodimerization activity Source: RGD
  • protein homodimerization activity Source: RGD

Protein-protein interaction databases

DIPiDIP-41048N.
IntActiP02563. 1 interactor.
MINTiMINT-348910.
STRINGi10116.ENSRNOP00000023301.

Structurei

3D structure databases

ProteinModelPortaliP02563.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini84 – 779Myosin motorAdd BLAST696
Domaini782 – 811IQPROSITE-ProRule annotationAdd BLAST30

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni656 – 678Actin-bindingAdd BLAST23
Regioni758 – 772Actin-bindingAdd BLAST15
Regioni789 – 806Calmodulin-bindingBy similarityAdd BLAST18
Regioni815 – 832Calmodulin-bindingBy similarityAdd BLAST18

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili842 – 1938Sequence analysisAdd BLAST1097

Domaini

The rodlike tail sequence is highly repetitive, showing cycles of a 28-residue repeat pattern composed of 4 heptapeptides, characteristic for alpha-helical coiled coils.
Limited proteolysis of myosin heavy chain produces 1 light meromyosin (LMM) and 1 heavy meromyosin (HMM). HMM can be further cleaved into 2 globular subfragments (S1) and 1 rod-shaped subfragment (S2).Curated

Sequence similaritiesi

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

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG0161. Eukaryota.
COG5022. LUCA.
HOGENOMiHOG000173959.
HOVERGENiHBG004704.
InParanoidiP02563.
PhylomeDBiP02563.

Family and domain databases

Gene3Di4.10.270.10. 1 hit.
InterProiIPR000048. IQ_motif_EF-hand-BS.
IPR027401. Myosin-like_IQ_dom.
IPR001609. Myosin_head_motor_dom.
IPR004009. Myosin_N.
IPR002928. Myosin_tail.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00063. Myosin_head. 1 hit.
PF02736. Myosin_N. 1 hit.
PF01576. Myosin_tail_1. 1 hit.
[Graphical view]
PRINTSiPR00193. MYOSINHEAVY.
SMARTiSM00242. MYSc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS50096. IQ. 1 hit.
PS51456. MYOSIN_MOTOR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P02563-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTDAQMADFG AARYLRKSEK ERLEAQTRPF DIRTECFVPD DKEEYVKAKI
60 70 80 90 100
VSREGGKVTA ETENGKTVTV KEDQVMQQNP PKFDKIEDMA MLTFLHEPAV
110 120 130 140 150
LYNLKERYAA WMIYTYSGLF CVTVNPYKWL PVYNAEVVAA YRGKKRSEAP
160 170 180 190 200
PHIFSISDNA YQYMLTDREN QSILITGESG AGKTVNTKRV IQYFASIAAI
210 220 230 240 250
GDRSKKDNPN ANKGTLEDQI IQANPALEAF GNAKTVRNDN SSRFGKFIRI
260 270 280 290 300
HFGATGKLAS ADIETYLLEK SRVIFQLKAE RNYHIFYQIL SNKKPELLDM
310 320 330 340 350
LLVTNNPYDY AFVSQGEVSV ASIDDSEELL ATDSAFDVLG FTAEEKAGVY
360 370 380 390 400
KLTGAIMHYG NMKFKQKQRE EQAEPDGTED ADKSAYLMGL NSADLLKGLC
410 420 430 440 450
HPRVKVGNEY VTKGQSVQQV YYSIGALAKS VYEKMFNWMV TRINATLETK
460 470 480 490 500
QPRQYFIGVL DIAGFEIFDF NSFEQLCINF TNEKLQQFFN HHMFVLEQEE
510 520 530 540 550
YKKEGIEWEF IDFGMDLQAC IDLIEKPMGI MSILEEECMF PKATDMTFKA
560 570 580 590 600
KLYDNHLGKS NNFQKPRNVK GKQEAHFSLV HYAGTVDYNI LGWLEKNKDP
610 620 630 640 650
LNETVVGLYQ KSSLKLMATL FSTYASADTG DSGKGKGGKK KGSSFQTVSA
660 670 680 690 700
LHRENLNKLM TNLRTTHPHF VRCIIPNERK APGVMDNPLV MHQLRCNGVL
710 720 730 740 750
EGIRICRKGF PNRILYGDFR QRYRILNPAA IPEGQFIDSG KGAEKLLGSL
760 770 780 790 800
DIDHNQYKFG HTKVFFKAGL LGLLEEMRDE RLSRIITRIQ AQARGQLMRI
810 820 830 840 850
EFKKMVERRD ALLVIQWNIR AFMGVKNWPW MKLYFKIKPL LKSAETEKEM
860 870 880 890 900
ANMKEEFGRV KDALEKSEAR RKELEEKMVS LLQEKNDLQL QVQAEQDNLA
910 920 930 940 950
DAEERCDQLI KNKIQLEAKV KEMTERLEDE EEMNAELTAK KRKLEDECSE
960 970 980 990 1000
LKKDIDDLEL TLAKVEKEKH ATENKVKNLT EEMAGLDEII AKLTKEKKAL
1010 1020 1030 1040 1050
QEAHQQALDD LQAEEDKVNT LTKSKVKLEQ QVDDLEGSLE QEKKVRMDLE
1060 1070 1080 1090 1100
RAKRKLEGDL KLTQESIMDL ENDKLQLEEK LKKKEFDISQ QNSKIEDEQA
1110 1120 1130 1140 1150
LALQLQKKLK ENQARIEELE EELEAERTAR AKVEKLRSDL TRELEEISER
1160 1170 1180 1190 1200
LEEAGGATSV QIEMNKKREA EFQKMRRDLE EATLQHEATA AALRKKHADS
1210 1220 1230 1240 1250
VAELGEQIDN LQRVKQKLEK EKSEFKLELD DVTSHMEQII KAKANLEKVS
1260 1270 1280 1290 1300
RTLEDQANEY RVKLEEAQRS LNDFTTQRAK LQTENGELAR QLEEKEALIW
1310 1320 1330 1340 1350
QLTRGKLSYT QQMEDLKRQL EEEGKAKNAL AHALQSARHD CDLLREQYEE
1360 1370 1380 1390 1400
EMEAKAELQR VLSKANSEVA QWRTKYETDA IQRTEELEEA KKKLAQRLQD
1410 1420 1430 1440 1450
AEEAVEAVNA KCSSLEKTKH RLQNEIEDLM VDVERSNAAA AALDKKQRNF
1460 1470 1480 1490 1500
DKILAEWKQK YEESQSELES SQKEARSLST ELFKLKNAYE ESLEHLETFK
1510 1520 1530 1540 1550
RENKNLQEEI SDLTEQLGEG GKNVHELEKI RKQLEVEKLE LQSALEEAEA
1560 1570 1580 1590 1600
SLEHEEGKIL RAQLEFNQIK AEIERKLAEK DEEMEQAKRN HLRVVDSLQT
1610 1620 1630 1640 1650
SLDAETRSRN EALRVKKKME GDLNEMEIQL SQANRIASEA QKHLKNAQAH
1660 1670 1680 1690 1700
LKDTQLQLDD AVRANDDLKE NIAIVERRNT LLQAELEELR AVVEQTERSR
1710 1720 1730 1740 1750
KLAEQELIET SERVQLLHSQ NTSLINQKKK MDADLSQLQT EVEEAVQECR
1760 1770 1780 1790 1800
NAEEKAKKAI TDAAMMAEEL KKEQDTSAHL ERMKKNMEQT IKDLQHRLDE
1810 1820 1830 1840 1850
AEQIALKGGK KQLQKLEARV RELENELEAE QKRNAESVKG MRKSERRIKE
1860 1870 1880 1890 1900
LTYQTEEDKK NLVRLQDLVD KLQLKVKAYK RQAEEAEEQA NTNLSKFRKV
1910 1920 1930
QHELDEAEER ADIAESQVNK LRAKSRDIGA KQKMHDEE
Length:1,938
Mass (Da):223,508
Last modified:October 1, 1989 - v2
Checksum:iD7BD33FC2B19E3C2
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti13R → AP (PubMed:6585819).Curated1
Sequence conflicti46V → A in AAA41648 (PubMed:6585819).Curated1
Sequence conflicti51 – 52VS → AP in AAA41648 (PubMed:6585819).Curated2
Sequence conflicti87E → Q in AAA41648 (PubMed:6585819).Curated1
Sequence conflicti109Missing in AAA41648 (PubMed:6585819).Curated1
Sequence conflicti1566F → FF (PubMed:7045682).Curated1
Sequence conflicti1575R → S in AAA41653 (PubMed:7045682).Curated1
Sequence conflicti1721N → T (PubMed:7045682).Curated1
Sequence conflicti1852T → N in AAA41653 (PubMed:7045682).Curated1
Sequence conflicti1870D → N in AAA41653 (PubMed:7045682).Curated1
Sequence conflicti1934M → I (PubMed:7045682).Curated1
Sequence conflicti1934M → I (PubMed:6241892).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15938 mRNA. Translation: CAA34064.1.
K01464 Genomic DNA. Translation: AAA41648.1.
J00751 mRNA. Translation: AAA41653.1.
M32697 mRNA. Translation: AAA41658.1.
PIRiS06005.
UniGeneiRn.225886.
Rn.54399.

Genome annotation databases

UCSCiRGD:62029. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15938 mRNA. Translation: CAA34064.1.
K01464 Genomic DNA. Translation: AAA41648.1.
J00751 mRNA. Translation: AAA41653.1.
M32697 mRNA. Translation: AAA41658.1.
PIRiS06005.
UniGeneiRn.225886.
Rn.54399.

3D structure databases

ProteinModelPortaliP02563.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-41048N.
IntActiP02563. 1 interactor.
MINTiMINT-348910.
STRINGi10116.ENSRNOP00000023301.

PTM databases

iPTMnetiP02563.
PhosphoSitePlusiP02563.

Proteomic databases

PaxDbiP02563.
PeptideAtlasiP02563.
PRIDEiP02563.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

UCSCiRGD:62029. rat.

Organism-specific databases

RGDi62029. Myh6.

Phylogenomic databases

eggNOGiKOG0161. Eukaryota.
COG5022. LUCA.
HOGENOMiHOG000173959.
HOVERGENiHBG004704.
InParanoidiP02563.
PhylomeDBiP02563.

Miscellaneous databases

PROiP02563.

Family and domain databases

Gene3Di4.10.270.10. 1 hit.
InterProiIPR000048. IQ_motif_EF-hand-BS.
IPR027401. Myosin-like_IQ_dom.
IPR001609. Myosin_head_motor_dom.
IPR004009. Myosin_N.
IPR002928. Myosin_tail.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00063. Myosin_head. 1 hit.
PF02736. Myosin_N. 1 hit.
PF01576. Myosin_tail_1. 1 hit.
[Graphical view]
PRINTSiPR00193. MYOSINHEAVY.
SMARTiSM00242. MYSc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS50096. IQ. 1 hit.
PS51456. MYOSIN_MOTOR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMYH6_RAT
AccessioniPrimary (citable) accession number: P02563
Secondary accession number(s): Q63351
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: October 1, 1989
Last modified: November 30, 2016
This is version 145 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

The cardiac alpha isoform is a 'fast' ATPase myosin, while the beta isoform is a 'slow' ATPase.

Caution

Represents a conventional myosin. This protein should not be confused with the unconventional myosin-6 (MYO6).Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 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.