Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Myosin-7

Gene

Myh7

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)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi178 – 1858ATP

GO - Molecular functioni

  • ATPase activity Source: RGD
  • ATP binding Source: RGD
  • microfilament motor activity Source: RGD
  • protein heterodimerization activity Source: RGD
  • protein homodimerization activity Source: RGD

GO - Biological processi

  • muscle contraction 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-7
Alternative name(s):
Myosin heavy chain 7
Myosin heavy chain slow isoform
Short name:
MyHC-slow
Myosin heavy chain, cardiac muscle beta isoform
Short name:
MyHC-beta
Gene namesi
Name:Myh7
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi62030. Myh7.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm, Thick filament

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 19351935Myosin-7PRO_0000123411Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei129 – 1291N6,N6,N6-trimethyllysineSequence analysis
Cross-linki207 – 207Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki213 – 213Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei1510 – 15101PhosphoserineCombined sources
Cross-linki1531 – 1531Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki1537 – 1537Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity

Keywords - PTMi

Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP02564.
PRIDEiP02564.

PTM databases

iPTMnetiP02564.
PhosphoSiteiP02564.

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). Interacts with ECM29 (By similarity).By similarity

GO - Molecular functioni

  • protein heterodimerization activity Source: RGD
  • protein homodimerization activity Source: RGD

Protein-protein interaction databases

IntActiP02564. 1 interaction.
MINTiMINT-4655412.
STRINGi10116.ENSRNOP00000024186.

Structurei

3D structure databases

ProteinModelPortaliP02564.
SMRiP02564. Positions 838-963.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini85 – 778694Myosin motorAdd
BLAST
Domaini781 – 81030IQPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni655 – 67723Actin-bindingAdd
BLAST
Regioni757 – 77115Actin-bindingAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili840 – 19351096Sequence analysisAdd
BLAST

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.
InParanoidiP02564.
KOiK17751.
PhylomeDBiP02564.

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.

P02564-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADREMAAFG AGAPFLRKSE KERLEAQTRP FDLKKDVFVP DDKEEFVKAK
60 70 80 90 100
IVSREGGKVT AETENGKTVT VKEDQVMQQN PPKFDKIEDM AMLTFLHEPA
110 120 130 140 150
VLYNLKERYA SWMIYTYSGL FCVTVNPYKW LPVYNAQVVA AYRGKKRSEA
160 170 180 190 200
PPHIFSISDN AYQYMLTDRE NQSILITGES GAGKTVNTKR VIQYFAVIAA
210 220 230 240 250
IGDRSKKDQT PGKGTLEDQI IQANPALEAF GNAKTVRNDN SSRFGKFIRI
260 270 280 290 300
HFGATGKLAS ADIETYLLEK SRVIFQLKAE RDYHIFYQIL SNKKPELLDM
310 320 330 340 350
LLITNNPYDY AFFSQGETTV ASIDDSEEHM ATDSAFDVLG FTPEEKNSIY
360 370 380 390 400
KLTGAIMHFG NMKFKQKQRE EQAEPDGTEE ADKSAYLMGL NSADLLKGLC
410 420 430 440 450
HPRVKVGNEY VTKGQNVQQV AYAIGALAKS VYEKMFNWMV TRINATLETK
460 470 480 490 500
QPRQYFIGVL DIAGFEIFDF NSFEQLCINF TNEKLQQFFN HHMFVLEQEE
510 520 530 540 550
YKKEGIEWTF IDFGMDLQAC IDLIEKPMGI MSILEEECMF PKATDMTFKA
560 570 580 590 600
KLYDNHLGKS NNFQKPRNIK GKQEAHFSLI HYAGTVDYNI LGWLQKNKDP
610 620 630 640 650
LNETVVGLYQ KSSLKLLSNL FANYAGADAP VDKGKGKAKK GSSFQTVSAL
660 670 680 690 700
HRENLNKLMT NLRSTHPHFV RCIIPNETKS PGVMDNPLVM HQLRCNGVLE
710 720 730 740 750
GIRICRKGFP NRILYGDFRQ RYRILNPAAI PEGQFIDSRK GAEKLLGSLD
760 770 780 790 800
IDHNQYKFGH TKVFFKAGLL GLLEEMRDER LSRIITRIQA QSRGVLSRME
810 820 830 840 850
FKKLLERRDS LLIIQWNIRA FMGVKNWPWM KLYFKIKPLL KSAETEKEMA
860 870 880 890 900
NMKEEFGRVK DALEKSEARR KELEEKMVSL LQEKNDLQLQ VQAEQDNLAD
910 920 930 940 950
AEERCDQLIK NKIQLEAKVK EMTERLEDEE EMNAELTAKK RKLEDECSEL
960 970 980 990 1000
KRDIDDLELT LAKVEKEKHA TENKVKNLTE EMAGLDEIIV KLTKEKKALQ
1010 1020 1030 1040 1050
EAHQQALDDL QAEEDKVNTL TKAKVKLEQQ VDDLEGSLDQ DKKVRMDLER
1060 1070 1080 1090 1100
AKRKLEGDLK LTQESIMDLE NDKQQLDERL KKKDFELNAL NARIEDEQAL
1110 1120 1130 1140 1150
GSQLQKKLKE LQARIEELEE ELEAERTARA KVEKLRSDLS RELEEISERL
1160 1170 1180 1190 1200
EEAGGATSVQ IEMNKKREAE FQKMRRDLEE ATLQHEATAA ALRKKHADSV
1210 1220 1230 1240 1250
AELGEQIDNL QRVKQKLEKE KSEFKLELDD VTSNMEQIIK AKANLEKMCR
1260 1270 1280 1290 1300
TLEDQMNEHR SKAEETQRSV NDLTRQRAKL QTENGELSRQ LDEKEALISQ
1310 1320 1330 1340 1350
LTRGKLTYTQ QLEDLKRQLE EEVKAKNALA HALQSARHDC DLLREQYEEE
1360 1370 1380 1390 1400
TEAKAELQRV LSKANSEVAQ WRTKYETDAI QRTEELEEAK KKLAQRLQDA
1410 1420 1430 1440 1450
EEAVEAVNAK CSSLEKTKHR LQNEIEDLMV DVERSNAAAA ALDKKQRNFD
1460 1470 1480 1490 1500
KILVEWKQKY EESQSELESS QKEARSLSTE LFKLKNAYEE SLEHLETFKR
1510 1520 1530 1540 1550
ENKNLQEEIS DLTEQLGSTG KSIHELEKIR KQLEAEKLEL QSALEEAEAS
1560 1570 1580 1590 1600
LEHEEGKILR AQLEFNQIKA EIERKLAEKD EEMEQAKRNH LRVVDSLQTS
1610 1620 1630 1640 1650
LDAETRSRNE ALRVKKKMEG DLNEMEIQLS HANRMAAEAQ KQVKSLQSLL
1660 1670 1680 1690 1700
KDTQIQLDDA VRANDDLKEN IAIVERRNNL LQAELEELRA VVEQTERSRK
1710 1720 1730 1740 1750
LAEQELIETS ERVQLLHSQN TSLINQKKKM DADLSQLQTE VEEAVQECRN
1760 1770 1780 1790 1800
AEEKAKKAIT DAAMMAEELK KEQDTSAHLE RMKNNMEQTI KDLQHRLDEA
1810 1820 1830 1840 1850
EQIALKGGKK QLQKLEARVR ELENELEAEQ KRNAESVKGM RKSERRIKEL
1860 1870 1880 1890 1900
TYQTEEDRKN LLRLQDLVDK LQLKVKAYKR QAEEAEEQAN TNLSKFRKVQ
1910 1920 1930
HELDEAEERA DIAESQVNKL RAKSRDIGAK GLNEE
Length:1,935
Mass (Da):223,083
Last modified:October 1, 1989 - v2
Checksum:iC8376C324A7BD82B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1529 – 15313IRK → VRR in AAA41654 (PubMed:7045682).Curated
Sequence conflicti1731 – 17311D → H in AAA41654 (PubMed:7045682).Curated
Sequence conflicti1784 – 17841N → K in AAA41654 (PubMed:7045682).Curated
Sequence conflicti1851 – 18511T → N in AAA41654 (PubMed:7045682).Curated
Sequence conflicti1858 – 18581R → K in AAA41654 (PubMed:7045682).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15939 mRNA. Translation: CAA34065.1.
J00752 mRNA. Translation: AAA41654.1.
M32698 mRNA. Translation: AAA41659.1.
PIRiS06006.
RefSeqiNP_058936.1. NM_017240.2.
UniGeneiRn.225886.
Rn.54399.

Genome annotation databases

GeneIDi29557.
KEGGirno:29557.
UCSCiRGD:62030. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15939 mRNA. Translation: CAA34065.1.
J00752 mRNA. Translation: AAA41654.1.
M32698 mRNA. Translation: AAA41659.1.
PIRiS06006.
RefSeqiNP_058936.1. NM_017240.2.
UniGeneiRn.225886.
Rn.54399.

3D structure databases

ProteinModelPortaliP02564.
SMRiP02564. Positions 838-963.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP02564. 1 interaction.
MINTiMINT-4655412.
STRINGi10116.ENSRNOP00000024186.

PTM databases

iPTMnetiP02564.
PhosphoSiteiP02564.

Proteomic databases

PaxDbiP02564.
PRIDEiP02564.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi29557.
KEGGirno:29557.
UCSCiRGD:62030. rat.

Organism-specific databases

CTDi4625.
RGDi62030. Myh7.

Phylogenomic databases

eggNOGiKOG0161. Eukaryota.
COG5022. LUCA.
HOGENOMiHOG000173959.
HOVERGENiHBG004704.
InParanoidiP02564.
KOiK17751.
PhylomeDBiP02564.

Miscellaneous databases

PROiP02564.

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...

Publicationsi

« Hide 'large scale' publications
  1. "Complete nucleotide sequence of full length cDNA for rat beta cardiac myosin heavy chain."
    Kraft R., Bravo-Zehnder M., Taylor D., Leinwand L.A.
    Nucleic Acids Res. 17:7529-7530(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Heart.
  2. "Full-length rat alpha and beta cardiac myosin heavy chain sequences. Comparisons suggest a molecular basis for functional differences."
    McNally E.M., Kraft R., Bravo-Zehnder M., Taylor D., Leinwand L.A.
    J. Mol. Biol. 210:665-671(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISCUSSION OF SEQUENCE.
  3. "Molecular characterization of two myosin heavy chain genes expressed in the adult heart."
    Mahdavi V., Periasamy M., Nadal-Ginard B.
    Nature 297:659-664(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1524-1935.
  4. "Cardiac myosin heavy chain isozymic transitions during development and under pathological conditions are regulated at the level of mRNA availability."
    Mahdavi V., Lompre A.M., Chambers A.P., Nadal-Ginard B.
    Eur. Heart J. 5:181-191(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1871-1935.
    Strain: Wistar.
    Tissue: Heart.
  5. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1510, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiMYH7_RAT
AccessioniPrimary (citable) accession number: P02564
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: October 1, 1989
Last modified: July 6, 2016
This is version 146 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-7 (MYO7).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.