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P24733 (MYS_AEQIR) Reviewed, UniProtKB/Swiss-Prot

Last modified September 21, 2011. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Myosin heavy chain, striated muscle
OrganismAequipecten irradians (Bay scallop) (Argopecten irradians)
Taxonomic identifier31199 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Mollusca › Bivalvia › Pteriomorphia › Pectinoida › Pectinoidea › Pectinidae › Argopecten

Protein attributes

Sequence length1938 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Muscle contraction.

Myosin is a protein that binds to F-actin and has ATPase activity that is activated by F-actin.

Subunit structure

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).

Subcellular location

Cytoplasm › myofibril. Note: Thick filaments of the myofibrils.

Sequence similarities

Contains 1 IQ domain.

Contains 1 myosin head-like domain.

Ontologies

Keywords
   Cellular componentCytoplasm
Thick filament
   DomainCoiled coil
   LigandATP-binding
Actin-binding
Calmodulin-binding
Nucleotide-binding
   Molecular functionMotor protein
Muscle protein
Myosin
   Technical term3D-structure
Gene Ontology (GO)
   Cellular componentmyofibril

Inferred from electronic annotation. Source: UniProtKB-SubCell

myosin filament

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

actin binding

Inferred from electronic annotation. Source: UniProtKB-KW

calmodulin binding

Inferred from electronic annotation. Source: UniProtKB-KW

motor activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 19381938Myosin heavy chain, striated muscle
PRO_0000123384

Regions

Domain1 – 777777Myosin head-like
Domain778 – 80528IQ
Nucleotide binding176 – 1838ATP By similarity
Region836 – 19381103Rodlike tail (S2 and LMM domains)
Coiled coil836 – 19381103 Potential

Secondary structure

1 ....................................................................................................................... 1938
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P24733 [UniParc].

Last modified March 1, 1992. Version 1.
Checksum: A5CCE4127D1A4896

FASTA1,938222,822
        10         20         30         40         50         60 
MNIDFSDPDF QYLAVDRKKL MKEQTAAFDG KKNCWVPDEK EGFASAEIQS SKGDEITVKI 

        70         80         90        100        110        120 
VADSSTRTVK KDDIQSMNPP KFEKLEDMAN MTYLNEASVL YNLRSRYTSG LIYTYSGLFC 

       130        140        150        160        170        180 
IAVNPYRRLP IYTDSVIAKY RGKRKTEIPP HLFSVADNAY QNMVTDRENQ SCLITGESGA 

       190        200        210        220        230        240 
GKTENTKKVI MYLAKVACAV KKKDEEASDK KEGSLEDQII QANPVLEAYG NAKTTRNNNS 

       250        260        270        280        290        300 
SRFGKFIRIH FGPTGKIAGA DIETYLLEKS RVTYQQSAER NYHIFYQICS NAIPELNDVM 

       310        320        330        340        350        360 
LVTPDSGLYS FINQGCLTVD NIDDVEEFKL CDEAFDILGF TKEEKQSMFK CTASILHMGE 

       370        380        390        400        410        420 
MKFKQRPREE QAESDGTAEA EKVAFLCGIN AGDLLKALLK PKVKVGTEMV TKGQNMNQVV 

       430        440        450        460        470        480 
NSVGALAKSL YDRMFNWLVR RVNKTLDTKA KRNYYIGVLD IAGFEIFDFN SFEQLCINYT 

       490        500        510        520        530        540 
NERLQQFFNH HMFILEQEEY KKEGIAWEFI DFGMDLQMCI DLIEKPMGIL SILEEECMFP 

       550        560        570        580        590        600 
KADDKSFQDK LYQNHMGKNR MFTKPGKPTR PNQGPAHFEL HHYAGNVPYS ITGWLEKNKD 

       610        620        630        640        650        660 
PINENVVALL GASKEPLVAE LFKAPEEPAG GGKKKKGKSS AFQTISAVHR ESLNKLMKNL 

       670        680        690        700        710        720 
YSTHPHFVRC IIPNELKQPG LVDAELVLHQ LQCNGVLEGI RICRKGFPSR LIYSEFKQRY 

       730        740        750        760        770        780 
SILAPNAIPQ GFVDGKTVSE KILAGLQMDP AEYRLGTTKV FFKAGVLGNL EEMRDERLSK 

       790        800        810        820        830        840 
IISMFQAHIR GYLIRKAYKK LQDQRIGLSV IQRNIRKWLV LRNWQWWKLY SKVKPLLSIA 

       850        860        870        880        890        900 
RQEEEMKEQL KQMDKMKEDL AKTERIKKEL EEQNVTLLEQ KNDLFLQLQT LEDSMGDQEE 

       910        920        930        940        950        960 
RVEKLIMQKA DFESQIKELE ERLLDEEDAA ADLEGIKKKM EADNANLKKD IGDLENTLQK 

       970        980        990       1000       1010       1020 
AEQDKAHKDN QISTLQGEIS QQDEHIGKLN KEKKALEEAN KKTSDSLQAE EDKCNHLNKL 

      1030       1040       1050       1060       1070       1080 
KAKLEQALDE LEDNLEREKK VRGDVEKAKR KVEQDLKSTQ ENVEDLERVK RELEENVRRK 

      1090       1100       1110       1120       1130       1140 
EAEISSLNSK LEDEQNLVSQ LQRKIKELQA RIEELEEELE AERNARAKVE KQRAELNREL 

      1150       1160       1170       1180       1190       1200 
EELGERLDEA GGATSAQIEL NKKREAELLK IRRDLEEASL QHEAQISALR KKHQDAANEM 

      1210       1220       1230       1240       1250       1260 
ADQVDQLQKV KSKLEKDKKD LKREMDDLES QMTHNMKNKG CSEKVMKQFE SQMSDLNARL 

      1270       1280       1290       1300       1310       1320 
EDSQRSINEL QSQKSRLQAE NSDLTRQLED AEHRVSVLSK EKSQLSSQLE DARRSLEEET 

      1330       1340       1350       1360       1370       1380 
RARSKLQNEV RNMHADMDAI REQLEEEQES KSDVQRQLSK ANNEIQQWRS KFESEGANRT 

      1390       1400       1410       1420       1430       1440 
EELEDQKRKL LGKLSEAEQT TEAANAKCSA LEKAKSRLQQ ELEDMSIEVD RANASVNQME 

      1450       1460       1470       1480       1490       1500 
KKQRAFDKTT AEWQAKVNSL QSELENSQKE SRGYSAELYR IKASIEEYQD SIGALRRENK 

      1510       1520       1530       1540       1550       1560 
NLADEIHDLT DQLSEGGRST HELDKARRRL EMEKEELQAA LEEAEGALEQ EEAKVMRAQL 

      1570       1580       1590       1600       1610       1620 
EIATVRNEID KRIQEKEEEF DNTRRNHQRA LESMQASLEA EAKGKADAMR IKKKLEQDIN 

      1630       1640       1650       1660       1670       1680 
ELEVALDASN RGKAEMEKTV KRYQQQIREM QTSIEEEQRQ RDEARESYNM AERRCTLMSG 

      1690       1700       1710       1720       1730       1740 
EVEELRAALE QAERARKASD NELADANDRV NELTSQVSSV QGQKRKLEGD INAMQTDLDE 

      1750       1760       1770       1780       1790       1800 
MHGELKGADE RCKKAMADAA RLADELRAEQ DHSNQVEKVR KNLESQVKEF QIRLDEAEAS 

      1810       1820       1830       1840       1850       1860 
SLKGGKKMIQ KLESRVHELE AELDNEQRRH AETQKNMRKA DRRLKELAFQ ADEDRKNQER 

      1870       1880       1890       1900       1910       1920 
LQELIDKLNA KIKTFKRQVE EAEEIAAINL AKYRKAQHEL EEAEERADTA DSTLQKFRAK 

      1930 
SRSSVSVQRS SVSVSASN

« Hide

References

[1]"Complete primary structure of a scallop striated muscle myosin heavy chain. Sequence comparison with other heavy chains reveals regions that might be critical for regulation."
Nyitray L., Goodwin E.B., Szent-Gyorgyi A.G.
J. Biol. Chem. 266:18469-18476(1991) [PubMed: 1917970] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Adductor muscle.
[2]"Nucleotide sequence of full length cDNA for a scallop striated muscle myosin heavy chain."
Nyitray L., Goodwin E.B., Szent-Gyorgyi A.G.
Nucleic Acids Res. 18:7158-7158(1990) [PubMed: 2263488] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Adductor muscle.
[3]"Structure of the regulatory domain of scallop myosin at 2.8-A resolution."
Xie X., Harrison D.H., Schlichting I., Sweet R.M., Kalabokis V.N., Szent-Gyorgyi A.G., Cohen C.
Nature 368:306-312(1994) [PubMed: 8127365] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 777-836.
[4]"Structure of the regulatory domain of scallop myosin at 2-A resolution: implications for regulation."
Houdusse A., Cohen C.
Structure 4:21-32(1996) [PubMed: 8805510] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 777-836.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X55714 mRNA. Translation: CAA39247.1.
PIRA40997.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1B7TX-ray2.50A1-835[»]
1DFKX-ray4.20A6-835[»]
1DFLX-ray4.20A/B5-835[»]
1KK7X-ray3.20A1-837[»]
1KK8X-ray2.30A1-837[»]
1KQMX-ray3.00A1-835[»]
1KWOX-ray3.80A1-835[»]
1L2OX-ray2.80A1-835[»]
1QVIX-ray2.54A1-840[»]
1S5GX-ray3.10A1-840[»]
1SCMX-ray2.80A777-836[»]
1SR6X-ray2.75A1-840[»]
1WDCX-ray2.00A774-837[»]
2W4Telectron microscopy35.00C5-835[»]
2W4Velectron microscopy35.00C5-835[»]
2W4Welectron microscopy35.00C5-835[»]
3BASX-ray2.30A/B835-885[»]
3BATX-ray2.30A/B/C/D835-885[»]
3JTDX-ray2.57A773-837[»]
3JVTX-ray2.10A773-837[»]
ProteinModelPortalP24733.
SMRP24733. Positions 6-921.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR000048. IQ_motif_EF-hand-BS.
IPR015650. Myosin_hc.
IPR001609. Myosin_head_motor_dom.
IPR004009. Myosin_N.
IPR002928. Myosin_tail.
[Graphical view]
PANTHERPTHR13140:SF22. Myosin_hc. 1 hit.
PfamPF00063. Myosin_head. 1 hit.
PF02736. Myosin_N. 1 hit.
PF01576. Myosin_tail_1. 1 hit.
[Graphical view]
PRINTSPR00193. MYOSINHEAVY.
SMARTSM00015. IQ. 1 hit.
SM00242. MYSc. 1 hit.
[Graphical view]
PROSITEPS50096. IQ. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMYS_AEQIR
AccessionPrimary (citable) accession number: P24733
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: March 1, 1992
Last modified: September 21, 2011
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents