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P10587 (MYH11_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 125. Feed History...

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

Names and origin

Protein namesRecommended name:
Myosin-11
Alternative name(s):
Myosin heavy chain 11
Myosin heavy chain, gizzard smooth muscle
Gene names
Name:MYH11
OrganismGallus gallus (Chicken) [Reference proteome]
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galliformes › Phasianidae › Phasianinae › Gallus

Protein attributes

Sequence length1979 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Muscle contraction.

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.

Domain

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.

Each myosin heavy chain can be split into 1 light meromyosin (LMM) and 1 heavy meromyosin (HMM). It can later be split further into 2 globular subfragments (S1) and 1 rod-shaped subfragment (S2).

Sequence similarities

Contains 1 IQ domain.

Contains 1 myosin head-like domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

MYL6P026072EBI-1027098,EBI-1027073

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.3
Chain2 – 19791978Myosin-11
PRO_0000123429

Regions

Domain2 – 791790Myosin head-like
Domain792 – 82130IQ
Nucleotide binding177 – 1848ATP
Region667 – 68923Actin-binding
Region768 – 78215Actin-binding
Region850 – 19791130Rodlike tail (S2 and LMM domains)
Coiled coil850 – 19791130 Potential

Amino acid modifications

Modified residue21Blocked amino end (Ser) Ref.3
Modified residue1281N6,N6,N6-trimethyllysine Ref.3

Experimental info

Sequence conflict205 – 21612KDTSI…GPSFS → RTPASLKVHLFP in CAA29793. Ref.1

Secondary structure

1 ....................................................................................................................... 1979
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P10587 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 2F583CDDD4D9557D

FASTA1,979228,796
        10         20         30         40         50         60 
MSQKPLSDDE KFLFVDKNFV NNPLAQADWS AKKLVWVPSE KHGFEAASIK EEKGDEVTVE 

        70         80         90        100        110        120 
LQENGKKVTL SKDDIQKMNP PKFSKVEDMA ELTCLNEASV LHNLRERYFS GLIYTYSGLF 

       130        140        150        160        170        180 
CVVINPYKQL PIYSEKIIDM YKGKKRHEMP PHIYAIADTA YRSMLQDRED QSILCTGESG 

       190        200        210        220        230        240 
AGKTENTKKV IQYLAVVASS HKGKKDTSIT QGPSFSYGEL EKQLLQANPI LEAFGNAKTV 

       250        260        270        280        290        300 
KNDNSSRFGK FIRINFDVTG YIVGANIETY LLEKSRAIRQ AKDERTFHIF YYLIAGASEQ 

       310        320        330        340        350        360 
MRNDLLLEGF NNYTFLSNGH VPIPAQQDDE MFQETLEAMT IMGFTEEEQT SILRVVSSVL 

       370        380        390        400        410        420 
QLGNIVFKKE RNTDQASMPD NTAAQKVCHL MGINVTDFTR SILTPRIKVG RDVVQKAQTK 

       430        440        450        460        470        480 
EQADFAIEAL AKAKFERLFR WILTRVNKAL DKTKRQGASF LGILDIAGFE IFEINSFEQL 

       490        500        510        520        530        540 
CINYTNEKLQ QLFNHTMFIL EQEEYQREGI EWNFIDFGLD LQPCIELIER PTNPPGVLAL 

       550        560        570        580        590        600 
LDEECWFPKA TDTSFVEKLI QEQGNHAKFQ KSKQLKDKTE FCILHYAGKV TYNASAWLTK 

       610        620        630        640        650        660 
NMDPLNDNVT SLLNQSSDKF VADLWKDVDR IVGLDQMAKM TESSLPSASK TKKGMFRTVG 

       670        680        690        700        710        720 
QLYKEQLTKL MTTLRNTNPN FVRCIIPNHE KRAGKLDAHL VLEQLRCNGV LEGIRICRQG 

       730        740        750        760        770        780 
FPNRIVFQEF RQRYEILAAN AIPKGFMDGK QACILMIKAL ELDPNLYRIG QSKIFFRTGV 

       790        800        810        820        830        840 
LAHLEEERDL KITDVIIAFQ AQCRGYLARK AFAKRQQQLT AMKVIQRNCA AYLKLRNWQW 

       850        860        870        880        890        900 
WRLFTKVKPL LQVTRQEEEM QAKDEELQRT KERQQKAEAE LKELEQKHTQ LCEEKNLLQE 

       910        920        930        940        950        960 
KLQAETELYA EAEEMRVRLA AKKQELEEIL HEMEARIEEE EERSQQLQAE KKKMQQQMLD 

       970        980        990       1000       1010       1020 
LEEQLEEEEA ARQKLQLEKV TADGKIKKME DDILIMEDQN NKLTKERKLL EERVSDLTTN 

      1030       1040       1050       1060       1070       1080 
LAEEEEKAKN LTKLKNKHES MISELEVRLK KEEKSRQELE KIKRKLEGES SDLHEQIAEL 

      1090       1100       1110       1120       1130       1140 
QAQIAELKAQ LAKKEEELQA ALARLEDETS QKNNALKKIR ELESHISDLQ EDLESEKAAR 

      1150       1160       1170       1180       1190       1200 
NKAEKQKRDL SEELEALKTE LEDTLDTTAT QQELRAKREQ EVTVLKRALE EETRTHEAQV 

      1210       1220       1230       1240       1250       1260 
QEMRQKHTQA VEELTEQLEQ FKRAKANLDK TKQTLEKDNA DLANEIRSLS QAKQDVEHKK 

      1270       1280       1290       1300       1310       1320 
KKLEVQLQDL QSKYSDGERV RTELNEKVHK LQIEVENVTS LLNEAESKNI KLTKDVATLG 

      1330       1340       1350       1360       1370       1380 
SQLQDTQELL QEETRQKLNV TTKLRQLEDD KNSLQEQLDE EVEAKQNLER HISTLTIQLS 

      1390       1400       1410       1420       1430       1440 
DSKKKLQEFT ATVETMEEGK KKLQREIESL TQQFEEKAAS YDKLEKTKNR LQQELDDLVV 

      1450       1460       1470       1480       1490       1500 
DLDNQRQLVS NLEKKQKKFD QMLAEEKNIS SKYADERDRA EAEAREKETK ALSLARALEE 

      1510       1520       1530       1540       1550       1560 
ALEAKEELER TNKMLKAEME DLVSSKDDVG KNVHELEKSK RTLEQQVEEM KTQLEELEDE 

      1570       1580       1590       1600       1610       1620 
LQAAEDAKLR LEVNMQAMKS QFERDLQARD EQNEEKRRQL LKQLHEHETE LEDERKQRAL 

      1630       1640       1650       1660       1670       1680 
AAAAKKKLEV DVKDLESQVD SANKAREEAI KQLRKLQAQM KDYQRDLDDA RAAREEIFAT 

      1690       1700       1710       1720       1730       1740 
ARENEKKAKN LEAELIQLQE DLAAAERARK QADLEKEEMA EELASANSGR TSLQDEKRRL 

      1750       1760       1770       1780       1790       1800 
EARIAQLEEE LDEEHSNIET MSDRMRKAVQ QAEQLNNELA TERATAQKNE NARQQLERQN 

      1810       1820       1830       1840       1850       1860 
KELRSKLQEM EGAVKSKFKS TIAALEAKIA SLEEQLEQEA REKQAAAKTL RQKDKKLKDA 

      1870       1880       1890       1900       1910       1920 
LLQVEDERKQ AEQYKDQAEK GNLRLKQLKR QLEEAEEESQ RINANRRKLQ RELDEATESN 

      1930       1940       1950       1960       1970 
DALGREVAAL KSKLRRGNEP VSFAPPRRSG GRRVIENATD GGEEEIDGRD GDFNGKASE

« Hide

References

[1]"Complete primary structure of vertebrate smooth muscle myosin heavy chain deduced from its complementary DNA sequence. Implications on topography and function of myosin."
Yanagisawa M., Hamada Y., Katsuragawa Y., Imamura M., Mikawa T., Masaki T.
J. Mol. Biol. 198:143-157(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]Masaki T.
Submitted (FEB-1989) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[3]"Amino acid sequence of the amino-terminal 24 kDa fragment of the heavy chain of chicken gizzard myosin."
Maita T., Onishi H., Yajima E., Matsuda G.
J. Biochem. 102:133-145(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-204, METHYLATION AT LYS-128.
[4]"Lys-65 and Glu-168 are the residues for carbodiimide-catalyzed cross-linking between the two heads of rigor smooth muscle heavy meromyosin."
Onishi H., Maita T., Matsuda G., Fujiwara K.
J. Biol. Chem. 265:19362-19368(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 54-64 AND 143-183.
[5]"Stability and photochemical properties of vanadate-trapped nucleotide complexes of gizzard myosin in the 6S and 10S conformations: identification of an active-site serine."
Cole D.G., Yount R.G.
Biochemistry 31:6186-6192(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 169-183.
[6]"Amino acid sequence of the 203-residue fragment of the heavy chain of chicken gizzard myosin containing the SH1-type cysteine residue."
Onishi H., Maita T., Miyanishi T., Watanabe S., Matsuda G.
J. Biochem. 100:1433-1447(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 653-855.
[7]"Crystal structure of a vertebrate smooth muscle myosin motor domain and its complex with the essential light chain: visualization of the pre-power stroke state."
Dominguez R., Freyzon Y., Trybus K.M., Cohen C.
Cell 94:559-571(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF 1-819, SEQUENCE REVISION TO 205-216.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X06546 mRNA. Translation: CAA29793.1.
IPIIPI00601453.
PIRS03166.
RefSeqNP_990605.1. NM_205274.1.
UniGeneGga.3225.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BR1X-ray3.50A/C/E/G3-819[»]
1BR2X-ray2.90A/B/C/D/E/F3-792[»]
1BR4X-ray3.62A/C/E/G3-819[»]
1I84electron microscopy20.00S/V3-1174[»]
3DTPelectron microscopy20.00A/B3-852[»]
3J04electron microscopy-A/D2-910[»]
DisProtDP00102.
ProteinModelPortalP10587.
SMRP10587. Positions 2-819.
ModBaseSearch...

Protein-protein interaction databases

IntActP10587. 1 interaction.
STRING9031.ENSGALP00000032964.

Proteomic databases

PaxDbP10587.
PRIDEP10587.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSGALT00000033605; ENSGALP00000032964; ENSGALG00000006520.
GeneID396211.
KEGGgga:396211.

Organism-specific databases

CTD4629.

Phylogenomic databases

eggNOGCOG5022.
GeneTreeENSGT00650000092896.
HOGENOMHOG000173958.
HOVERGENHBG004704.
InParanoidP10587.
KOK10352.
OMAQYEEKAA.
OrthoDBEOG4TXBR1.

Enzyme and pathway databases

ReactomeREACT_115433. Developmental Biology.

Family and domain databases

InterProIPR000048. IQ_motif_EF-hand-BS.
IPR001609. Myosin_head_motor_dom.
IPR004009. Myosin_N.
IPR002928. Myosin_tail.
[Graphical view]
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...

Other

EvolutionaryTraceP10587.
NextBio20816263.

Entry information

Entry nameMYH11_CHICK
AccessionPrimary (citable) accession number: P10587
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: April 3, 2013
This is version 125 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

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·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents