Reviewed, UniProtKB/Swiss-Prot P13538 (MYSS_CHICK)

Names and origin

Protein names	Recommended name:     Myosin heavy chain, skeletal muscle, adult
Organism	Gallus gallus (Chicken)
Taxonomic identifier	9031 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galliformes › Phasianidae › Phasianinae › Gallus

Protein attributes

Sequence length	1939 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.
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.
Miscellaneous	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.

Ontologies

Keywords
Cellular component	Cytoplasm Thick filament
Domain	Coiled coil
Ligand	ATP-binding Actin-binding Calmodulin-binding Nucleotide-binding
Molecular function	Motor protein Muscle protein Myosin
PTM	Acetylation Methylation Phosphoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Cellular component	myofibril Inferred from electronic annotation. Source: UniProtKB-SubCell myosin filament Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	ATP 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: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.2 Ref.6

Chain

2 – 1939

1938

Myosin heavy chain, skeletal muscle, adult

PRO_0000123434

Regions

Domain

2 – 783

782

Myosin head-like

Domain

784 – 813

30

IQ

Nucleotide binding

180 – 187

8

ATP Potential

Region

658 – 680

23

Actin-binding

Region

760 – 774

15

Actin-binding

Region

839 – 841

3

Hinge

Coiled coil

842 – 1939

1098

Potential

Amino acid modifications

Modified residue

2

1

N-acetylalanine

Modified residue

36

1

N6-methyllysine

Modified residue

131

1

N6,N6,N6-trimethyllysine

Modified residue

552

1

N6,N6,N6-trimethyllysine

Modified residue

756

1

Pros-methylhistidine

Experimental info

Sequence conflict

908

1

C → Q Ref.7

Sequence conflict

908

1

C → Q Ref.8

Sequence conflict

981

1

L → F in AAB47555. Ref.1

Sequence conflict

1344

1

E → D AA sequence Ref.5

Sequence conflict

1546

1

S → A AA sequence Ref.5

Sequence conflict

1797 – 1798

2

HV → QL AA sequence Ref.5

Sequence conflict

1831

1

S → A AA sequence Ref.5

Sequence conflict

1864

1

I → V in AAA48970. Ref.10

Sequence conflict

1930 – 1932

3

IHG → FH in AAA48970. Ref.10

Secondary structure

1

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1939

Helix Strand Turn

Details...

Helix

15 – 18

4

Turn

22 – 25

4

Helix

26 – 29

4

Turn

35 – 37

3

Beta strand

38 – 42

5

Beta strand

44 – 56

13

Beta strand

58 – 63

6

Beta strand

66 – 68

3

Beta strand

71 – 74

4

Helix

75 – 77

3

Beta strand

86 – 88

3

Helix

92 – 94

3

Helix

100 – 109

10

Turn

110 – 114

5

Beta strand

117 – 119

3

Beta strand

124 – 127

4

Helix

134 – 136

3

Helix

140 – 143

4

Turn

144 – 146

3

Helix

156 – 170

15

Beta strand

174 – 180

7

Helix

186 – 200

15

Helix

219 – 234

16

Beta strand

242 – 245

4

Beta strand

247 – 255

9

Beta strand

257 – 263

7

Beta strand

266 – 269

4

Helix

273 – 276

4

Helix

287 – 292

6

Helix

298 – 304

7

Helix

310 – 312

3

Helix

314 – 316

3

Helix

328 – 341

14

Helix

346 – 362

17

Beta strand

367 – 369

3

Beta strand

376 – 379

4

Helix

383 – 391

9

Helix

395 – 403

9

Beta strand

410 – 412

3

Helix

420 – 449

30

Beta strand

458 – 466

9

Beta strand

472 – 474

3

Helix

476 – 506

31

Helix

518 – 528

11

Helix

533 – 540

8

Helix

548 – 559

12

Beta strand

563 – 567

5

Beta strand

579 – 583

5

Beta strand

588 – 591

4

Helix

596 – 601

6

Helix

606 – 613

8

Helix

618 – 623

6

Helix

651 – 666

16

Beta strand

668 – 676

9

Helix

689 – 699

11

Helix

701 – 708

8

Beta strand

715 – 717

3

Helix

718 – 725

8

Helix

726 – 728

3

Turn

729 – 731

3

Helix

743 – 748

6

Beta strand

751 – 753

3

Beta strand

756 – 762

7

Beta strand

765 – 768

4

Helix

772 – 827

56

Helix

831 – 839

9

Turn

840 – 842

3

Sequences

	Sequence		Length	Mass (Da)
	P13538-1 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: F6DAD73CABD82BFD	FASTA	1,939	223,145
	10 20 30 40 50 60 MASPDAEMAA FGEAAPYLRK SEKERIEAQN KPFDAKSSVF VVHPKESFVK GTIQSKEGGK 70 80 90 100 110 120 VTVKTEGGET LTVKEDQVFS MNPPKYDKIE DMAMMTHLHE PAVLYNLKER YAAWMIYTYS 130 140 150 160 170 180 GLFCVTVNPY KWLPVYNPEV VLAYRGKKRQ EAPPHIFSIS DNAYQFMLTD RENQSILITG 190 200 210 220 230 240 ESGAGKTVNT KRVIQYFATI AASGEKKKEE QSGKMQGTLE DQIISANPLL EAFGNAKTVR 250 260 270 280 290 300 NDNSSRFGKF IRIHFGATGK LASADIETYL LEKSRVTFQL PAERSYHIFY QIMSNKKPEL 310 320 330 340 350 360 IDMLLITTNP YDYHYVSQGE ITVPSIDDQE ELMATDSAID ILGFSADEKT AIYKLTGAVM 370 380 390 400 410 420 HYGNLKFKQK QREEQAEPDG TEVADKAAYL MGLNSAELLK ALCYPRVKVG NEFVTKGQTV 430 440 450 460 470 480 SQVHNSVGAL AKAVYEKMFL WMVIRINQQL DTKQPRQYFI GVLDIAGFEI FDFNSFEQLC 490 500 510 520 530 540 INFTNEKLQQ FFNHHMFVLE QEEYKKEGIE WEFIDFGMDL AACIELIEKP MGIFSILEEE 550 560 570 580 590 600 CMFPKATDTS FKNKLYDQHL GKSNNFQKPK PAKGKAEAHF SLVHYAGTVD YNISGWLEKN 610 620 630 640 650 660 KDPLNETVIG LYQKSSVKTL ALLFATYGGE AEGGGGKKGG KKKGSSFQTV SALFRENLNK 670 680 690 700 710 720 LMANLRSTHP HFVRCIIPNE TKTPGAMEHE LVLHQLRCNG VLEGIRICRK GFPSRVLYAD 730 740 750 760 770 780 FKQRYRVLNA SAIPEGQFMD SKKASEKLLG SIDVDHTQYR FGHTKVFFKA GLLGLLEEMR 790 800 810 820 830 840 DDKLAEIITR TQARCRGFLM RVEYRRMVER RESIFCIQYN VRSFMNVKHW PWMKLFFKIK 850 860 870 880 890 900 PLLKSAESEK EMANMKEEFE KTKEELAKSE AKRKELEEKM VVLLQEKNDL QLQVQAEADS 910 920 930 940 950 960 LADAEERCDQ LIKTKIQLEA KIKEVTERAE DEEEINAELT AKKRKLEDEC SELKKDIDDL 970 980 990 1000 1010 1020 ELTLAKVEKE KHATENKVKN LTEEMAVLDE TIAKLTKEKK ALQEAHQQTL DDLQVEEDKV 1030 1040 1050 1060 1070 1080 NTLTKAKTKL EQQVDDLEGS LEQEKKLRMD LERAKRKLEG DLKLAHDSIM DLENDKQQLD 1090 1100 1110 1120 1130 1140 EKLKKKDFEI SQIQSKIEDE QALGMQLQKK IKELQARIEE LEEEIEAERT SRAKAEKHRA 1150 1160 1170 1180 1190 1200 DLSRELEEIS ERLEEAGGAT AAQIEMNKKR EAEFQKMRRD LEEATLQHEA TAAALRKKHA 1210 1220 1230 1240 1250 1260 DSTAELGEQI DNLQRVKQKL EKEKSELKME IDDLASNMES VSKAKANLEK MCRTLEDQLS 1270 1280 1290 1300 1310 1320 EIKTKEEQNQ RMINDLNTQR ARLQTETGEY SRQAEEKDAL ISQLSRGKQG FTQQIEELKR 1330 1340 1350 1360 1370 1380 HLEEEIKAKN ALAHALQSAR HDCELLREQY EEEQEAKGEL QRALSKANSE VAQWRTKYET 1390 1400 1410 1420 1430 1440 DAIQRTEELE EAKKKLAQRL QDAEEHVEAV NAKCASLEKT KQRLQNEVED LMVDVERSNA 1450 1460 1470 1480 1490 1500 ACAALDKKQK NFDKILAEWK QKYEETQTEL EASQKESRSL STELFKMKNA YEESLDHLET 1510 1520 1530 1540 1550 1560 LKRENKNLQQ EIADLTEQIA EGGKAVHELE KVKKHVEQEK SELQASLEEA EASLEHEEGK 1570 1580 1590 1600 1610 1620 ILRLQLELNQ IKSEIDRKIA EKDEEIDQLK RNHLRIVESM QSTLDAEIRS RNEALRLKKK 1630 1640 1650 1660 1670 1680 MEGDLNEMEI QLSHANRMAA EAQKNLRNTQ GTLKDTQIHL DDALRTQEDL KEQVAMVERR 1690 1700 1710 1720 1730 1740 ANLLQAEVEE LRGALEQTER SRKVAEQELL DATERVQLLH TQNTSLINTK KKLETDIVQI 1750 1760 1770 1780 1790 1800 QSEMEDTIQE ARNAEEKAKK AITDAAMMAE ELKKEQDTSA HLERMKKNMD QTVKDLHVRL 1810 1820 1830 1840 1850 1860 DEAEQLALKG GKKQLQKLEA RVRELEGEVD SEQKRSAEAV KGVRKYERRV KELTYQCEED 1870 1880 1890 1900 1910 1920 RKNILRLQDL VDKLQMKVKS YKRQAEEAEE LSNVNLSKFR KIQHELEEAE ERADIAESQV 1930 NKLRVKSREI HGKKIEEEE

References

[1]	"Cloning, nucleotide sequence and characterization of a full-length cDNA encoding the myosin heavy chain from adult chicken pectoralis major muscle." Chao T.H., Bandman E. Gene 199:265-270(1997) [PubMed: 9358064] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: White leghorn. Tissue: Pectoralis muscle.
[2]	"The primary structure of skeletal muscle myosin heavy chain: I. Sequence of the amino-terminal 23 kDa fragment." Hayashida M., Maita T., Matsuda G. J. Biochem. 110:54-59(1991) [PubMed: 1939027] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-206. Tissue: Pectoralis muscle.
[3]	"The primary structure of skeletal muscle myosin heavy chain: II. Sequence of the 50 kDa fragment of subfragment-1." Komine Y., Maita T., Matsuda G. J. Biochem. 110:60-67(1991) [PubMed: 1939028] [Abstract] Cited for: PROTEIN SEQUENCE OF 207-637. Tissue: Pectoralis muscle.
[4]	"The primary structure of skeletal muscle myosin heavy chain: III. Sequence of the 22 kDa fragment and the alignment of the 23 kDa, 50 kDa, and 22 kDa fragments." Maita T., Miyanishi T., Matsuzono K., Tanioka Y., Matsuda G. J. Biochem. 110:68-74(1991) [PubMed: 1939029] [Abstract] Cited for: PROTEIN SEQUENCE OF 638-838. Tissue: Pectoralis muscle.
[5]	"The primary structure of skeletal muscle myosin heavy chain: IV. Sequence of the rod, and the complete 1,938-residue sequence of the heavy chain." Maita T., Yajima E., Nagata S., Miyanishi T., Nakayama S., Matsuda G. J. Biochem. 110:75-87(1991) [PubMed: 1939030] [Abstract] Cited for: PROTEIN SEQUENCE OF 839-1939. Tissue: Pectoralis muscle.
[6]	"The primary structure of the myosin head." Maita T., Hayashida M., Tanioka Y., Komine Y., Matsuda G. Proc. Natl. Acad. Sci. U.S.A. 84:416-420(1987) [PubMed: 3467365] [Abstract] Cited for: PRELIMINARY PROTEIN SEQUENCE OF 2-809.
[7]	"Complete amino-acid sequence of subfragment-2 in adult chicken skeletal muscle myosin." Watanabe B. Biol. Chem. Hoppe-Seyler 370:1027-1034(1989) [PubMed: 2610940] [Abstract] Cited for: PROTEIN SEQUENCE OF 843-1271.
[8]	"Amino-acid sequence of the short subfragment-2 in adult chicken skeletal muscle myosin." Watanabe B. Biol. Chem. Hoppe-Seyler 370:549-558(1989) [PubMed: 2775482] [Abstract] Cited for: PROTEIN SEQUENCE OF 853-1109.
[9]	"Amino-acid sequence of the hinge region in chicken myosin subfragment-2." Watanabe B. Biol. Chem. Hoppe-Seyler 370:55-61(1989) [PubMed: 2713098] [Abstract] Cited for: PROTEIN SEQUENCE OF 1146-1271.
[10]	"Genomic clones encoding chicken myosin heavy-chain genes." Moriarity D.M., Barringer K.J., Dodgson J.B., Richter H.E., Young R.B. DNA 6:91-99(1987) [PubMed: 3034534] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1858-1939.
[11]	"Three-dimensional structure of myosin subfragment-1: a molecular motor." Rayment I., Rypniewski W.R., Schmidt-Base K., Smith R., Tomchick D.R., Benning M.M., Winkelmann D.A., Wesenberg G., Holden H.M. Science 261:50-58(1993) [PubMed: 8316857] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1-844.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

U87231 mRNA. Translation: AAB47555.1.
M16557 Genomic DNA. Translation: AAA48970.1.

IPI

IPI00584804.

RefSeq

NP_001013415.1.

UniGene

Gga.40396

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ALM	model	-	A	1-844	[»]
1M8Q	electron microscopy	70.00	A/D/G/P	5-844	[»]
1MVW	electron microscopy	70.00	A/D/G/J/M/P	5-843	[»]
1O18	electron microscopy	70.00	A/D/G/J/M/P	5-843	[»]
1O19	electron microscopy	70.00	A/D/G/J/M/S	5-843	[»]
1O1A	electron microscopy	70.00	A/D/G/J/M/P	5-843	[»]
1O1B	electron microscopy	70.00	A/D/G/J	5-843	[»]
1O1C	electron microscopy	70.00	A/D/G/J/P	5-843	[»]
1O1D	electron microscopy	70.00	A/D/G/J/M/P	5-843	[»]
1O1E	electron microscopy	70.00	A/D/G/J/M/P	5-843	[»]
1O1F	electron microscopy	70.00	A/D/G/J	5-843	[»]
1O1G	electron microscopy	70.00	A/D/G/J/M/P	5-843	[»]
2MYS	X-ray	2.80	A	2-844	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

P13538.

Genome annotation databases

Ensembl

ENSGALT00000001421; ENSGALP00000001419; ENSGALG00000023800; Gallus gallus. [Genome view]
ENSGALT00000001427; ENSGALP00000001425; ENSGALG00000023800; Gallus gallus. [Genome view]

GeneID

427788.

KEGG

gga:427788.

Phylogenomic databases

HOVERGEN

P13538.

InParanoid

P13538.

Family and domain databases

InterPro

IPR000048. IQ_CaM_bd_region.
IPR015650. Myosin_hc.
IPR001609. Myosin_head.
IPR004009. Myosin_N.
IPR002928. Myosin_tail.
[Graphical view]

PANTHER

PTHR13140:SF22. Myosin_hc. 1 hit.

Pfam

PF00612. IQ. 1 hit.
PF00063. Myosin_head. 1 hit.
PF02736. Myosin_N. 1 hit.
PF01576. Myosin_tail_1. 1 hit.
[Graphical view]

PRINTS

PR00193. MYOSINHEAVY.

SMART

SM00015. IQ. 1 hit.
SM00242. MYSc. 1 hit.
[Graphical view]

PROSITE

PS50096. IQ. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

MYSS_CHICK

Accession

Primary (citable) accession number: P13538
Secondary accession number(s): O13228

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	January 23, 2007
Last modified:	December 15, 2009
This is version 101 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)