MYH11_CHICK
ID MYH11_CHICK Reviewed; 1979 AA.
AC P10587;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Myosin-11;
DE AltName: Full=Myosin heavy chain 11;
DE AltName: Full=Myosin heavy chain, gizzard smooth muscle;
GN Name=MYH11;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2892941; DOI=10.1016/0022-2836(87)90302-0;
RA Yanagisawa M., Hamada Y., Katsuragawa Y., Imamura M., Mikawa T., Masaki T.;
RT "Complete primary structure of vertebrate smooth muscle myosin heavy chain
RT deduced from its complementary DNA sequence. Implications on topography and
RT function of myosin.";
RL J. Mol. Biol. 198:143-157(1987).
RN [2]
RP SEQUENCE REVISION.
RA Masaki T.;
RL Submitted (FEB-1989) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 2-204, AND METHYLATION AT LYS-128.
RX PubMed=3312184; DOI=10.1093/oxfordjournals.jbchem.a122025;
RA Maita T., Onishi H., Yajima E., Matsuda G.;
RT "Amino acid sequence of the amino-terminal 24 kDa fragment of the heavy
RT chain of chicken gizzard myosin.";
RL J. Biochem. 102:133-145(1987).
RN [4]
RP PROTEIN SEQUENCE OF 54-64 AND 143-183.
RX PubMed=1977747; DOI=10.1016/s0021-9258(17)30667-1;
RA Onishi H., Maita T., Matsuda G., Fujiwara K.;
RT "Lys-65 and Glu-168 are the residues for carbodiimide-catalyzed cross-
RT linking between the two heads of rigor smooth muscle heavy meromyosin.";
RL J. Biol. Chem. 265:19362-19368(1990).
RN [5]
RP PROTEIN SEQUENCE OF 169-183.
RX PubMed=1385724; DOI=10.1021/bi00142a003;
RA Cole D.G., Yount R.G.;
RT "Stability and photochemical properties of vanadate-trapped nucleotide
RT complexes of gizzard myosin in the 6S and 10S conformations: identification
RT of an active-site serine.";
RL Biochemistry 31:6186-6192(1992).
RN [6]
RP PROTEIN SEQUENCE OF 653-855.
RX PubMed=3571180; DOI=10.1093/oxfordjournals.jbchem.a121849;
RA Onishi H., Maita T., Miyanishi T., Watanabe S., Matsuda G.;
RT "Amino acid sequence of the 203-residue fragment of the heavy chain of
RT chicken gizzard myosin containing the SH1-type cysteine residue.";
RL J. Biochem. 100:1433-1447(1986).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF 1-819, AND SEQUENCE REVISION TO
RP 205-216.
RX PubMed=9741621; DOI=10.1016/s0092-8674(00)81598-6;
RA Dominguez R., Freyzon Y., Trybus K.M., Cohen C.;
RT "Crystal structure of a vertebrate smooth muscle myosin motor domain and
RT its complex with the essential light chain: visualization of the pre-power
RT stroke state.";
RL Cell 94:559-571(1998).
CC -!- FUNCTION: Muscle contraction.
CC -!- SUBUNIT: Muscle myosin is a hexameric protein that consists of 2 heavy
CC chain subunits (MHC), 2 alkali light chain subunits (MLC) and 2
CC regulatory light chain subunits (MLC-2).
CC -!- INTERACTION:
CC P10587; P02607: MYL6; NbExp=2; IntAct=EBI-1027098, EBI-1027073;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril. Note=Thick filaments of the
CC myofibrils.
CC -!- DOMAIN: The rodlike tail sequence is highly repetitive, showing cycles
CC of a 28-residue repeat pattern composed of 4 heptapeptides,
CC characteristic for alpha-helical coiled coils.
CC -!- DOMAIN: Limited proteolysis of myosin heavy chain produces 1 light
CC meromyosin (LMM) and 1 heavy meromyosin (HMM). HMM can be further
CC cleaved into 2 globular subfragments (S1) and 1 rod-shaped subfragment
CC (S2). {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X06546; CAA29793.1; -; mRNA.
DR PIR; S03166; S03166.
DR PDB; 1BR1; X-ray; 3.50 A; A/C/E/G=3-819.
DR PDB; 1BR2; X-ray; 2.90 A; A/B/C/D/E/F=3-792.
DR PDB; 1BR4; X-ray; 3.62 A; A/C/E/G=3-819.
DR PDB; 1I84; EM; 20.00 A; S/V=2-1175.
DR PDB; 3DTP; EM; 20.00 A; A/B=3-852.
DR PDB; 3J04; EM; -; A/D=2-910.
DR PDB; 5M05; X-ray; 2.67 A; A=1-790.
DR PDB; 5T45; X-ray; 2.80 A; A=1-790.
DR PDB; 6BIH; EM; 6.00 A; H=1-790.
DR PDB; 7MF3; EM; 3.40 A; A/B/G/H=2-1979.
DR PDBsum; 1BR1; -.
DR PDBsum; 1BR2; -.
DR PDBsum; 1BR4; -.
DR PDBsum; 1I84; -.
DR PDBsum; 3DTP; -.
DR PDBsum; 3J04; -.
DR PDBsum; 5M05; -.
DR PDBsum; 5T45; -.
DR PDBsum; 6BIH; -.
DR PDBsum; 7MF3; -.
DR AlphaFoldDB; P10587; -.
DR SMR; P10587; -.
DR IntAct; P10587; 1.
DR STRING; 9031.ENSGALP00000010520; -.
DR PaxDb; P10587; -.
DR PRIDE; P10587; -.
DR VEuPathDB; HostDB:geneid_396211; -.
DR eggNOG; KOG0161; Eukaryota.
DR InParanoid; P10587; -.
DR OrthoDB; 47111at2759; -.
DR PhylomeDB; P10587; -.
DR TreeFam; TF333601; -.
DR SABIO-RK; P10587; -.
DR EvolutionaryTrace; P10587; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005859; C:muscle myosin complex; IMP:CAFA.
DR GO; GO:0030016; C:myofibril; IEA:UniProtKB-SubCell.
DR GO; GO:0032982; C:myosin filament; IBA:GO_Central.
DR GO; GO:0016460; C:myosin II complex; IBA:GO_Central.
DR GO; GO:0003779; F:actin binding; IMP:CAFA.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0043531; F:ADP binding; IMP:CAFA.
DR GO; GO:0005524; F:ATP binding; IMP:CAFA.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IMP:CAFA.
DR GO; GO:0000146; F:microfilament motor activity; IMP:CAFA.
DR GO; GO:0045159; F:myosin II binding; IPI:CAFA.
DR GO; GO:0032027; F:myosin light chain binding; IPI:CAFA.
DR GO; GO:0008307; F:structural constituent of muscle; IMP:CAFA.
DR GO; GO:0031032; P:actomyosin structure organization; IBA:GO_Central.
DR GO; GO:0055013; P:cardiac muscle cell development; ISS:UniProtKB.
DR GO; GO:0048251; P:elastic fiber assembly; ISS:UniProtKB.
DR GO; GO:0030239; P:myofibril assembly; IMP:CAFA.
DR GO; GO:0030241; P:skeletal muscle myosin thick filament assembly; ISS:UniProtKB.
DR GO; GO:0006939; P:smooth muscle contraction; ISS:UniProtKB.
DR DisProt; DP00102; -.
DR Gene3D; 1.20.5.370; -; 1.
DR Gene3D; 2.30.30.360; -; 1.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR004009; Myosin_N.
DR InterPro; IPR008989; Myosin_S1_N.
DR InterPro; IPR002928; Myosin_tail.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR014751; XRCC4-like_C.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF02736; Myosin_N; 1.
DR Pfam; PF01576; Myosin_tail_1; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00015; IQ; 1.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50096; IQ; 1.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS51844; SH3_LIKE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Actin-binding; ATP-binding; Calmodulin-binding; Coiled coil;
KW Cytoplasm; Direct protein sequencing; Methylation; Motor protein;
KW Muscle protein; Myosin; Nucleotide-binding; Reference proteome;
KW Thick filament.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:3312184"
FT CHAIN 2..1979
FT /note="Myosin-11"
FT /id="PRO_0000123429"
FT DOMAIN 30..80
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01190"
FT DOMAIN 84..789
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 792..821
FT /note="IQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT REGION 667..689
FT /note="Actin-binding"
FT REGION 768..782
FT /note="Actin-binding"
FT REGION 850..1979
FT /note="Rodlike tail (S2 and LMM domains)"
FT REGION 1130..1150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1709..1736
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1891..1979
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 850..1979
FT /evidence="ECO:0000255"
FT COMPBIAS 1709..1723
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1891..1921
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1953..1979
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 177..184
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT MOD_RES 2
FT /note="Blocked amino end (Ser)"
FT /evidence="ECO:0000269|PubMed:3312184"
FT MOD_RES 128
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000269|PubMed:3312184"
FT CONFLICT 205..216
FT /note="KDTSITQGPSFS -> RTPASLKVHLFP (in Ref. 1; CAA29793)"
FT /evidence="ECO:0000305"
FT HELIX 10..12
FT /evidence="ECO:0007829|PDB:1BR1"
FT HELIX 23..28
FT /evidence="ECO:0007829|PDB:1BR1"
FT STRAND 34..39
FT /evidence="ECO:0007829|PDB:5M05"
FT TURN 40..42
FT /evidence="ECO:0007829|PDB:5M05"
FT STRAND 43..53
FT /evidence="ECO:0007829|PDB:5M05"
FT STRAND 56..61
FT /evidence="ECO:0007829|PDB:5M05"
FT TURN 62..64
FT /evidence="ECO:0007829|PDB:5M05"
FT STRAND 67..71
FT /evidence="ECO:0007829|PDB:5M05"
FT HELIX 72..74
FT /evidence="ECO:0007829|PDB:5M05"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:5M05"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:5M05"
FT HELIX 97..109
FT /evidence="ECO:0007829|PDB:5M05"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:5M05"
FT STRAND 118..124
FT /evidence="ECO:0007829|PDB:5M05"
FT HELIX 131..133
FT /evidence="ECO:0007829|PDB:5T45"
FT HELIX 135..141
FT /evidence="ECO:0007829|PDB:5M05"
FT HELIX 146..148
FT /evidence="ECO:0007829|PDB:5M05"
FT HELIX 153..167
FT /evidence="ECO:0007829|PDB:5M05"
FT STRAND 171..176
FT /evidence="ECO:0007829|PDB:5M05"
FT HELIX 183..197
FT /evidence="ECO:0007829|PDB:5M05"
FT HELIX 219..224
FT /evidence="ECO:0007829|PDB:5M05"
FT HELIX 227..235
FT /evidence="ECO:0007829|PDB:5M05"
FT STRAND 236..239
FT /evidence="ECO:0007829|PDB:1BR1"
FT STRAND 245..256
FT /evidence="ECO:0007829|PDB:5M05"
FT STRAND 258..260
FT /evidence="ECO:0007829|PDB:7MF3"
FT STRAND 262..270
FT /evidence="ECO:0007829|PDB:5M05"
FT HELIX 274..277
FT /evidence="ECO:0007829|PDB:5M05"
FT HELIX 288..296
FT /evidence="ECO:0007829|PDB:5M05"
FT HELIX 299..304
FT /evidence="ECO:0007829|PDB:5M05"
FT HELIX 310..312
FT /evidence="ECO:0007829|PDB:5M05"
FT STRAND 314..316
FT /evidence="ECO:0007829|PDB:7MF3"
FT HELIX 328..342
FT /evidence="ECO:0007829|PDB:5M05"
FT HELIX 346..362
FT /evidence="ECO:0007829|PDB:5M05"
FT STRAND 371..374
FT /evidence="ECO:0007829|PDB:7MF3"
FT STRAND 375..377
FT /evidence="ECO:0007829|PDB:5M05"
FT HELIX 382..391
FT /evidence="ECO:0007829|PDB:5M05"
FT HELIX 395..403
FT /evidence="ECO:0007829|PDB:5M05"
FT STRAND 406..408
FT /evidence="ECO:0007829|PDB:5T45"
FT STRAND 410..414
FT /evidence="ECO:0007829|PDB:5M05"
FT HELIX 420..450
FT /evidence="ECO:0007829|PDB:5M05"
FT TURN 451..453
FT /evidence="ECO:0007829|PDB:5T45"
FT STRAND 458..465
FT /evidence="ECO:0007829|PDB:5M05"
FT STRAND 473..475
FT /evidence="ECO:0007829|PDB:1BR2"
FT HELIX 477..506
FT /evidence="ECO:0007829|PDB:5M05"
FT HELIX 517..521
FT /evidence="ECO:0007829|PDB:5M05"
FT HELIX 522..529
FT /evidence="ECO:0007829|PDB:5M05"
FT STRAND 532..534
FT /evidence="ECO:0007829|PDB:5M05"
FT HELIX 537..545
FT /evidence="ECO:0007829|PDB:5M05"
FT HELIX 552..563
FT /evidence="ECO:0007829|PDB:5M05"
FT STRAND 569..571
FT /evidence="ECO:0007829|PDB:1BR2"
FT TURN 576..578
FT /evidence="ECO:0007829|PDB:1BR1"
FT STRAND 580..585
FT /evidence="ECO:0007829|PDB:5M05"
FT STRAND 588..593
FT /evidence="ECO:0007829|PDB:5M05"
FT HELIX 597..602
FT /evidence="ECO:0007829|PDB:5M05"
FT HELIX 607..614
FT /evidence="ECO:0007829|PDB:5M05"
FT HELIX 619..624
FT /evidence="ECO:0007829|PDB:5M05"
FT STRAND 654..656
FT /evidence="ECO:0007829|PDB:7MF3"
FT HELIX 659..675
FT /evidence="ECO:0007829|PDB:5M05"
FT STRAND 677..685
FT /evidence="ECO:0007829|PDB:5M05"
FT HELIX 698..707
FT /evidence="ECO:0007829|PDB:5M05"
FT HELIX 710..718
FT /evidence="ECO:0007829|PDB:5M05"
FT STRAND 723..726
FT /evidence="ECO:0007829|PDB:5M05"
FT HELIX 727..734
FT /evidence="ECO:0007829|PDB:5M05"
FT TURN 735..737
FT /evidence="ECO:0007829|PDB:5T45"
FT STRAND 740..742
FT /evidence="ECO:0007829|PDB:5M05"
FT HELIX 749..758
FT /evidence="ECO:0007829|PDB:5M05"
FT TURN 759..761
FT /evidence="ECO:0007829|PDB:5M05"
FT STRAND 766..769
FT /evidence="ECO:0007829|PDB:5M05"
FT STRAND 771..776
FT /evidence="ECO:0007829|PDB:5M05"
FT TURN 778..784
FT /evidence="ECO:0007829|PDB:5M05"
FT HELIX 785..791
FT /evidence="ECO:0007829|PDB:7MF3"
FT HELIX 793..839
FT /evidence="ECO:0007829|PDB:7MF3"
FT HELIX 841..845
FT /evidence="ECO:0007829|PDB:7MF3"
FT HELIX 848..853
FT /evidence="ECO:0007829|PDB:7MF3"
FT HELIX 855..948
FT /evidence="ECO:0007829|PDB:7MF3"
FT HELIX 1414..1526
FT /evidence="ECO:0007829|PDB:7MF3"
FT STRAND 1528..1530
FT /evidence="ECO:0007829|PDB:7MF3"
FT HELIX 1533..1622
FT /evidence="ECO:0007829|PDB:7MF3"
SQ SEQUENCE 1979 AA; 228796 MW; 2F583CDDD4D9557D CRC64;
MSQKPLSDDE KFLFVDKNFV NNPLAQADWS AKKLVWVPSE KHGFEAASIK EEKGDEVTVE
LQENGKKVTL SKDDIQKMNP PKFSKVEDMA ELTCLNEASV LHNLRERYFS GLIYTYSGLF
CVVINPYKQL PIYSEKIIDM YKGKKRHEMP PHIYAIADTA YRSMLQDRED QSILCTGESG
AGKTENTKKV IQYLAVVASS HKGKKDTSIT QGPSFSYGEL EKQLLQANPI LEAFGNAKTV
KNDNSSRFGK FIRINFDVTG YIVGANIETY LLEKSRAIRQ AKDERTFHIF YYLIAGASEQ
MRNDLLLEGF NNYTFLSNGH VPIPAQQDDE MFQETLEAMT IMGFTEEEQT SILRVVSSVL
QLGNIVFKKE RNTDQASMPD NTAAQKVCHL MGINVTDFTR SILTPRIKVG RDVVQKAQTK
EQADFAIEAL AKAKFERLFR WILTRVNKAL DKTKRQGASF LGILDIAGFE IFEINSFEQL
CINYTNEKLQ QLFNHTMFIL EQEEYQREGI EWNFIDFGLD LQPCIELIER PTNPPGVLAL
LDEECWFPKA TDTSFVEKLI QEQGNHAKFQ KSKQLKDKTE FCILHYAGKV TYNASAWLTK
NMDPLNDNVT SLLNQSSDKF VADLWKDVDR IVGLDQMAKM TESSLPSASK TKKGMFRTVG
QLYKEQLTKL MTTLRNTNPN FVRCIIPNHE KRAGKLDAHL VLEQLRCNGV LEGIRICRQG
FPNRIVFQEF RQRYEILAAN AIPKGFMDGK QACILMIKAL ELDPNLYRIG QSKIFFRTGV
LAHLEEERDL KITDVIIAFQ AQCRGYLARK AFAKRQQQLT AMKVIQRNCA AYLKLRNWQW
WRLFTKVKPL LQVTRQEEEM QAKDEELQRT KERQQKAEAE LKELEQKHTQ LCEEKNLLQE
KLQAETELYA EAEEMRVRLA AKKQELEEIL HEMEARIEEE EERSQQLQAE KKKMQQQMLD
LEEQLEEEEA ARQKLQLEKV TADGKIKKME DDILIMEDQN NKLTKERKLL EERVSDLTTN
LAEEEEKAKN LTKLKNKHES MISELEVRLK KEEKSRQELE KIKRKLEGES SDLHEQIAEL
QAQIAELKAQ LAKKEEELQA ALARLEDETS QKNNALKKIR ELESHISDLQ EDLESEKAAR
NKAEKQKRDL SEELEALKTE LEDTLDTTAT QQELRAKREQ EVTVLKRALE EETRTHEAQV
QEMRQKHTQA VEELTEQLEQ FKRAKANLDK TKQTLEKDNA DLANEIRSLS QAKQDVEHKK
KKLEVQLQDL QSKYSDGERV RTELNEKVHK LQIEVENVTS LLNEAESKNI KLTKDVATLG
SQLQDTQELL QEETRQKLNV TTKLRQLEDD KNSLQEQLDE EVEAKQNLER HISTLTIQLS
DSKKKLQEFT ATVETMEEGK KKLQREIESL TQQFEEKAAS YDKLEKTKNR LQQELDDLVV
DLDNQRQLVS NLEKKQKKFD QMLAEEKNIS SKYADERDRA EAEAREKETK ALSLARALEE
ALEAKEELER TNKMLKAEME DLVSSKDDVG KNVHELEKSK RTLEQQVEEM KTQLEELEDE
LQAAEDAKLR LEVNMQAMKS QFERDLQARD EQNEEKRRQL LKQLHEHETE LEDERKQRAL
AAAAKKKLEV DVKDLESQVD SANKAREEAI KQLRKLQAQM KDYQRDLDDA RAAREEIFAT
ARENEKKAKN LEAELIQLQE DLAAAERARK QADLEKEEMA EELASANSGR TSLQDEKRRL
EARIAQLEEE LDEEHSNIET MSDRMRKAVQ QAEQLNNELA TERATAQKNE NARQQLERQN
KELRSKLQEM EGAVKSKFKS TIAALEAKIA SLEEQLEQEA REKQAAAKTL RQKDKKLKDA
LLQVEDERKQ AEQYKDQAEK GNLRLKQLKR QLEEAEEESQ RINANRRKLQ RELDEATESN
DALGREVAAL KSKLRRGNEP VSFAPPRRSG GRRVIENATD GGEEEIDGRD GDFNGKASE
