MYH11_PIG
ID MYH11_PIG Reviewed; 65 AA.
AC P81271;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Myosin-11;
DE AltName: Full=Myosin heavy chain 11;
DE AltName: Full=Myosin heavy chain, smooth muscle isoform;
DE AltName: Full=SMMHC;
DE Flags: Fragments;
GN Name=MYH11;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP PROTEIN SEQUENCE.
RC TISSUE=Aortic smooth muscle;
RX PubMed=8428912; DOI=10.1016/s0021-9258(18)53787-x;
RA Katoh T., Morita F.;
RT "Actin-binding peptides obtained from the C-terminal 24-kDa fragment of
RT porcine aorta smooth muscle myosin subfragment-1 heavy chain.";
RL J. Biol. Chem. 268:2380-2388(1993).
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 -!- SUBCELLULAR LOCATION: Melanosome {ECO:0000250}. Cytoplasm, myofibril.
CC Note=Thick filaments of the 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}.
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DR PIR; A45200; A45200.
DR AlphaFoldDB; P81271; -.
DR SMR; P81271; -.
DR STRING; 9823.ENSSSCP00000000151; -.
DR PaxDb; P81271; -.
DR PeptideAtlas; P81271; -.
DR eggNOG; KOG0161; Eukaryota.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
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:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000146; F:microfilament motor activity; IBA:GO_Central.
DR GO; GO:0031032; P:actomyosin structure organization; IBA:GO_Central.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00063; Myosin_head; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
PE 1: Evidence at protein level;
KW Actin-binding; ATP-binding; Coiled coil; Cytoplasm;
KW Direct protein sequencing; Motor protein; Muscle protein; Myosin;
KW Nucleotide-binding; Reference proteome; Thick filament.
FT CHAIN <1..>65
FT /note="Myosin-11"
FT /id="PRO_0000123426"
FT DOMAIN <1..>65
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT NON_CONS 53..54
FT /evidence="ECO:0000305"
FT NON_TER 1
FT NON_TER 65
SQ SEQUENCE 65 AA; 7864 MW; A03446B967C3221E CRC64;
RSGKLDAFLV LEQLRCNGVL EGIRICRQGF PNRIVFQEFR QRYEILAANA IPKLRNWQWW
RLFTK