MYSU_RABIT
ID MYSU_RABIT Reviewed; 501 AA.
AC Q99105;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 25-MAY-2022, entry version 86.
DE RecName: Full=Myosin heavy chain, embryonic smooth muscle isoform;
DE Flags: Fragment;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Fetal aorta;
RX PubMed=1995631; DOI=10.1016/s0021-9258(19)67861-0;
RA Kuro-o M., Nagai R., Nakahara K., Katoh H., Tsai R.C., Tsuchimochi H.,
RA Yazaki Y., Ohkubo A., Takaku F.;
RT "cDNA cloning of a myosin heavy chain isoform in embryonic smooth muscle
RT and its expression during vascular development and in arteriosclerosis.";
RL J. Biol. Chem. 266:3768-3773(1991).
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: 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}.
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DR EMBL; D10280; BAA01124.1; -; mRNA.
DR PIR; A38650; A38650.
DR AlphaFoldDB; Q99105; -.
DR SMR; Q99105; -.
DR STRING; 9986.ENSOCUP00000014315; -.
DR eggNOG; KOG0160; Eukaryota.
DR eggNOG; KOG0161; Eukaryota.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0030016; C:myofibril; IEA:UniProtKB-SubCell.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0032982; C:myosin filament; IEA:UniProtKB-KW.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR InterPro; IPR002928; Myosin_tail.
DR Pfam; PF01576; Myosin_tail_1; 1.
PE 2: Evidence at transcript level;
KW Actin-binding; ATP-binding; Coiled coil; Cytoplasm; Motor protein;
KW Muscle protein; Myosin; Nucleotide-binding; Reference proteome;
KW Thick filament.
FT CHAIN <1..501
FT /note="Myosin heavy chain, embryonic smooth muscle isoform"
FT /id="PRO_0000123390"
FT REGION <1..501
FT /note="Rodlike tail (S2 and LMM domains)"
FT REGION 182..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 221..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 397..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1..457
FT /evidence="ECO:0000255"
FT COMPBIAS 222..242
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..440
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
SQ SEQUENCE 501 AA; 58119 MW; 49F793247D00973E CRC64;
REAREKETKA LSLSRALEEA LEAKEEFERQ NKQLRADMED LMSSKDDVGK NVHELEKSKR
ALEQQVEEMR TQLEELEDEL QATEDAKLRL EVNTQAMKAQ FERDLQARDE QSEEKKRLLT
KQVRELEAEL EDERKQRALA VASKKKMEID LKDLEAQIEA ANKARERRVK QLRRLQAQMK
DYQRELEEAR GSRDEIFAQS KESEKKLKSL EAEILQLQEE LASSERARRH AEQERDELAD
EIANSASGKS ALLDEKRRLE ARMRQLEEEL EEEQSNMELL NDRFRKTTLQ VDTLNAELAA
ERSAAQKSDN ARQQLERQNK DLKAKLQELE GAVKSKFKAT ISALEAKIGQ LEEQLEQEAK
ERAAANKLVR RTEKKLKEIF MQVEDERRHA DQYKEQMEKA NARMKQLKRQ LEEAEEEATR
ANASRRKLQR ELDDATEANE GLSREVSTLK NRLRRGGPIS FSSSRSGRPQ LHIEGASLEL
SDDDTESKTS DVNETQPPQS E