ID   MYH8_RAT                Reviewed;         257 AA.
AC   P04462;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   13-AUG-1987, sequence version 1.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=Myosin-8;
DE   AltName: Full=Myosin heavy chain 8;
DE   AltName: Full=Myosin heavy chain, skeletal muscle, perinatal;
DE            Short=MyHC-perinatal;
DE   Flags: Fragment;
GN   Name=Myh8;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=6149224; DOI=10.1016/s0021-9258(18)90731-3;
RA   Periasamy M., Wieczorek D.F., Nadal-Ginard B.;
RT   "Characterization of a developmentally regulated perinatal myosin heavy-
RT   chain gene expressed in skeletal muscle.";
RL   J. Biol. Chem. 259:13573-13578(1984).
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   -!- DEVELOPMENTAL STAGE: Transiently expressed during perinatal skeletal
CC       muscle development. It is first detected late in fetal life, is
CC       maximally expressed at the end of the 1st postnatal week, and is not
CC       found in the adult. Although their expression temporally overlaps.
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   ---------------------------------------------------------------------------
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; K02111; AAA41650.1; -; mRNA.
DR   PIR; A02991; A02991.
DR   AlphaFoldDB; P04462; -.
DR   SMR; P04462; -.
DR   IntAct; P04462; 1.
DR   PhosphoSitePlus; P04462; -.
DR   PeptideAtlas; P04462; -.
DR   UCSC; RGD:620356; rat.
DR   RGD; 620356; Myh8.
DR   InParanoid; P04462; -.
DR   PhylomeDB; P04462; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005923; C:bicellular tight junction; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0030016; C:myofibril; IEA:UniProtKB-SubCell.
DR   GO; GO:0016459; C:myosin complex; ISO:RGD.
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; ISO:RGD.
DR   GO; GO:0016887; F:ATP hydrolysis activity; ISO:RGD.
DR   GO; GO:0000146; F:microfilament motor activity; ISO:RGD.
DR   GO; GO:0046034; P:ATP metabolic process; ISO:RGD.
DR   GO; GO:0030049; P:muscle filament sliding; ISO:RGD.
DR   GO; GO:0150105; P:protein localization to cell-cell junction; IBA:GO_Central.
DR   GO; GO:0003009; P:skeletal muscle contraction; ISO:RGD.
DR   Gene3D; 1.20.5.370; -; 2.
DR   InterPro; IPR002928; Myosin_tail.
DR   InterPro; IPR014751; XRCC4-like_C.
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; Phosphoprotein;
KW   Reference proteome; Thick filament.
FT   CHAIN           <1..257
FT                   /note="Myosin-8"
FT                   /id="PRO_0000123415"
FT   COILED          <1..257
FT                   /evidence="ECO:0000255"
FT   MOD_RES         33
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         45
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         58
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   NON_TER         1
SQ   SEQUENCE   257 AA;  29844 MW;  20AD7F26C44BEDA4 CRC64;
     RAALQAEIEE LRATLEQTER SRKIAEQELL DASERVQLLH TQNASLINAK KKLENDVSQL
     QSEVEEVIQR ARNAEEKAKK AITDAAMMAE ELKKEQDTSA HLERMKKNME QTVKDLQHRL
     DEAEQLALKG GKKQIQKLEA RVRELEGEVE NEQKRNAEAV KGLRKHERRV KELTYQTEED
     RKNVLRLQDL VDKLQAKVKS YKRQAEEAEE QSNVNLAKFR KLQHELEEAE ERADIAESQV
     NKLRVKSREV HTKISAE