MYH7_RABIT
ID MYH7_RABIT Reviewed; 736 AA.
AC P04461;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 25-MAY-2022, entry version 131.
DE RecName: Full=Myosin-7;
DE AltName: Full=Beta isomyosin;
DE AltName: Full=Myosin heavy chain 7;
DE AltName: Full=Myosin heavy chain slow isoform;
DE Short=MyHC-slow;
DE AltName: Full=Myosin heavy chain, cardiac muscle beta isoform;
DE Short=MyHC-beta;
DE Flags: Fragment;
GN Name=MYH7;
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=Heart ventricle;
RX PubMed=6321481; DOI=10.1016/s0021-9258(17)43213-3;
RA Kavinsky C.J., Umeda P.K., Levin J.E., Sinha A.M., Nigro J.M., Jakovcic S.,
RA Rabinowitz M.;
RT "Analysis of cloned mRNA sequences encoding subfragment 2 and part of
RT subfragment 1 of alpha- and beta-myosin heavy chains of rabbit heart.";
RL J. Biol. Chem. 259:2775-2781(1984).
RN [2]
RP PROTEIN SEQUENCE OF 309-321, AND LACK OF METHYLATION AT HIS-317.
RC TISSUE=Heart;
RX PubMed=5058224; DOI=10.1016/s0021-9258(19)45670-6;
RA Huszar G., Elzinga M.;
RT "Homologous methylated and nonmethylated histidine peptides in skeletal and
RT cardiac myosins.";
RL J. Biol. Chem. 247:745-753(1972).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 458-544.
RX PubMed=6328491; DOI=10.1073/pnas.81.10.3044;
RA Friedman D.J., Umeda P.K., Sinha A.M., Hsu H.J., Jokovcic S.,
RA Rabinowitz M.;
RT "Characterization of genomic clones specifying rabbit alpha- and beta-
RT ventricular myosin heavy chains.";
RL Proc. Natl. Acad. Sci. U.S.A. 81:3044-3048(1984).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 600-720.
RX PubMed=6193509; DOI=10.1073/pnas.79.19.5847;
RA Sinha A.M., Umeda P.K., Kavinsky C.J., Rajamanickam C., Hsu H.J.,
RA Jakovcic S., Rabinowitz M.;
RT "Molecular cloning of mRNA sequences for cardiac alpha- and beta-form
RT myosin heavy chains: expression in ventricles of normal, hypothyroid, and
RT thyrotoxic rabbits.";
RL Proc. Natl. Acad. Sci. U.S.A. 79:5847-5851(1982).
CC -!- FUNCTION: Myosins are actin-based motor molecules with ATPase activity
CC essential for muscle contraction. Forms regular bipolar thick filaments
CC that, together with actin thin filaments, constitute the fundamental
CC contractile unit of skeletal and cardiac muscle.
CC {ECO:0000250|UniProtKB:P12883}.
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). Interacts with ECPAS.
CC Interacts (via C-terminus) with LRRC39. {ECO:0000250|UniProtKB:P12883}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril
CC {ECO:0000250|UniProtKB:P02564}. Cytoplasm, myofibril, sarcomere
CC {ECO:0000250|UniProtKB:P02564}. Note=Thick filaments of the myofibrils.
CC {ECO:0000250|UniProtKB:P02564}.
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 -!- 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. Four skip residues
CC (Skip1-4) introduce discontinuities in the coiled-coil heptad repeats.
CC The first three skip residues are structurally comparable and induce a
CC unique local relaxation of the coiled-coil superhelical pitch and the
CC fourth skip residue lies within a highly flexible molecular hinge that
CC is necessary for myosin incorporation in the bare zone of sarcomeres.
CC {ECO:0000250|UniProtKB:P12883}.
CC -!- MISCELLANEOUS: The cardiac alpha isoform is a 'fast' ATPase myosin,
CC while the beta isoform is a 'slow' ATPase.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000305}.
CC -!- CAUTION: Represents a conventional myosin. This protein should not be
CC confused with the unconventional myosin-7 (MYO7). {ECO:0000305}.
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DR EMBL; K02444; AAA31414.1; -; mRNA.
DR EMBL; K01696; AAA31417.1; -; mRNA.
DR EMBL; J00672; AAA31413.1; -; mRNA.
DR AlphaFoldDB; P04461; -.
DR SMR; P04461; -.
DR STRING; 9986.ENSOCUP00000021291; -.
DR ABCD; P04461; 1 sequenced antibody.
DR eggNOG; KOG0161; Eukaryota.
DR InParanoid; P04461; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0030016; C:myofibril; ISS:UniProtKB.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0032982; C:myosin filament; ISS:UniProtKB.
DR GO; GO:0030017; C:sarcomere; ISS:UniProtKB.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0003774; F:cytoskeletal motor activity; IEA:InterPro.
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; IPR002928; Myosin_tail.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF01576; Myosin_tail_1; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50096; IQ; 1.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
PE 1: Evidence at protein level;
KW Actin-binding; ATP-binding; Calmodulin-binding; Coiled coil; Cytoplasm;
KW Direct protein sequencing; Motor protein; Muscle protein; Myosin;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Thick filament.
FT CHAIN <1..>736
FT /note="Myosin-7"
FT /id="PRO_0000123412"
FT DOMAIN <1..342
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 345..374
FT /note="IQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT REGION 219..241
FT /note="Actin-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT REGION 716..736
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 403..>736
FT /evidence="ECO:0000255"
FT MOD_RES 701
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02563"
FT CONFLICT 318..319
FT /note="NQ -> QN (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT NON_TER 1
FT NON_TER 736
SQ SEQUENCE 736 AA; 85432 MW; 37D8BD7A4B6DEC43 CRC64;
NWMVTRINAT LETKQPRQYF IGVLDIAGFE IFDFNSFEQL CINFTNEKLQ QFLNHHMFVL
EQEEYKKEGI EWTFIDLGMD LQACIDLIEK PMGIMSILEE ECMFPKATDM TFKAKLYDNH
LGKSNNFQKP RNIKGKPEAH FALIHYAGTV DYNILGWLQK NKDPLNETVV ALYQKSSLKL
LSNLFANYAG ADAPVEKGKG KAKKGSSFQT VSALHRENLN KLMTNLRSTH PHFVRCIIPN
ETKSPGVIDN PLVMHQLRCN GVLEGIRICR KGFPNRILYG DFRQRYRILN PAAIPEGQFI
DSRKGAEKLL SSLDIDHNQY KFGHTKVFFK AGLLGLLEEM RDERLSRIIT RIQAQSRGVL
SRMEYKKLLE RRDSLLIIQW NIRAFMGVKN WPWMKLYFKI KPLLKSAETE KEMATMKEEF
ARVKEALEKS EARRKELEEK TVSLLQEKND LQLQVQAEQD NLADAEERCD QLIKNKIQLE
AKVKEMNERL EDEEEMNAEL TAKKRKLEDE CSELKRDIDD LELTLAKVEK EKHATENKVK
NLTEEMAGLD EIIAKLTKKK KALQEAHQQA LDDLQAEEDK VNTLTKAKVK LEQQVDDLEG
SLEQEKKVRM DLERAKRKLE GDLKLTQESI MDLENDKQQL DERLKKKDFE LNALNARIED
EQALGSQLQK KLKELQARIE ELEEELEAER TARAKVEKLR SDLSRELEEI SERLEEAGGA
TSVQIEMNKK REAEFQ
