MYSS_CYPCA
ID MYSS_CYPCA Reviewed; 1935 AA.
AC Q90339;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 2.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Myosin heavy chain, fast skeletal muscle;
OS Cyprinus carpio (Common carp).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Cyprininae; Cyprinus.
OX NCBI_TaxID=7962;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Fast-twitch skeletal muscle;
RX PubMed=9208928; DOI=10.1111/j.1432-1033.1997.t01-2-00380.x;
RA Hirayama Y., Watabe S.;
RT "Structural differences in the crossbridge head of temperature-associated
RT myosin subfragment-1 isoforms from carp fast skeletal muscle.";
RL Eur. J. Biochem. 246:380-387(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 981-1935.
RC TISSUE=Fast-twitch skeletal muscle;
RX PubMed=9023993; DOI=10.1242/jeb.200.1.27;
RA Imai J., Hirayama Y., Kikuchi K., Kakinuma M., Watabe S.;
RT "cDNA cloning of myosin heavy chain isoforms from carp fast skeletal muscle
RT and their gene expression associated with temperature acclimation.";
RL J. Exp. Biol. 200:27-34(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1387-1528.
RX PubMed=7887920; DOI=10.1006/bbrc.1995.1313;
RA Watabe S., Imai J., Nakaya M., Hirayama Y., Okamoto Y., Masaki H.,
RA Uozumi T., Hirono I., Aoki T.;
RT "Temperature acclimation induces light meromyosin isoforms with different
RT primary structures in carp fast skeletal muscle.";
RL Biochem. Biophys. Res. Commun. 208:118-125(1995).
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}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000305}.
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DR EMBL; D89992; BAA22069.1; -; mRNA.
DR EMBL; D50476; BAA09069.1; -; mRNA.
DR EMBL; D43700; BAA07802.1; -; mRNA.
DR PIR; I50496; I50496.
DR PIR; S66521; S66521.
DR AlphaFoldDB; Q90339; -.
DR SMR; Q90339; -.
DR PRIDE; Q90339; -.
DR Proteomes; UP000694384; 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:0051015; F:actin filament binding; IEA:InterPro.
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; 1.20.5.370; -; 4.
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; 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 2: Evidence at transcript level;
KW Actin-binding; ATP-binding; Calmodulin-binding; Coiled coil; Cytoplasm;
KW Methylation; Motor protein; Muscle protein; Myosin; Nucleotide-binding;
KW Reference proteome; Thick filament.
FT CHAIN 1..1935
FT /note="Myosin heavy chain, fast skeletal muscle"
FT /id="PRO_0000123435"
FT DOMAIN 32..81
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01190"
FT DOMAIN 85..779
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 782..811
FT /note="IQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT REGION 659..681
FT /note="Actin-binding"
FT REGION 761..775
FT /note="Actin-binding"
FT REGION 812..839
FT /note="Hinge"
FT REGION 1589..1608
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1902..1935
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 840..1935
FT /evidence="ECO:0000255"
FT COMPBIAS 1591..1606
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 178..185
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 129
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1935 AA; 221601 MW; 9A1244B67D63C83B CRC64;
MGDGEMECFG PAAVYLRKTE RERIEAQNTP FDAKTAFFVV DPDEMYLKGT LVSKEGGKAT
VKTHSGKTVT VKEDEIFPMN PPKFDKIEDM AMMTHLNEPA VLFNLKERYA AWMIYTYSGL
FCVTVNPYKW LPVYDAVVVG GYRGKKRIEA PPHIFSISDN AYQFMLTDRE NQSVLITGES
GAGKTVNTKR VIQYFATVGA MSGPKKPEPV PGKMQGSLED QIVAANPLLE AYGNAKTVRN
DNSSRFGKFI RIHFGTTGKL ASADIETYLL EKSRVTFQLS AERSYHIFYQ LMTGHKPELL
EALLITTNPY DYPMISQGEI TVKSINDVEE FIATDTAIDI LGFTADEKIS IYKLTGAVMH
HGNMKFKQKQ REEQAEPDGT EVADKIAYLM GLNSADMLKA LCFPRVKVGN EMVTKGQTVP
QVNNAVSALS KSVYEKMFLW MVIRINEMLD TKQPRQFFIG VLDIAGFEIF DFNSLEQLCI
NFTNEKLQQF FNHHMFVLEQ EEYKKEGIEW EFIDFGMDLA ACIELIEKPM GIFSILEEEC
MFPKATDTSF KNKLHDQHLG KTAAFQKPKP AKGKAEAHFS LVHYAGTVDY NIVGWLDKNK
DPLNDSVVQL YQKSSLKVLA FLYATHGAEA EGGGGKKGKK KGGSFQTVSA LFRENLGKLM
TNLRSTHPHF VRCLIPNESK TPGLMENYLV IHQLRCNGVL EGIRICRKGF PSRILYGDFK
QRYKVLNASV IPEGQFIDNK KASEKLLGSI DVDHTQYKFG HTKVFFKAGL LGALEEMRDE
KLALLVTMTQ ALCRGYVMRK EFVKMMERRE SIYSIQYNIR SFMNVKHWPW MKLYFKIKPL
LKSAETEKEM AAMKENYEKM KEDLTKALAK KKELEEKMVS LLQEKNDLQL QVTAESENLS
DAEERCEGLI KSKIQLEAKL KETNERLEDE EEINAELTAK KRKLEDECSE LKKDIDDLEL
TLAKVEKEKH ATENKVKNLT EEMASQDESI AKLTKEKKAL QEAHQQTLDD LQAEEDKVNT
LTKAKTKLEQ QVDDLEGSLE QEKKLRMDLE RAKRKLEGDL KLAQESIMDL ENEKQQSDEK
IKKKDFEISQ LLSKIEDEQS LGAQLQKKIK ELQARIEELE EEIEAERAAR AKVEKQRADL
SRELEEISER LEEAGGATAA QIEMNKKREA EFQKMRRDLE ESTLQHEATA AALRKEQADS
VAELGEQIDN LQRVKQKLEK EKSEYKMEID DLTSNMEAVA KAKANLEKMC RTLEDQLSEI
KTKSDENVRQ LNDMNAQRAR LQTENGEFSR QLEEKEALVS QLTRGKQAYT QQIEELKRHI
EEEVKAKNAL AHAVQSARHD CDLLREQYEE EQEAKAELQR GMSKANSEVA QWRTKYETDA
IQRTEELEEA KKKLAQRLQD AEESIEAVNS KCASLEKTKQ RLQGEVEDLM IDVERANSLA
ANLDKKQRNF DKVLAEWKQK YEESQAELEG AQKEARSLST ELFKMKNSYE EALDHLETLK
RENKNLQQEI SDLTEQLGET GKSIHELEKA KKTVESEKSE IQTALEEAEG TLEHEESKIL
RVQLELNQVK SEIDRKLAEK DEEMEQIKRN SQRVIDSMQS TLDSEVRSRN DALRVKKKME
GDLNEMEIQL SHANRQAAEA QKQLRNVQGQ LKDAQLHLDE AVRGQEDMKE QVAMVERRNS
LMQAEIEELR AALEQTERGR KVAEQELVDA SERVGLLHSQ NTSLINTKKK LEADLVQVQG
EVDDAVQEAR NAEEKAKKAI TDAAMMAEEL KKEQDTSAHL ERMKKNLEVT VKDLQHRLDE
AESLAMKGGK KQLQKLESRV RELEAEVEAE QRRGADAVKG VRKYERRVKE LTYQTEEDKK
NVIRLQDLVD KLQLKVKVYK RQAEEAEEQT NTHLSRYRKV QHELEEAQER ADVAESQVNK
LRAKSRDAGK SKDEE
