ID O42352_CYPCA Unreviewed; 1931 AA.
AC O42352;
DT 01-JAN-1998, integrated into UniProtKB/TrEMBL.
DT 01-JAN-1998, sequence version 1.
DT 24-JAN-2024, entry version 109.
DE SubName: Full=Myosin heavy chain {ECO:0000313|EMBL:BAA22068.1};
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 {ECO:0000313|EMBL:BAA22068.1};
RN [1] {ECO:0000313|EMBL:BAA22068.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Fast skeletal muscle {ECO:0000313|EMBL:BAA22068.1};
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).
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 {ECO:0000256|ARBA:ARBA00038612}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril
CC {ECO:0000256|ARBA:ARBA00004657}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000256|ARBA:ARBA00008314,
CC ECO:0000256|PROSITE-ProRule:PRU00782}.
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; D89991; BAA22068.1; -; mRNA.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0051015; F:actin filament binding; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003774; F:cytoskeletal motor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0048731; P:system development; IEA:UniProt.
DR CDD; cd01377; MYSc_class_II; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.5.340; -; 5.
DR Gene3D; 1.20.5.370; -; 4.
DR Gene3D; 1.20.5.4820; -; 1.
DR Gene3D; 1.20.58.530; -; 1.
DR Gene3D; 6.10.250.2420; -; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR Gene3D; 2.30.30.360; Myosin S1 fragment, N-terminal; 1.
DR Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 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 PANTHER; PTHR45615; MYOSIN HEAVY CHAIN, NON-MUSCLE; 1.
DR PANTHER; PTHR45615:SF44; MYOSIN-4; 1.
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; SSF90257; Myosin rod fragments; 6.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF57997; Tropomyosin; 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 {ECO:0000256|ARBA:ARBA00023203, ECO:0000256|PROSITE-
KW ProRule:PRU00782};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00782};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Motor protein {ECO:0000256|ARBA:ARBA00023175, ECO:0000256|PROSITE-
KW ProRule:PRU00782};
KW Myosin {ECO:0000256|ARBA:ARBA00023123, ECO:0000256|PROSITE-
KW ProRule:PRU00782};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00782}.
FT DOMAIN 32..81
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 85..776
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 653..675
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1877..1931
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 840..1154
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1191..1830
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 178..185
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1931 AA; 221163 MW; 59466B7BD0872DDD CRC64;
MGDGEMECFG PAAIYLRKPE RERIEAQTAP FDAKTAFFVT DAAEMYLKST LVSREGGKAT
VKTHCGKTVT VKEDEIFQMN PPKFDKMEDM AMMTHLNEPS VLFNLKERYA AWMIYTYSGL
FCATVNPYKW LPVYDAVVVA GYRGKKRIEA PPHIFSISDN AYQFMLTDRE NQSILITGES
GAGKTVNTKR VIQYFATVAM SGPKKTEAVP GKMQGSLEDQ IIAANPLLEA YGNAKTIRND
NSSRFGKFIR IHFGTTGKLA KADIETYLLE KSRVTFQLSA ERSYHIFYQL MTGHKPELLE
ALLITTNPYD YPMISQGEIT VKSIDDVEEF IATDTAIDIL GFTADEKISI YKLTGAVMHH
GSMKFKQKQR EEQAEPDGNE AADKIAYLLG INSADMLKAL CYPRVKVGNE MVTKGQTVPQ
VNNAVSALCK SIYEKMFLWM VVRINEMLNT TNPREFYIGV LDIAGFEIFD YNSLEQLCIN
FTNEKLQQFF NHTMFVLEQE EYKKEGIEWA FIDFGMDLAA CIELIEKPMG IFSILEEECM
FPKATDTSFK NKLHDQHLGK SAAFQKPKPA KGKPEAHFSL LHYAGTVDYN IAGWLEKNKD
PLNDSVVQLY QKSALKVLAL LYVAVPEEGG GKKAGKKKGG SFQTVSALFR ENLAKLMTNL
RSTHPHFVRC LIPNESKTPG LMENFLVIHQ LRCNGVLEGI RICRKGFPSR IHYGDFKQRY
KILNASVIPE GHFIDNKKAT EKLLGSIDVD HTQYKFGHTK VFFKAGLLGA LEEMRDEKLV
NLVTMTQALA RGYVMRKEFV KMMERREAIF SIQYNIRSFM NVKHWPWMKV YFKIKPLLKT
AESEKEMASM KENFEKMKED LTKALAKKKE LEEKMVSLVQ EKNDLLLQVT SESENLCDAE
ERCEGLIKSK IQLEGKLKET NERLEDEEEI NAELTAKKRK LEDECSELKK DIDDLELTLA
KVEKEKHATE NKVKNLTEEM ACQDESIAKL TKEKKALQEA HQQTLDDLQA EEDKVNTLTK
AKTKLEQQVD DLEGSLEQEK KLRMDLERVK RKLEGDLKLA QESIMDLENE KQQSDEKIKK
KDFEISQFLS KIEDEQSLGA QLQKKIKELQ ARIEELEEEI EAERSARAKV EKQRADLSRE
LEEISERLEE AGGATAAQIE MNKKREADFQ KMRRDLEEST LQHEATAAAL RKKQADTVAE
LGEQIDNLQR VKQKLEKEKS EYKMEIDDLT SNMEAVAKAK GNLEKMCRTL EDQLSEIKAK
SDENSRQLND MNAQRARLQT ENGEFSRQLE EKEALVSQLT RGKQAFTQQI EDLQRHVEEE
VKAKNALAHA VQSARHDCDL LREQYEEEQE AKTELQRGMS KANSEVAQWR AKYETDAIQR
TEELEEAKKK LAQRLQDAEE SIEAVSSKCA SLEKTKQRLQ GEVEDLMIDG ERANALAANL
DKKQRNFDKV LAEWKQKYEE SQAELEAAQK EARSLSTELF KMKNSYEEAL DHLETLKREN
KNLQQEISDL SEQLGETGKS IHELEKAKKI VESEKAEIQT ALEEAESTLE HEESKILRVQ
LELNQVKSEI DRKLAEKDEE IEQIKRNSQR VMDSMQSTLD SEIRSRNDAL RVKKKMEGDL
NEMEVQLSHA NRQAAEAQKQ LRNVQGQLKD AQLHLDEAVR GQEDMKEQVA MVERRNTLMQ
AEIEELRAAL EQTERGRKVA EQELVDASER VGLLHSQNTS LINTKKKLET DLLQVQGEVD
DAVQEARNAE EKAKKAITDA AMMAEELKKE QDTSAHLERM KKNMEVTVKD LQHRLDEAES
LAMKGGKKQL QKLESRVHEL EAEVEAEQRR GADAVKGVRK YERRVKELTY QTEEDKKSVT
RLQDLVDKLQ LKVKAYKRQA EEAEEQANTH LSRYRKVQHE LEESHERADI AESQVNKLRA
KSREAGKTKD E
//