MYH1_CANLF
ID MYH1_CANLF Reviewed; 1939 AA.
AC Q076A6;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 2.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Myosin-1;
DE AltName: Full=Myosin heavy chain 1;
DE AltName: Full=Myosin heavy chain 2x;
DE Short=MyHC-2x;
DE AltName: Full=Myosin heavy chain, skeletal muscle, adult 1;
GN Name=MYH1;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Maccatrozzo L., Patruno M., Mascarello F., Reggiani C.;
RT "Canine myosin heavy chain expression.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Muscle contraction. {ECO:0000250}.
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). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril {ECO:0000250}. Note=Thick
CC filaments of the myofibrils. {ECO:0000250}.
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}.
CC -!- CAUTION: Represents a conventional myosin. This protein should not be
CC confused with the unconventional myosin-1 (MYO1). {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABB96408.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; DQ227281; ABB96408.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; NP_001107189.1; NM_001113717.1.
DR RefSeq; XP_005619524.1; XM_005619467.2.
DR AlphaFoldDB; Q076A6; -.
DR SMR; Q076A6; -.
DR STRING; 9612.ENSCAFP00000025847; -.
DR PaxDb; Q076A6; -.
DR GeneID; 100135061; -.
DR KEGG; cfa:100135061; -.
DR CTD; 4619; -.
DR eggNOG; KOG0161; Eukaryota.
DR InParanoid; Q076A6; -.
DR OrthoDB; 47111at2759; -.
DR TreeFam; TF314375; -.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0030016; C:myofibril; IEA:UniProtKB-SubCell.
DR GO; GO:0032982; C:myosin filament; IBA:GO_Central.
DR GO; GO:0016460; C:myosin II complex; IBA:GO_Central.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0000146; F:microfilament motor activity; IBA:GO_Central.
DR GO; GO:0006936; P:muscle contraction; IBA:GO_Central.
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; SM00015; IQ; 2.
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 3: Inferred from homology;
KW Actin-binding; ATP-binding; Calmodulin-binding; Coiled coil; Cytoplasm;
KW Methylation; Motor protein; Muscle protein; Myosin; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Thick filament.
FT CHAIN 1..1939
FT /note="Myosin-1"
FT /id="PRO_0000274162"
FT DOMAIN 33..82
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01190"
FT DOMAIN 86..782
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 785..814
FT /note="IQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT REGION 659..681
FT /note="Actin-binding"
FT /evidence="ECO:0000250"
FT REGION 761..775
FT /note="Actin-binding"
FT /evidence="ECO:0000250"
FT REGION 1125..1147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1153..1172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 843..1939
FT /evidence="ECO:0000255"
FT BINDING 179..186
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 64
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 69
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 130
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000255"
FT MOD_RES 389
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 392
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 419
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 424
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 625
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 757
FT /note="Pros-methylhistidine"
FT /evidence="ECO:0000250|UniProtKB:Q28641"
FT MOD_RES 1092
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1096
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1162
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1237
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1241
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1243
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1255
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1261
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1265
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1286
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1288
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1292
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1303
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1306
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1464
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1467
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1474
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1492
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1495
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1501
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1514
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1517
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1554
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1574
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1600
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1603
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1714
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1726
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1730
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1736
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1739
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
SQ SEQUENCE 1939 AA; 223148 MW; DA9D9C477D77051C CRC64;
MSSDQEMAIF GEAAPYLRKS EKERIEAQNR PFDAKTSVFV AEPKESFVKG TVQSREGGKV
TVKTEAGATL TVKEDQVFPM NPPKYDKIED MAMMTHLHEP AVLYNLKERY AAWMIYTYSG
LFCVTVNPYK WLPVYNAEVV TAYRGKKRQE APPHIFSISD NAYQFMLTDR ENQSILITGE
SGAGKTVNTK RVIQYFATIA VTGDKKKEEV TSGKIQGTLE DQIISANPLL EAFGNAKTVR
NDNSSRFGKF IRIHFGTTGK LASADIETYL LEKSRVTFQL KAERSYHIFY QIMSNKKPDL
IEMLLITTNP YDYAFVSQGE ITVPSIDDQE ELIATDSAID ILGFTSDERV SIYKLTGAVM
HYGNMKFKQK QREEQAEPDG TEVADKAAYL QSLNSADLLK ALCYPRVKVG NEFVTKGQTV
QQVYNAVGAL AKAVYEKMFL WMVTRINQQL DTKQPRQYFI GVLDIAGFEI FDFNSLEQLC
INFTNEKLQQ FFNHHMFVLE QEEYKKEGIE WEFIDFGMDL AACIELIEKP MGIFSILEEE
CMFPKATDTS FKNKLYEQHL GKSNNFQKPK PAKGKVEAHF SLIHYAGTVD YNIGGWLDKN
KDPLNETVVG LYQKSAMKTL ANLFSGATAA EAEAGGGKKG GKKKGSSFQT VSALFRENLN
KLMTNLRSTH PHFVRCIIPN ETKTPGAMEH ELVLHQLRCN GVLEGIRICR KGFPSRILYA
DFKQRYKVLN ASAIPEGQFI DSKKASEKLL GSIDVDHTQY KFGHTKVFFK AGLLGLLEEM
RDDKLAQLIT RTQARCRGFL ARVEYQKMVE RRESIFCIQY NIRAFMNVKH WPWMKLYFKI
KPLLKSAETE KEMANMKEEF EKTKESLAKA EAKRKELEEK MVALMQEKND LQLQVQAEAD
SLADAEERCD QLIKTKIQLE AKIKEVTERA EDEEEINAEL TAKKRKLEDE CSELKKDIDD
LELTLAKVEK EKHATENKVK NLTEEMAGLD ETIAKLTKEK KALQEAHQQT LDDLQAEEDK
VNTLTKAKIK LEQQVDDLEG SLEQEKKIRM DLERAKRKLE GDLKLAQEST MDIENDKQQL
DEKLKKKEFE MSNLQSKIED EQALAMQLQK KIKELQARIE ELEEEIEAER ASRAKAEKQR
SDLSRELEEI SERLEEAGGA TSAQIEMNKK REAEFQKMRR DLEEATLQHE ATAATLRKKH
ADSVAELGEQ IDNLQRVKQK LEKEKSEMKM EIDDLASNME TVSKAKGNLE KMCRTLEDQV
SELKTKEEEQ QRLINDLTAQ RARLQTESGE YSRQLDEKDS LVSQLSRGKL AFTQQIEELK
RQLEEEIKAK SALAHALQSA RHDCDLLREQ YEEEQEGKAE LQRAMSKANS EVAQWRTKYE
TDAIQRTEEL EEAKKKLAQR LQDAEEHVEA VNAKCASLEK TKQRLQNEVE DLMIDVERTN
AACAALDKKQ RNFDKILAEW KQKYEETHAE LEASQKESRS LSTELFKIKN AYEESLDQLE
TLKRENKNLQ QEISDLTEQI AEGGKRIHEL EKIKKQVEQE KTELQAALEE AEASLEHEEG
KILRIQLELN QVKSEIDRKI AEKDEEIDQL KRNHIRVVES MQSTLDAEIR SRNDAIRLKK
KMEGDLNEME IQLNHANRMA AEALRNYRNT QGILKDTQIH LDDALRGQED LKEQLAMVER
RANLLQAEIE ELRATLEQTE RSRKIAEQEL LDASERVQLL HTQNTSLINT KKKLETDISQ
IQGEMEDIIQ EARNAEEKAK KAITDAAMMA EELKKEQDTS AHLERMKKNM EQTVKDLQHR
LDEAEQLALK GGKKQIQKLE ARVRELEGEV ESEQKHNIET VKSLRKHERR VKELTYQTEE
DRKNVLRLQD LVDKLQAKVK AYKRQAEEAE EQSNVNLSKF RKLQHELEEA EERADIAESQ
VNKLRVKSRE VHTKIISEE
