MYH8_CANLF
ID MYH8_CANLF Reviewed; 1939 AA.
AC Q076A4;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Myosin-8;
DE AltName: Full=Developmental myosin heavy chain neonatal;
DE AltName: Full=Myosin heavy chain 8;
DE AltName: Full=Myosin heavy chain, skeletal muscle, perinatal;
DE Short=MyHC-perinatal;
GN Name=MYH8;
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}.
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DR EMBL; DQ227283; ABB96410.1; -; Genomic_DNA.
DR RefSeq; NP_001070703.1; NM_001077235.1.
DR RefSeq; XP_013968652.1; XM_014113177.1.
DR AlphaFoldDB; Q076A4; -.
DR SMR; Q076A4; -.
DR STRING; 9612.ENSCAFP00000025828; -.
DR PaxDb; Q076A4; -.
DR PRIDE; Q076A4; -.
DR GeneID; 403808; -.
DR KEGG; cfa:403808; -.
DR CTD; 4626; -.
DR eggNOG; KOG0161; Eukaryota.
DR HOGENOM; CLU_000192_4_0_1; -.
DR InParanoid; Q076A4; -.
DR OMA; XPLGIFS; -.
DR OrthoDB; 47111at2759; -.
DR TreeFam; TF314375; -.
DR Reactome; R-CFA-390522; Striated Muscle Contraction.
DR Proteomes; UP000002254; Chromosome 5.
DR Bgee; ENSCAFG00000017522; Expressed in tongue and 12 other tissues.
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; 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-8"
FT /id="PRO_0000274170"
FT DOMAIN 35..84
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01190"
FT DOMAIN 88..783
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 783..815
FT /note="IQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT REGION 660..682
FT /note="Actin-binding"
FT /evidence="ECO:0000250"
FT REGION 762..776
FT /note="Actin-binding"
FT /evidence="ECO:0000250"
FT COILED 844..1939
FT /evidence="ECO:0000255"
FT BINDING 181..188
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 66
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 71
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 132
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000255"
FT MOD_RES 391
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 421
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 426
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 627
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 758
FT /note="Pros-methylhistidine"
FT /evidence="ECO:0000250|UniProtKB:Q28641"
FT MOD_RES 1093
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1097
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1163
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1238
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1242
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1244
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1256
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1262
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1266
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1287
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1293
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1304
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1307
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1465
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1468
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1475
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1493
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1496
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1502
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1515
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1518
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1555
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1575
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1601
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1604
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1715
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1727
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1731
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1740
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
SQ SEQUENCE 1939 AA; 222810 MW; 12F2CACED632C07E CRC64;
MSASSDAEMA VFGEAAPFLR KSEKERIEAQ NKPFDAKTSV FVAEPKASYV KSTIQSKEGG
KVTVKTEGGA TLTVREDQVF PMNPPKYDKI EDMAMMTHLH EPGVLYNLKE RYAAWMIYTY
SGLFCVTVNP YKWLPVYNPE VVAAYRGKKR QEAPPHIFSI SDNAYQFMLT DRENQSILIT
GESGAGKTVN TKRVIQYFAT IAVTGEKKKE EATSGKMQGT LEDQIISANP LLEAFGNAKT
VRNDNSSRFG KFIRIHFGTT GKLASADIET YLLEKSRVTF QLKAERSYHI FYQITSNKKP
DLIEMLLITT NPYDYAFVSQ GEITVPSIDD QEELMATDSA IDILGFTPEE KVSIYKLTGA
VMHYGNMKFK QKQREEQAEP DGTEVADKAA YLQNLNSADL LKALCYPRVK VGNEYVTKGQ
TVQQVYNAVG ALAKAVYEKM FLWMVTRINQ QLDTKQPRQY FIGVLDIAGF EIFDFNSLEQ
LCINFTNEKL QQFFNHHMFV LEQEEYKKEG IEWTFIDFGM DLAACIELIE KPLGIFSILE
EECMFPKATD TSFKNKLYDQ HLGKSANFQK PKVVKGKAEA HFSLIHYAGT VDYNIGGWLD
KNKDPLNDTV VGLYQKSAMK TLASLFSTYA SAEADSGAKK GAKKKGSSFQ TVSALFRENL
NKLMTNLRST HPHFVRCIIP NETKTPGAME HELVLHQLRC NGVLEGIRIC RKGFPSRILY
GDFKQRYKVL NASAIPEGQF IDSKKASEKL LASIDIDHTQ YKFGHTKVFF KAGLLGLLEE
MRDEKLSQII TRTQAVCRGF LMRVEYQKML QRREALFCIQ YNIRAFMNVK HWPWMRLFFK
IKPLLKSAET EKEMATMKEE FQKTKDELAK SEAKRKELEE KMVTLLKEKN DLQLQVQSEA
DALADAEERC EQLIKNKIQL EAKIKEVTER AEDEEEINAE LTAKKRKLED ECSELKKDID
DLELTLAKVE KEKHATENKV KNLTEEMAGL DETIAKLTKE KKALQEAHQQ TLDDLQAEED
KVNTLTKAKT KLEQQVDDLE GSLEQERKLR MDLERAKRKL EGDLKLAQES TMDAENDKQQ
LDEKLKKKEF EISNLLSKIE DEQAIEIQLQ KKIKELQARI EELEEEIEAE RASRAKAEKQ
RSDLSRELEE ISERLEEAGG ATSAQIEMNK KREAEFQKMR RDLEEATLQH EATAATLRKK
HADSVAELGE QIDNLQRVKQ KLEKEKSEMK MEIDDLASNA ETISKAKGNL EKMCRTLEDQ
VSELKTKEEE QQRLINDLTA QRARLQTEAG EYSRQLDEKD ALVSQLSRSK QASTQQIEEL
KRQLEEETKA KNALAHALQS SRHDCDLLRE QYEEEQEGKA ELQRALSKAN SEVAQWRTKY
ETDAIQRTEE LEEAKKKLAQ RLQEAEEHVE AVNAKCASLE KTKQRLQNEV EDLMLDVERS
NAACAALDKK QRNFDKVLAE WKQKYEETQA ELEASQKEAR TLSTELFKVK NAYEESLDQV
ETLKRENKNL QQEISDLTEQ IAEGGKQIHE LEKIKKQVEQ EKCDIQAALE EAEASLEHEE
GKILRIQLEL NQVKSEVDRK IAEKDEEIDQ LKRNHIRVME SMQSTLDAEI RSRNDALRVK
KKMEGDLNEM EIQLNHANRL AAESLRNYRN TQGILKDTQL HLDDALRGQE DLKEQLAMVE
RRANLLQAEI EELRATLEQT ERSRKTAEQE LLDASERVQL LHTQNTSLIN TKKKLENDVS
QLQSEVEEVI QESRNAEEKA KKAITDAAMM AEELKKEQDT SAHLERMKKN MEQTVKDLQH
RLDEAEQLAL KGGKKQIQKL EARVHELEGE VESEQKRNAE AVKGLRKHER RVKELTYQTE
EDRKNVLRLQ DLVDKLQAKV KSYKRQAEEA EEQSNTNLAK FRKLQHELEE AEERADIAES
QVNKLRVKSR EVHTKISAE
