MYH2_CANLF
ID MYH2_CANLF Reviewed; 1940 AA.
AC Q076A7;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Myosin-2;
DE AltName: Full=Myosin heavy chain 2;
DE AltName: Full=Myosin heavy chain 2a;
DE Short=MyHC-2a;
DE AltName: Full=Myosin heavy chain, skeletal muscle, adult 2;
GN Name=MYH2;
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. Required for cytoskeleton organization
CC (By similarity). {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). Interacts with GCSAM.
CC {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-2 (MYO2). {ECO:0000305}.
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DR EMBL; DQ227280; ABB96407.1; -; Genomic_DNA.
DR RefSeq; NP_001070263.1; NM_001076795.1.
DR RefSeq; XP_005619589.1; XM_005619532.2.
DR RefSeq; XP_013968678.1; XM_014113203.1.
DR AlphaFoldDB; Q076A7; -.
DR SMR; Q076A7; -.
DR STRING; 9615.ENSCAFP00000025869; -.
DR ABCD; Q076A7; 1 sequenced antibody.
DR Ensembl; ENSCAFT00030003826; ENSCAFP00030003397; ENSCAFG00030002092.
DR Ensembl; ENSCAFT00040033469; ENSCAFP00040029127; ENSCAFG00040017838.
DR Ensembl; ENSCAFT00845004767; ENSCAFP00845003815; ENSCAFG00845002613.
DR GeneID; 608242; -.
DR KEGG; cfa:608242; -.
DR CTD; 4620; -.
DR VEuPathDB; HostDB:ENSCAFG00845002613; -.
DR GeneTree; ENSGT00940000154760; -.
DR InParanoid; Q076A7; -.
DR OrthoDB; 47111at2759; -.
DR Proteomes; UP000002254; Chromosome 5.
DR Bgee; ENSCAFG00000030337; Expressed in tongue and 26 other tissues.
DR GO; GO:0031672; C:A band; IEA:Ensembl.
DR GO; GO:0005826; C:actomyosin contractile ring; IEA:Ensembl.
DR GO; GO:0005911; C:cell-cell junction; IEA:Ensembl.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
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:0070252; P:actin-mediated cell contraction; IEA:Ensembl.
DR GO; GO:0006936; P:muscle contraction; IBA:GO_Central.
DR GO; GO:0001778; P:plasma membrane repair; IEA:Ensembl.
DR GO; GO:0014823; P:response to activity; IEA:Ensembl.
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..1940
FT /note="Myosin-2"
FT /id="PRO_0000274166"
FT DOMAIN 33..82
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01190"
FT DOMAIN 86..783
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 786..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 REGION 1154..1173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1884..1920
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 844..1940
FT /evidence="ECO:0000255"
FT COMPBIAS 1902..1920
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 625
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 1287
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1289
FT /note="Phosphoserine"
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 1543
FT /note="Phosphoserine"
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 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 1737
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1740
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
SQ SEQUENCE 1940 AA; 223211 MW; DE214B4C5B951033 CRC64;
MSSDQEMAIF GEAAPYLRKS EKERIEAQNR PFDAKTSVFV AEPKESFVKG TVQSREGGKV
TVKTEAGATL TVKEDQVFPM NPPKYDKIED MAMMTHLHEP AVLYNLKERY AAWMIYTYSG
LFCVTVNPYK WLPVYNPEVV TAYRGKKRQE APPHIFSISD NAYQFMLTDR ENQSILITGE
SGAGKTVNTK RVIQYFATIA VTGEKKKEEA TSGKMQGTLE DQIISANPLL EAFGNAKTVR
NDNSSRFGKF IRIHFGTTGK LASADIETYL LEKSRVTFQL KAERSYHIFY QITSNKKPEL
IEMLLITTNP YDYPFVSQGE ISVASIDDQE ELIATDSAID ILGFTNEEKV SIYKLTGAVM
HYGNLKFKQK QREEQAEPDG TEVADKAAYL QSLNSADLLK ALCYPRVKVG NEFVTKGQTV
EQVTNAVGAL AKAVYEKMFL WMVTRINQQL DTKQPRQYFI GVLDIAGFEI FDFNSLEQLC
INFTNEKLQQ FFNHHMFVLE QEEYKKEGIE WTFIDFGMDL AACIELIEKP MGIFSILEEE
CMFPKATDTS FKNKLYEQHL GKSANFQKPK VVKGKAEAHF SLIHYAGVVD YNITGWLDKN
KDPLNETVVG LYQKSSMKTL AYLFSGAQTA EAEASGGAKK GGKKKGSSFQ TVSALFRENL
NKLMTNLRST HPHFVRCIIP NETKTPGAME HELVLHQLRC NGVLEGIRIC RKGFPSRILY
ADFKQRYKVL NASAIPEGQF IDSKKASEKL LASIDIDHTQ YKFGHTKVFF KAGLLGLLEE
MRDDKLAQLI TRTQARCRGF LARVEYQKMV ERRESIFCIQ YNIRAFMNVK HWPWMKLFFK
IKPLLKSAET EKEMATMKEE FQKTKDELAK SEAKRKELEE KMVTLLKEKN DLQLQVQAEA
EGLADAEERC DQLIKTKIQL EAKIKEVTER AEDEEEINAE LTAKKRKLED ECSELKKDID
DLELTLAKVE KEKHATENKV KNLTEEMAGL DETIAKLTKE KKALQEAHQQ TLDDLQAEED
KVNTLTKAKI KLEQQVDDLE GSLEQEKKLR MDLERAKRKL EGDLKLAQES IMDIENEKQQ
LDEKLKKKEF EMSNLQSKIE DEQALGIQLQ KKIKELQARI EELEEEIEAE RASRAKAEKQ
RSDLSRELEE ISERLEEAGG ATSAQIEMNK KREAEFQKMR RDLEEATLQH EATAATLRKK
HADSVAELGE QIDNLQRVKQ KLEKEKSEMK MEIDDLASNV ETVSKAKGNL EKMCRTLEDQ
VSELKSKEEE QQRLINDLTT QRGRLQTESG EFSRQLDEKE ALVSQLSRGK LAFTQQIEEL
KRQLEEEIKA KNALAHALQS SRHDCDLLRE QYEEEQESKA ELQRALSKAN SEVAQWRTKY
ETDAIQRTEE LEEAKKKLAQ RLQAAEEHVE AVNAKCASLE KTKQRLQNEV EDLMLDVERT
NAACAALDKK QRNFDKILAE WKQKYEETHA ELEASQKEAR SLGTELFKMK NAYEESLDQL
ETLKRENKNL QQEISDLTEQ IAEGGKRIHE LEKIKKQVEQ EKSEIQAALE EAEASLEHEE
GKILRIQLEL NQVKSEIDRK IAEKDEEIDQ LKRNHIRVVE SMQTMLDAEI RSRNDAIRLK
KKMEGDLNEM EIQLNHANRM AAEALRNYRN TQGILKDTQI HLDDALRGQE DLKEQLAMVE
RRANLLQAEI EELRATLEQT ERSRKIAEQE LLDASERVQL LHTQNTSLIN TKKKLETDIS
QIQGEMEDII QEARNAEEKA KKAITDAAMM AEELKKEQDT SAHLERMKKN MEQTVKDLQH
RLDEAEQLAL KGGKKQIQKL EARVRELEGE VESEQKRNAE AVKGLRKHER RVKELTYQTE
EDRKNILRLQ DLVDKLQAKV KSYKRQAEEA EEQSNTNLSK FRKLQHELEE AEERADIAES
QVNKLRVKSR EVHTKVISEE
