ID A0A3Q1MDD2_BOVIN Unreviewed; 1931 AA.
AC A0A3Q1MDD2;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Myosin-4 {ECO:0000256|ARBA:ARBA00044107};
DE AltName: Full=Myosin heavy chain 2b {ECO:0000256|ARBA:ARBA00044300};
DE AltName: Full=Myosin heavy chain 4 {ECO:0000256|ARBA:ARBA00044226};
GN Name=MYH4 {ECO:0000313|Ensembl:ENSBTAP00000068935.1,
GN ECO:0000313|VGNC:VGNC:55854};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913 {ECO:0000313|Ensembl:ENSBTAP00000068935.1, ECO:0000313|Proteomes:UP000009136};
RN [1] {ECO:0000313|Ensembl:ENSBTAP00000068935.1, ECO:0000313|Proteomes:UP000009136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000068935.1,
RC ECO:0000313|Proteomes:UP000009136};
RA Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT "ARS-UCD1.2.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSBTAP00000068935.1}
RP IDENTIFICATION.
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000068935.1};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Muscle contraction. {ECO:0000256|ARBA:ARBA00037488}.
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}.
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DR Ensembl; ENSBTAT00000075858.1; ENSBTAP00000068935.1; ENSBTAG00000037794.4.
DR VEuPathDB; HostDB:ENSBTAG00000037794; -.
DR VGNC; VGNC:55854; MYH4.
DR GeneTree; ENSGT00940000163211; -.
DR Proteomes; UP000009136; Chromosome 19.
DR Bgee; ENSBTAG00000037794; Expressed in laryngeal cartilage and 25 other cell types or tissues.
DR ExpressionAtlas; A0A3Q1MDD2; baseline.
DR GO; GO:0030016; C:myofibril; IEA:UniProtKB-SubCell.
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 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:SF78; 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; 5.
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 3: Inferred from homology;
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}; Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Methylation {ECO:0000256|ARBA:ARBA00022481};
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}; Reference proteome {ECO:0000313|Proteomes:UP000009136}.
FT DOMAIN 34..83
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 87..774
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 651..673
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1145..1164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 177..184
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1931 AA; 222235 MW; E116972E3FF39FC6 CRC64;
MVNSDQEMAI FGEAAPYLRK SEKERIEAQN KPFDAKTSVF VVDPKESFVK ATVQSREGGK
VTAKTEAGAT VTVKEDQVFP MNPPKYDKIE DMAMMTHLHE PAVLYNLKER YAAWMIYTYS
GLFCVTVNPY KWLPVYNAEV VTAYRGKKRQ EAPPHIFSIS DNAYQFMLTG ELDVSIGESG
AGKTVNTKRV IQYFATIAVT GEKKKEEPTS GKMQGTLEDQ IISANPLLEA FGNAKTVRND
NSSRFGKFIR IHFGTTGKLA SADIETYLLE KSRVTFQLKA ERSYHIFYQI MSNKKPELIE
MLLITTNPYD YAYVSQGEIT VPSIDDQEEL IATDSAIDIL GFTSDERVSI YKLTGAVMHY
GNLKFKQKQR EEQAEPDGTE VADKAAYLQS LNSADLLKAL CYPRVKVGNE FVTKGQTVQQ
VSVYNAVGAL AKAVYEKMFL WMVTRINQQL DTKQPRQYFI GVLDIAGFEI FDFNSLEQLC
INFTNEKLQQ FFNHHMFVLE QEEYKKEGIE WEFIDFGMDL AACIELIEKP MGIFSILEEE
CMFPKATDTS FKNKLYEQHL GKSNNFQKPK PAKGKAEAHF SLVHYAGTVD YNIAGWLDKN
KDPLNETVVG LYQKSAMKTL AFLFAGGPSA EGGKKKGSSF QTVSALFREN LNKLMTNLRS
THPHFVRCII PNETKTPGAM EHELVLHQLR CNGVLEGIRI CRKGFPSRIL YADFKQRYKV
LNASAIPEGQ FIDSKKASEK LLGSIDIDHT QYKFGHTKVF FKAGLLGILE EMRDEKLAQL
ITRTQAICRG FLMRVEFRKM MERRESIFCI QYNVRAFMNV KHWPWMKLYF KIKPLLKSAE
TEKEMANMKE EFEKTKEELA KSEAKRKELE EKMVTLMQEK NDLQLQVQSE ADGLADAEER
CDQLIKTKIQ LEAKIKELTE RAEDEEEINA ELTAKKRKLE DECSELKKDI DDLELTLAKV
EKEKHATENK VKNLTEEMAG LDENIAKLTK EKKALQEAHQ QTLDDLQAEE DKVNTLTKSK
TKLEQQVEDL EGSLEQEKKL RMDLERAKRK LEGDLKLAQE STMDIENDKQ QLDEKLKKKE
FEMSNLQSKI EDEQALAMQL QKKIKELQAR IEELEEEIEA ERASRAKAEK LRSDLSRELE
EISERLEEAG GATSAQIEMN KKREAEFQKM RRDLEEATLQ HEATAAALRK KHADSVAELG
EQIDNLQRVK QKLEKEKSEM KMEIDDLASN METVSKAKGN LEKMCRTLED QLSEVKSKEE
EHQRLINELS VQKAHLHTES GEFSRQLEEK DALVSQLSRG KQAFTQQIEE LKRQLEEETK
AKSALAHALQ SARHDCDLLR EQYEEEQEGK AELQRALSKA NSEVAQWRTK YETDAIQRTE
ELEEAKKKLA QRLQDAEEHV EVVNAKCASL EKTKQRLQNE VEDLMLDVER SNAACAALDK
KQRNFDKVLS EWKQKYEETQ ADLEASQKES RSLSTELFKV KNAYEESLDQ LETLKRENKN
LQQEISDLTE QIAEGGKHIH ELEKVKKQIE QEKGELQAAL EEAEASLEHE EGKILRIQLE
LNQVKSEIDR KIAEKDEEID QLKRNHLRVV ESMQSTLDAE IRSRNDALRI KKKMEGDLNE
MEIQLNHANR QATEAIKNLR NTQGVLKDTQ LHLDDAIRGQ DDLKEQLAMV ERRANLMQAE
IEELRASLEQ TERSRRVAEQ ELLDASERVQ LLHTQNTSLI NTKKKLETDI TQIQGEMEDI
VQEARNAEEK AKKAITDAAM MAEELKKEQD TSAHLERMKK NMEQTVKDLQ HRLDEAEQLA
LKGGKKQIQK LEARVRELEN EVENEQKRNA EAVKGLRKHE RRVKELTYQT EEDRKNVLRL
QDLVDKLQSK VKAYKRQAEE AEEQSNVNLA KFRKLQHELE EAEERADIAE SQVNKLRVKS
REVHTKVISE E
//
