ID A0A287D4P4_ICTTR Unreviewed; 1928 AA.
AC A0A287D4P4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Myosin heavy chain 1 {ECO:0000313|Ensembl:ENSSTOP00000028561.1};
GN Name=MYH1 {ECO:0000313|Ensembl:ENSSTOP00000028561.1};
OS Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS tridecemlineatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC Xerinae; Marmotini; Ictidomys.
OX NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000028561.1, ECO:0000313|Proteomes:UP000005215};
RN [1] {ECO:0000313|Proteomes:UP000005215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Assembly & Analysis Group;
RG Computational R&D Group;
RG and Sequencing Platform;
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT "The Draft Genome of Spermophilus tridecemlineatus.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSTOP00000028561.1}
RP IDENTIFICATION.
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 -!- 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 EMBL; AGTP01071022; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR Ensembl; ENSSTOT00000041238.1; ENSSTOP00000028561.1; ENSSTOG00000008642.3.
DR GeneTree; ENSGT00940000154760; -.
DR Proteomes; UP000005215; Unassembled WGS sequence.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0032982; C:myosin filament; 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; cd14910; MYSc_Myh1_mammals; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.5.340; -; 4.
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:SF2; MYOSIN-1; 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; SM00015; IQ; 1.
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};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Motor protein {ECO:0000256|ARBA:ARBA00023175, ECO:0000256|PROSITE-
KW ProRule:PRU00782}; Muscle protein {ECO:0000256|ARBA:ARBA00023179};
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:UP000005215};
KW Thick filament {ECO:0000256|ARBA:ARBA00022433}.
FT DOMAIN 33..82
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 86..785
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 662..684
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1132..1169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1291..1916
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1132..1158
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:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1928 AA; 221519 MW; 23A02C2E83E3115D CRC64;
MSSDADMAVF GEAAPYLRKS EKERIEAQNK PFDAKTSVFV VDAKESFVKA TVQSREGGKV
TAKTEGGATV TVKDDQVFPM NPPKYDKIED MAMMTHLHEP AVLYNLKERY AAWMIYTYSG
LFCVTVNPYK WLPVYNAEVV AAYRGKKRQE APPHIFSISD NAYQFMLTDR ENQSILITGE
SGAGKTVNTK RVIQYFATIA VTGEKKKEEA TSGKMQGTLE DQIISANPLL EAFGNAKTVR
NDNSSRFGKF IRIHFGTTGK LASADIETYL LEKSRVTFQL KAERSYHIFY QIMSNKKPDL
IEMLLITTNP YDYAFVSQGE ITVPSIDDQE ELMATDSAID ILGFTSEERV SIYKLTGGVM
HYGNMKFKQK QREEQAEPDG TEVADKAAYL QSLNSADLLK ALCYPRVKVG NEYVTKGQTV
QQVYNAVGAL AKAVYEKMFL WMVTRINQQL DTKQPRQYFI GVLDIAGFEI FDFNSLEQLC
INFTNEKLQQ FFNHHMFVLE QEEYKKEGIE WEFIDFGMDL AACIELIEKP MGIFSILEEE
CMFPKATDTS FKNKLYEQHL GKSNNFQKPK PAKGKVEAHF SLVHYAGTVD YNIAGWLDKN
KDPLNETVVG LYQKSSMKTL AYLFSGAAAA AEAEAGGGGG KKGGKKKGSS FQTVSALFRE
NLNKLMTNLR STHPHFVRCI IPNETKTPGA MEHELVLHQL RCNGVLEGIR ICRKGFPSRI
VYADFKQRYK VLNASAIPEG QFIDSKKASE KLLGSIDIDH TQYKFGHTKV FFKAGLLGLL
EEMRDDKLAQ LITRTQAMCR GFLARVEYQK MVERRESIFC IQYNVRAFMN VKHWPWMKLY
FKIKPLLKSA ETEKEMANMK EEFEKTKESL AKAEAKRKEL EEKMVALMQE KNDLQLQVQS
EADSLADAEE RCDQLIKTKI QLEAKIKEVT ERAEDEEEIN AELTAKKRKL EDECSELKKD
IDDLELTLAK VEKEKHATEN KVKNLTEEMA GLDETIAKLT KEKKALQEAH QQTLDDLQAE
EDKVNTLTKA KIKLEQQVDD LEGSLEQEKK IRMDLERAKR KLEGDLKLAQ ESTMDIENDK
QQLDEKLKKK EFEMSNLQSK IEDEQALGMQ LQKKIKELQA RIEELEEEIE AERASRAKAE
KQRSDLSGEL EEISERLEEA GGATSAQIEM NKKREAEFQK MRRDLEEATL QHEATAATLR
KKHADSVAEL GEQIDNLQRV KQKLEKEKSE MKMEIDDLAS NMETISKSKS QGGFCRTETF
NNWQEETWVR DSSNKSWGEY SRQLDEKDSL VSQLSRGKQA FTQQIEELKR QLEEEVKAKS
ALAHALQSSR HDCDLLREQY EEEQEAKAEL QRAMSKANSE VAQWRTKYET DAIQRTEELE
EAKKKLAQRL QDAEEHVEAV NAKCASLEKT KQRLQNEVED LMIDVERTNA ACAALDKKQR
NFDKILAEWK QKYEETHAEL EASQKESRSL STELFKIKNA YEESLDQLET LKRENKNLQQ
EISDLTEQIA EGGKRIHELE KIKKQIEQEK TELQAALEEA EASLEHEEGK ILRIQLELNQ
VKSEIDRKIA EKDEEIDQLK RNHIRVVESM QSTLDAEIRS RNDAIRIKKK MEGDLNEMEI
QLNHANRMAA EALRNYRNTQ GILKDTQLHL DDALRGQEDL KEQLAMVERR ANLLQAEIEE
LRATLEQTER SRKIAEQELL DASERVQLLH TQNTSLINTK KKLETDISQI QGEMEDIVQE
ARNAEEKAKK AITDAAMMAE ELKKEQDTSA HLERMKKNLE QTVKDLQHRL DEAEQLALKG
GKKQIQKLEA RVRELEGEVE NEQKRNVEAV KGLRKHERRV KELTYQTEED RKNILRLQDL
VDKLQAKVKA YKRQAEEAEE QSNVNLAKFR KIQHELEEAE ERADIAESQV NKLRVKSREV
HTKIISEE
//
