ID H2QCA0_PANTR Unreviewed; 1937 AA.
AC H2QCA0;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 2.
DT 27-MAR-2024, entry version 69.
DE SubName: Full=Myosin heavy chain 1 {ECO:0000313|Ensembl:ENSPTRP00000014942.6};
GN Name=MYH1 {ECO:0000313|Ensembl:ENSPTRP00000014942.6,
GN ECO:0000313|VGNC:VGNC:57856};
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000014942.6, ECO:0000313|Proteomes:UP000002277};
RN [1] {ECO:0000313|Ensembl:ENSPTRP00000014942.6, ECO:0000313|Proteomes:UP000002277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16136131; DOI=10.1038/nature04072;
RG Chimpanzee sequencing and analysis consortium;
RT "Initial sequence of the chimpanzee genome and comparison with the human
RT genome.";
RL Nature 437:69-87(2005).
RN [2] {ECO:0000313|Ensembl:ENSPTRP00000014942.6}
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; AACZ04027042; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PaxDb; 9598-ENSPTRP00000014942; -.
DR Ensembl; ENSPTRT00000016146.6; ENSPTRP00000014942.6; ENSPTRG00000008771.7.
DR VGNC; VGNC:57856; MYH1.
DR eggNOG; KOG0161; Eukaryota.
DR GeneTree; ENSGT00940000154760; -.
DR HOGENOM; CLU_000192_8_1_1; -.
DR InParanoid; H2QCA0; -.
DR TreeFam; TF314375; -.
DR Proteomes; UP000002277; Chromosome 17.
DR Bgee; ENSPTRG00000008771; Expressed in skeletal muscle tissue and 5 other cell types or tissues.
DR GO; GO:0031672; C:A band; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IEA:Ensembl.
DR GO; GO:0014704; C:intercalated disc; IEA:Ensembl.
DR GO; GO:0005859; C:muscle myosin complex; 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-UniRule.
DR GO; GO:0000146; F:microfilament motor activity; IBA:GO_Central.
DR GO; GO:0006936; P:muscle contraction; IBA:GO_Central.
DR CDD; cd14910; MYSc_Myh1_mammals; 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: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 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 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:UP000002277};
KW Thick filament {ECO:0000256|ARBA:ARBA00022433}.
FT DOMAIN 34..83
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 87..783
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 660..682
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1126..1148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1154..1173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 180..187
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1937 AA; 222902 MW; 5F55BFAE659D2509 CRC64;
AMSSDSEMAI FGEAAPFLRK SERERIEAQN KPFDAKTSVF VVDPKESFVK ATVQSREGGK
VTAKTEAGAT VTVKDDQVFP MNPPKYDKIE DMAMMTHLHE PAVLYNLKER YAAWMIYTYS
GLFCVTVNPY KWLPVYNAEV VTAYRGKKRQ EAPPHIFSIS DNAYQFMLTD RENQSILITG
ESGAGKTVNT KRVIQYFATI AVTGEKKKEE VTSGKMQGTL EDQIISANPL LEAFGNAKTV
RNDNSSRFGK FIRIHFGTTG KLASADIETY LLEKSRVTFQ LKAERSYHIF YQIMSNKKPD
LIEMLLITTN PYDYAFVSQG EITVPSIDDQ EELMATDSAI EILGFTSDER VSIYKLTGAV
MHYGNMKFKQ KQREEQAEPD GTEVADKAAY LQNLNSADLL KALCYPRVKV GNEYVTKGQT
VQQVYNAVGA LAKAVYDKMF LWMVTRINQQ LDTKQPRQYF IGVLDIAGFE IFDFNSLEQL
CINFTNEKLQ QFFNHHMFVL EQEEYKKEGI EWTFIDFGMD LAACIELIEK PMGIFSILEE
ECMFPKATDI SFKNKLYEQH LGKSNNFQKP KPAKGKPEAH FSLIHYAGTV DYNIAGWLDK
NKDPLNETVV GLYQKSAMKT LALLFAGATG AEAEAGGGKK GGKKKGSSFQ TVSALFRENL
NKLMTNLRST HPHFVRCIIP NETKTPGAME HELVLHQLRC NGVLEGIRIC RKGFPSRILY
ADFKQRYKVL NASAIPEGQF IDSKKASEKL LGSIDIDHTQ YKFGHTKVFF KAGLLGLLEE
MRDEKLAQLI TRTQAMCRGF LARVEYQKMV ERRESIFCIQ YNVRAFMNVK HWPWMKLYFK
IKPLLKSAET EKEMANMKQE FEKTKEELAK TEAKRKELEE KMVTLMQEKN DLQLQVQAEA
DSLADAEERC DQLIKTKIQL EAKIKEVTER AEDEEEINAE LTAKKRKLED ECSELKKDID
DLELTLAKVE KEKHATENKV KNLTEEMAGL DETIAKLTKE KKALQEAHQQ TLDDLQAEED
KVNTLTKAKI KLEQQVDDLE GSLEQEKKIR MDLERAKRKL EGDLKLAQES TMDIENDKQQ
LEEKLKKKEF EMSGLQSKIE DEQALGMQLQ KKIKELQARI EELEEEIEAE RASRAKAEKQ
RSDLSRELEE ISERLEEAGG ATSAQIEMNK KREAEFQKMR RDLEEATLQH EATAATLRKK
HADSVAELGE QIDNLQRVKQ KLEKEKSEMK MEIDDLASNM ETVSKAKGNL EKMCRALEDQ
LSEIKTKEEE QQRLINDLTA QRARLQTESG EYSRQLDEKD TLVSQLSRGK QAFTQQIEEL
KRQLEEEIKA KSALAHALQS SRHDCDLLRE QYEEEQEAKA ELQRAMSKAN SEVAQWRTKY
ETDAIQRTEE LEEAKKKLAQ RLQDAEEHVE AVNAKCASLE KTKQRLQNEV EDLMIDVERT
NAACAALDKK QRNFDKILAE WKQKCEETHA ELEASQKESR SLSTELFKIK NAYEESLDQL
ETLKRENKNL QQEISDLTEQ IAEGGKRIHE LEKIKKQVEQ EKSELQAALE EAEASLEHEE
GKILRIQLEL NQVKSEVDRK IAEKDEEIDQ MKRNHIRIVE SMQSTLDAEI RSRNDAIRLK
KKMEGDLNEM EIQLNHANRM AAEALRNYRN TQGILKLILD AWLRSQEDLK EQLAMVERRA
NLLQAEIEEL RATLEQTERS RKIAEQELLD ASERVQLLHT QNTSLINTKK KLETDISQIQ
GEMEDIIQEA RNAEEKAKKA ITDAAMMAEE LKKEQDTSAH LERMKKNLEQ TVKDLQHRLD
EAEQLALKGG KKQIQKLEAR VRELEGEVES EQKRNVEAVK GLRKHERKVK ELTYQTEEDR
KNILRLQDLV DKLQAKVKSY KRQAEEAEEQ SNVNLSKFRR IQHELEEAEE RADIAESQVN
KLRVKSREVH TKIISEE
//
