UniProt: G3QGY2

Database: UniProt
Entry: G3QGY2_GORGO

LinkDB:  G3QGY2_GORGO 
Original site:  G3QGY2_GORGO

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Ontology (11)   
   GO (11)   
Gene (3)   
   ENSEMBL-UP (3)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (16)   
   InterPro (8)   
   Pfam (3)   
   PROSITE (3)   
   SMART (2)   
Literature (1)   
   PubMed (1)   
All databases (32)   

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ID   G3QGY2_GORGO            Unreviewed;      1940 AA.
AC   G3QGY2;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 2.
DT   27-MAR-2024, entry version 65.
DE   SubName: Full=Myosin heavy chain 1 {ECO:0000313|Ensembl:ENSGGOP00000001597.3};
OS   Gorilla gorilla gorilla (Western lowland gorilla).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Gorilla.
OX   NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000001597.3, ECO:0000313|Proteomes:UP000001519};
RN   [1] {ECO:0000313|Ensembl:ENSGGOP00000001597.3, ECO:0000313|Proteomes:UP000001519}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Scally A.;
RT   "Insights into the evolution of the great apes provided by the gorilla
RT   genome.";
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSGGOP00000001597.3, ECO:0000313|Proteomes:UP000001519}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=22398555; DOI=10.1038/nature10842;
RA   Scally A., Dutheil J.Y., Hillier L.W., Jordan G.E., Goodhead I.,
RA   Herrero J., Hobolth A., Lappalainen T., Mailund T., Marques-Bonet T.,
RA   McCarthy S., Montgomery S.H., Schwalie P.C., Tang Y.A., Ward M.C., Xue Y.,
RA   Yngvadottir B., Alkan C., Andersen L.N., Ayub Q., Ball E.V., Beal K.,
RA   Bradley B.J., Chen Y., Clee C.M., Fitzgerald S., Graves T.A., Gu Y.,
RA   Heath P., Heger A., Karakoc E., Kolb-Kokocinski A., Laird G.K., Lunter G.,
RA   Meader S., Mort M., Mullikin J.C., Munch K., O'Connor T.D., Phillips A.D.,
RA   Prado-Martinez J., Rogers A.S., Sajjadian S., Schmidt D., Shaw K.,
RA   Simpson J.T., Stenson P.D., Turner D.J., Vigilant L., Vilella A.J.,
RA   Whitener W., Zhu B., Cooper D.N., de Jong P., Dermitzakis E.T.,
RA   Eichler E.E., Flicek P., Goldman N., Mundy N.I., Ning Z., Odom D.T.,
RA   Ponting C.P., Quail M.A., Ryder O.A., Searle S.M., Warren W.C.,
RA   Wilson R.K., Schierup M.H., Rogers J., Tyler-Smith C., Durbin R.;
RT   "Insights into hominid evolution from the gorilla genome sequence.";
RL   Nature 483:169-175(2012).
RN   [3] {ECO:0000313|Ensembl:ENSGGOP00000001597.3}
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; CABD030103660; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   STRING; 9593.ENSGGOP00000001597; -.
DR   Ensembl; ENSGGOT00000001632.3; ENSGGOP00000001597.3; ENSGGOG00000036891.1.
DR   GeneTree; ENSGT00940000154760; -.
DR   HOGENOM; CLU_000192_8_0_1; -.
DR   InParanoid; G3QGY2; -.
DR   OMA; CERMAKQ; -.
DR   Proteomes; UP000001519; Chromosome 17.
DR   Bgee; ENSGGOG00000036891; Expressed in multicellular organism and 1 other cell type or tissue.
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; 4.
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};
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:UP000001519};
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   COILED          847..1928
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   BINDING         180..187
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   1940 AA;  223227 MW;  8192DC0F8B2105A4 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
     ECMFPKATDT SFKNKLYEQH LGKSNNFQKP KPAKGKPEAH FSLIHYAGTV DYNIAGWLDK
     NKDPLNETVV GLYQKSAMKT LALLFVGATG AEAEAGGGKK GGKKKGSSFQ TVSALFRENL
     NKLMTNLRST HPHFVRCIIP NETKTPGAME HELVLHQLRC NGVLEGIRIC RKGFPSRILY
     ADFKQRYKVL NASAIPEGQF IDSKKASEKL LGSIDIDHTQ YKFGHTKVFF KAGLLGLLEE
     MRDEKLAQLI TRTQAMCRGF LARVEYQKMV ERRESIFCIQ YNVRAFMNVK HWPWMKLYFK
     IKPLLKSAET EKEMANMKEE FEKTKEELAK TEAKRKELEE KMVTLMQEKN DLQLQVQAEA
     DSLADAEERC DQLIKTKIQL EAKIKEVTER AEDEEEINAE LTAKKRKLED ECSELKKDID
     DLELTLAKVE KEKHATENKV KNLTEEMAGL DETIAKLTKE KKALQEAHQQ TLDDLQAEED
     KVNTLTKAKI KLEQQVDDLE GSLEQEKKIR MDLERAKRKL EGDLKLAQES TMDIENDKQQ
     LDEKLKKKEF EMSGLQSKIE DEQALGMQLQ KKIKELQARI EELEEEIEAE RASRAKAEKQ
     RSDLSRELEE ISERLEEAGG ATSAQIEMNK KREAEFQKMR RDLEEATLQH EATAATLRKK
     HADSVAELGE QIDNLQRVKQ KLEKEKSEMK MEIDDLASNM ETVSKAKGNL EKMCRTLEDQ
     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 TQAILKDTQL HLDDALRSQE DLKEQLAMVE
     RRANLLQAEI EELRATLEQT ERSRKIAEQE LLDASERVQL LHTQNTSLIN TKKKLETDIS
     QIQGEMEDII QEARNAEEKA KKAITDAAMM AEELKKEQDT SAHLERMKKN LEQTVKDLQH
     RLDEAEQLAL KGGKKQIQKL EARVRELEGE VESEQKHNVE AVKGLRKHER KVKELTYQTE
     EDRKNILRLQ DLVDKLQAKV KSYKRQAEEA EEQSNVNLSK FRRIQHELEE AEERADIAES
     QVNKLRVKSR EVHTKIISEE
//

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