ID A0A2R9C3E4_PANPA Unreviewed; 1896 AA.
AC A0A2R9C3E4;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Myosin-2 {ECO:0000256|ARBA:ARBA00039812};
DE AltName: Full=Myosin heavy chain 2 {ECO:0000256|ARBA:ARBA00041436};
DE AltName: Full=Myosin heavy chain 2a {ECO:0000256|ARBA:ARBA00042414};
DE AltName: Full=Myosin heavy chain, skeletal muscle, adult 2 {ECO:0000256|ARBA:ARBA00041387};
GN Name=MYH2 {ECO:0000313|Ensembl:ENSPPAP00000035350.1};
OS Pan paniscus (Pygmy chimpanzee) (Bonobo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9597 {ECO:0000313|Ensembl:ENSPPAP00000035350.1, ECO:0000313|Proteomes:UP000240080};
RN [1] {ECO:0000313|Ensembl:ENSPPAP00000035350.1, ECO:0000313|Proteomes:UP000240080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22722832; DOI=10.1038/nature11128;
RA Prufer K., Munch K., Hellmann I., Akagi K., Miller J.R., Walenz B.,
RA Koren S., Sutton G., Kodira C., Winer R., Knight J.R., Mullikin J.C.,
RA Meader S.J., Ponting C.P., Lunter G., Higashino S., Hobolth A., Dutheil J.,
RA Karakoc E., Alkan C., Sajjadian S., Catacchio C.R., Ventura M.,
RA Marques-Bonet T., Eichler E.E., Andre C., Atencia R., Mugisha L.,
RA Junhold J., Patterson N., Siebauer M., Good J.M., Fischer A., Ptak S.E.,
RA Lachmann M., Symer D.E., Mailund T., Schierup M.H., Andres A.M., Kelso J.,
RA Paabo S.;
RT "The bonobo genome compared with the chimpanzee and human genomes.";
RL Nature 486:527-531(2012).
RN [2] {ECO:0000313|Ensembl:ENSPPAP00000035350.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Muscle contraction. Required for cytoskeleton organization.
CC {ECO:0000256|ARBA:ARBA00037212}.
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:0000256|ARBA:ARBA00038665}.
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; AJFE02061868; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR Ensembl; ENSPPAT00000058238.1; ENSPPAP00000035350.1; ENSPPAG00000040402.1.
DR GeneTree; ENSGT00940000161336; -.
DR Proteomes; UP000240080; Chromosome 17.
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 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:SF39; MYOSIN-2; 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:UP000240080};
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..762
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 639..661
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT COILED 826..1884
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 1896 AA; 217826 MW; 042E021CC1B17F63 CRC64;
AMSSDSELAV FGEAAPFLRK SERERIEAQN RPFDAKTSVF VAEPKESFVK GTIQSREGGK
VTVKTEGGAT LTVKDDQVFP MNPPKYDKIE DMAMMTHLHE PAVLYNLKER YAAWMIYTYS
GLFCVTVNPY KWLPVYKPEV VTAYRGKKRQ EAPPHIFSIS DNAYQFMLTD RENQSILITG
ESGAGKTVNT KRVIQYFATI AVTGEKKKEE ITSGKIQGTL EDQIISANPL LEAFGNAKTV
RNDNSSRFGK FIRIHFGTTG KLASADIETY LLEKSRVVFQ LKAERSYHIF YQITSNKKPE
LIEMLLITTN PYDYPFVSQG EISVASIDDQ EELMATDSAI DILGFTNEEK VSIYKLTGAV
MHYGNLKFKQ KQREEQAEPD GTEVADKAAY LQSLNSADLL KALCYPRVKV GNEYVTKGQT
VEQVTNAVGA LAKAVYEKMF LWMVARINQQ LDTKQPRQYF IGVLDIAGFE IFDFNSLEQL
CINFTNEKLQ QFFNHHMFVL EQEEYKKEGI EWTFIDFGMD LAACIELIEK VGFRSACSLR
QQTPPSRTSC MTSTWAHFSL IHYAGVVDYN ITGWLEKNKD PLNETVVGLY QKSAMKTLAH
LFSGTQTAEG EGAGGGAKKG GKKKGSSFQT VSALFRENLN KLMTNLRSTH PHFVRCIIPN
ETKTPGAMEH ELVLHQLRCN GVLEGIRICR KGFPSRILYA DFKQRYKVLN ASAIPEGQFI
DSKKASEKLL ASIDIDHTQY KFGHTKVFFK AGLLGLLEEM RDDKLAQLIT RTQARCRGFL
ARVEYQRMVE RREAIFCIQY NIRSFMNVKH WPWMKLFFKI KPLLKSAETE KEMATMKEEF
QKIKDELAKS EAKRKELEEK MVTLLKEKND LQLQVQAEAE GLADAEERCD QLIKTKIQLE
AKIKEVTERA EDEEEINAEL TAKKRKLEDE CSELKKDIDD LELTLAKVEK EKHATENKVK
NLTEEMAGLD ETIAKLTKEK KALQEAHQQT LDDLQAEEDK VNTLTKAKIK LEQQVDDLEG
SLEQEKKLRM DLERAKRKLE GDLKLAQESI MDIENEKQQL DEKLKKKEFE ISNLQSKIED
EQALGIQLQK KIKELQARIE ELEEEIEAER ASRAKAEKQR SDLSRELEEI SERLEEAGGA
TSAQIEMNKK REAEFQKMRR DLEEATLQHE ATAATLRKKH ADSVAELGEQ IDNLNVETVS
KAKGNLEKMC RTLEDQLSEL KSKEEEQQRL INDLTAQRGR LQTESGEFSR QLDEKEALVT
QLSRGKQAFT QQIEELKRQL EEEIKAKNAL AHALQSSRHD CDLLREQYEE EQESKAELQR
ALSKANTEVA QWRTKYETDA IQRTEELEEA KKKLAQRLQA AEEHVEAVNA KCASLEKTKQ
RLQNEVEDLM LDVERTNAAC AALDKKQRNF DKILAEWKQK CEETHAELEA SQKEARSLGT
ELFKIKNAYE ESLDQLETLK RENKNLQQEI SDLTEQIAEG GKRIHELEKI KKQVEQEKCE
LQAALEEAEA SLEHEEGKIL RIQLELNQVK SEVDRKIAEK DEEIDQMKRN HIRIVESMQS
TLDAEIRSRN DAIRLKKKME GDLNEMEIQL NHANRMAAEA LRNYRNTQGI LKDTQIHLDD
ALRSQEDLKE QLAMVERRAN LLQAEIEELR ATLEQTERSR KIAEQELLDA SERVQLLHTQ
NTSLINTKKK LETDISQMQG EMEDILQEAR NAEEKAKKAI TDAAMMAEEL KKEQDTSAHL
ERMKKNMEQT VKDLQLRLDE AEQLALKGGK KQIQKLEARV RELEGEVESE QKRNAEAVKG
LRKHERRVKE LTYQTEEDRK NILRLQDLVD KLQAKVKSYK RQAEEAEEQS NTNLAKFRKL
QHELEEAEER ADIAESQVNK LRVKSREVHT KVISEE
//
