ID G3PQ56_GASAC Unreviewed; 1952 AA.
AC G3PQ56;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=Myosin-11 {ECO:0000256|ARBA:ARBA00040393};
DE AltName: Full=Myosin heavy chain 11 {ECO:0000256|ARBA:ARBA00042406};
OS Gasterosteus aculeatus (Three-spined stickleback).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae;
OC Gasterosteus.
OX NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000019741.1, ECO:0000313|Proteomes:UP000007635};
RN [1] {ECO:0000313|Ensembl:ENSGACP00000019741.1, ECO:0000313|Proteomes:UP000007635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGACP00000019741.1}
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 STRING; 69293.ENSGACP00000019741; -.
DR Ensembl; ENSGACT00000019779.1; ENSGACP00000019741.1; ENSGACG00000014959.1.
DR eggNOG; KOG0161; Eukaryota.
DR GeneTree; ENSGT00940000155421; -.
DR InParanoid; G3PQ56; -.
DR OMA; NCACYLR; -.
DR TreeFam; TF333601; -.
DR Proteomes; UP000007635; Unassembled WGS sequence.
DR Bgee; ENSGACG00000014959; Expressed in pharyngeal gill and 2 other cell types or tissues.
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 GO; GO:0048731; P:system development; IEA:UniProt.
DR CDD; cd01377; MYSc_class_II; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.5.340; -; 5.
DR Gene3D; 1.20.5.4820; -; 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 PANTHER; PTHR45615; MYOSIN HEAVY CHAIN, NON-MUSCLE; 1.
DR PANTHER; PTHR45615:SF23; MYOSIN-11; 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 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};
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:UP000007635}.
FT DOMAIN 30..80
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 84..779
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 657..679
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1601..1684
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1699..1724
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1745..1809
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1831..1892
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1905..1952
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 846..1280
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1699..1716
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1754..1785
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1786..1805
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 1952 AA; 223318 MW; 5B2F6F19FA5E1DA2 CRC64;
AMADPAPDDS KFLFLDNDFR NSGVAQADWS AKKMVWVASE KEGFEAASVK EEKGDEVTLV
ELSNGQKVTV NKDDIQKMNP PKFSKVEDMA ALTFLNEASV LQNLRERYFS KHQLVQTYSG
LFCVVVNPYK MLPIYSEKII EMYKGKKRHE VPPHIYSITD NAYRNMMQDR EDQSILCTGE
SGAGKTENTK KVIQYLAVVA SSHKGKKDNP GELEKQLLQA NPILEAFGNA KTIKNDNSSR
FGKFIKLNFD VTGYLVGANI DTYLLEKSRC IRQGNTERAF HIFYYMVAGA KDKLKEELLL
EDFSSYRFLV AGHVEISGQE DDEMFIETLE AMEIMGFTEE ERIGMMKVVS TVLQLGNVKF
EKERNSEQAT MPDNTAAQKV CHLQGINVTD FTRAILTPRI KVGREVVQKA QTKQQADFAV
EALAKAMYER LFRWILARVN KTLDKSKRQS CSFLGILDIA GFEIFEVRPP HPCTPCVSSP
ARHSLTHTMF ILEQEEYKRE GIEWNFIDFG LDLLPCIELI ERPNNPPGIL ALLDEECWFP
KATDVSFVDK LLNTHTGHVK FSKPKQHKDK LMFTVMHYAG KVDYNAASWL TKNMDPLNDN
VTALLNTSSS NFIQDLWKDA DRVVGLETMT KMSESSAPTK SKKGMFRTVG QLYKESLGKL
MTTLHNTQPN FVRCIIPNHE KRAGKMDSNL VLEQLRCNGV LEGIRICRQG FPNRIVFQEF
RQRYEILAAH AIPKGFMDGK QACCLMVKHL DLDTNLYRIG QSKMFFRTGV LAQLEEERDL
KLTVVIIAFQ AQARGFLARK AFSKRQQQLT AMKVIQRNCA CYLKLKNWQW WRLFSSGVQV
KPLLQVTRQE EEMGQKDEEL KAAKEVAVKT EADLKEITQK HTQLMEERVQ LETKLQAETE
LYAEAEEMRV RLEAKKQELE EVLHEMEARL EEEEDRSHAL HQEKKEMEQQ LQLMEAHIAE
EEDARQQLQL EKVAVEGKVK KLEEDVLVME DQNNKLQKER KLLEERMADM SSNLAEEEEK
SKNLNKLKTK HESMISDLEV RMKKEEKGRQ DMEKAKRKVE AELADLQDQN ADLQAQLAEL
RAQLAAKEEE LQATLARLEE ECNQRAAAVK RVRELEALLS ELQEDLEAER ATRGKVEAAR
RDLGEELNAL RSELEDSLDT TAAQQELRAK REQEVAALKK TMDDEGRSHE AQIQDLRQKH
SQVVDSLTFR IRSSVQVRAG LEKAKQALEK ESADLGADLR SLANGKQDVE HKKKKLEGQL
NDLHSRFNES ERQKTELAER VSKMSMELDS MTSVLNDAEG KNIKLSKDVS GLSSQLQDAQ
ELLSEETRQK LNLSGRLRQM EEDRNALMEQ LEEETEAKRA VERQASSLNM QLSDCKKKLE
ESCGAAEMLE EGKKRLQREL EVANSEYEEK ASAYDKLEKS RSRMQQELED VLMDLDSQRQ
LVSNLEKKQK KFDQMLAEER AVSCKFAEER DRAEAEAREK ETRALALARA LEENQDALEE
AEKMVKALRG EMEDLISSKD DVGKSVHDLD KAKRGLEAMV DEMRTQMEEL EDELQVAEDA
KLRLEVNTQA LRAQHERELH ARDEMGEEKR KQLLKQVREL EAELEEERKQ RSQTAGSKKK
LEGEMKDLED QLEATSRGRD EAVKQLRKIQ GQVKDLQRDL EDSRAAQKEV LSTARESERR
TKAVEADVVQ LHEMLAAAER ARKQAEAERD ELSEELASNS GKSLLLDEKR RLDAKISQLE
EELEEEQANV ESLNERLRKS QQQVDQIGAE LAAERSTSQS REGSRQQLER QNRELKAKLQ
EVEGQGRSKL KASIAALELK LREVEEQLEI ESRERQANAK NLRQKEKKLK DLSIQMEDER
KQAQQYKDQA EKGNARVKQL KHQLEEAEEE AQRVAAARRK LQRELDEAAE ANDALSRDVA
SMRSKLRRGG GGEAAFSSPG PRSSGGGAVR SL
//
