ID   MYH11_RABIT             Reviewed;        1972 AA.
AC   P35748;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   03-AUG-2022, entry version 133.
DE   RecName: Full=Myosin-11;
DE   AltName: Full=Myosin heavy chain 11;
DE   AltName: Full=Myosin heavy chain, smooth muscle isoform;
DE   AltName: Full=SMMHC;
GN   Name=MYH11;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1961735; DOI=10.1073/pnas.88.23.10676;
RA   Babij P., Kelly C., Periasamy M.;
RT   "Characterization of a mammalian smooth muscle myosin heavy-chain gene:
RT   complete nucleotide and protein coding sequence and analysis of the 5' end
RT   of the gene.";
RL   Proc. Natl. Acad. Sci. U.S.A. 88:10676-10680(1991).
CC   -!- FUNCTION: Muscle contraction.
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   -!- SUBCELLULAR LOCATION: Melanosome {ECO:0000250}. Cytoplasm, myofibril.
CC       Note=Thick filaments of the myofibrils.
CC   -!- DOMAIN: The rodlike tail sequence is highly repetitive, showing cycles
CC       of a 28-residue repeat pattern composed of 4 heptapeptides,
CC       characteristic for alpha-helical coiled coils.
CC   -!- DOMAIN: Limited proteolysis of myosin heavy chain produces 1 light
CC       meromyosin (LMM) and 1 heavy meromyosin (HMM). HMM can be further
CC       cleaved into 2 globular subfragments (S1) and 1 rod-shaped subfragment
CC       (S2). {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Myosin family. {ECO:0000305}.
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DR   EMBL; M77812; AAA31395.1; -; mRNA.
DR   RefSeq; NP_001075777.1; NM_001082308.1.
DR   AlphaFoldDB; P35748; -.
DR   SMR; P35748; -.
DR   IntAct; P35748; 1.
DR   STRING; 9986.ENSOCUP00000024188; -.
DR   PRIDE; P35748; -.
DR   GeneID; 100009145; -.
DR   KEGG; ocu:100009145; -.
DR   CTD; 4629; -.
DR   eggNOG; KOG0161; Eukaryota.
DR   InParanoid; P35748; -.
DR   OrthoDB; 47111at2759; -.
DR   Proteomes; UP000001811; Unplaced.
DR   GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005859; C:muscle myosin complex; IMP:CAFA.
DR   GO; GO:0030016; C:myofibril; IEA:UniProtKB-SubCell.
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-KW.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0000146; F:microfilament motor activity; IMP:CAFA.
DR   GO; GO:0045159; F:myosin II binding; IPI:CAFA.
DR   GO; GO:0008307; F:structural constituent of muscle; IMP:CAFA.
DR   GO; GO:0055013; P:cardiac muscle cell development; ISS:UniProtKB.
DR   GO; GO:0048251; P:elastic fiber assembly; ISS:UniProtKB.
DR   GO; GO:0030239; P:myofibril assembly; IMP:CAFA.
DR   GO; GO:0030241; P:skeletal muscle myosin thick filament assembly; IDA:UniProtKB.
DR   GO; GO:0006939; P:smooth muscle contraction; IDA:UniProtKB.
DR   Gene3D; 2.30.30.360; -; 1.
DR   Gene3D; 3.40.850.10; -; 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   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; SSF52540; SSF52540; 1.
DR   PROSITE; PS50096; IQ; 1.
DR   PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR   PROSITE; PS51844; SH3_LIKE; 1.
PE   2: Evidence at transcript level;
KW   Actin-binding; ATP-binding; Calmodulin-binding; Coiled coil; Cytoplasm;
KW   Methylation; Motor protein; Muscle protein; Myosin; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome; Thick filament.
FT   CHAIN           1..1972
FT                   /note="Myosin-11"
FT                   /id="PRO_0000123427"
FT   DOMAIN          31..81
FT                   /note="Myosin N-terminal SH3-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01190"
FT   DOMAIN          85..783
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT   DOMAIN          785..807
FT                   /note="IQ"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT   REGION          661..683
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000250"
FT   REGION          763..777
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000250"
FT   REGION          1744..1802
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1866..1972
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1935..1972
FT                   /note="C-terminal"
FT   COILED          844..1934
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1761..1787
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1788..1802
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1866..1915
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1945..1972
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         178..185
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         8
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P35749"
FT   MOD_RES         23
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P35749"
FT   MOD_RES         40
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z406"
FT   MOD_RES         129
FT                   /note="N6,N6,N6-trimethyllysine"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         1177
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z406"
FT   MOD_RES         1684
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q63862"
FT   MOD_RES         1722
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q63862"
FT   MOD_RES         1954
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P35749"
FT   MOD_RES         1971
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O08638"
SQ   SEQUENCE   1972 AA;  227319 MW;  2061A224288D6A4C CRC64;
     MAQKGQLSDD EKFLFVDKNF INSPVAQADW VAKRLVWVPS EKQGFEAASI KEEKGDEVVV
     ELVENGKKVT VGKDDIQKMN PPKFSKVEDM AELTCLNEAS VLHNLRERYF SGLIYTYSGL
     FCVVVNPYKQ LPIYSEKIVD MYKGKKRHEM PPHIYAIADT AYRSMLQDRE DQSILCTGES
     GAGKTENTKK VIQYLAVVAS SHKGKKDTSI TGELEKQLLQ ANPILEAFGN AKTVKNDNSS
     RFGKFIRINF DVTGYIVGAN IETYLLEKSR AIRQAREERT FHIFYYLIAG AKEKMRNDLL
     LEGFNNYTFL SNGFVPIPAA QDDEMFQETV EAMSIMGFSE EEQLSVLKVV SSVLQLGNIV
     FKKERNTDQA SMPDNTAAQK VCHLMGINVT DFTRSILTPR IKVGRDVVQK AQTKEQADFA
     VEALAKATYE RLFRWILSRV NKALDKTHRQ GASFLGILDI AGFEIFEVNS FEQLCINYTN
     EKLQQLFNHT MFILEQEEYQ REGIEWNFID FGLDLQPCIE LIERPNNPPG VLALLDEECW
     FPKATDKSFV EKLCTEQGNH PKFQKPKQLK DKTEFSIIHY AGKVDYNASA WLTKNMDPLN
     DNVTSLLNAS SDKFVADLWK DVDRIVGLDQ MAKMTESSLP SASKTKKGMF RTVGQLYKEQ
     LGKLMTTLRN TTPNFVRCII PNHEKRSGKL DAFLVLEQLR CNGVLEGIRI CRQGFPNRIV
     FQEFRQRYEI LAANAIPKGF MDGKQACILM IKALELDPNL YRIGQSKIFF RTGVLAHLEE
     ERDLKITDVI MAFQAMCRGY LARKAFAKRQ QQLTAMKVIQ RNCAAYLKLR NWQWWRLFTK
     VKPLLQVTRQ EEEMQAKEDE LQKIKERQQK AESELQELQQ KHTQLSEEKN LLQEQLQAET
     ELYAEAEEMR VRLAAKKQEL EEILHEMEAR LEEEEDRGQQ LQAERKKMAQ QMLDLEEQLE
     EEEAARQKLQ LEKVTAEAKI KKLEDDILVM DDQNNKLSKE RKLLEERISD LTTNLAEEEE
     KAKNLTKLKN KHESMISELE VRLKKEEKSR QELEKLKRKM DGEASDLHEQ IADLQAQIAE
     LKMQLAKKEE ELQAALARLE DETSQKNNAL KKIRELEGHI SDLQEDLDSE RAARNKAEKQ
     KRDLGEELEA LKTELEDTLD TTATQQELRA KREQEVTVLK KALDEETRSH EAQVQEMRQK
     HTQVVEELTE QLEQFKRAKA NLDKTKQTLE KENADLAGEL RVLGQAKQEV EHKKKKLEVQ
     LQELQSKCSD GERARAELND KVHKLQNEVE SVTGMLSEAE GKAIKLAKEV ASLGSQLQDT
     QELLQEETRQ KLNVSTKLRQ LEDERNSLQE QLDEEMEAKQ NLERHISTLN IQLSDSKKKL
     QDFASTVESL EEGKKRFQKE IESLTQQYEE KAAAYDKLEK TKNRLQQELD DLVVDLDNQR
     QLVSNLEKKQ KKFDQLLAEE KNISSKYADE RDRAEAEARE KETKALSLAR ALEEALEAKE
     ELERTNKMLK AEMEDLVSSK DDVGKNVHEL EKSKRALETQ MEEMKTQLEE LEDELQATED
     AKLRLEVNMQ ALKVQFERDL QARDEQNEEK RRQLQRQLHE YETELEDERK QRALAAAAKK
     KLEGDLKDLE LQADSAIKGR EEAIKQLLKL QAQMKDFQRE LEDARASRDE IFATAKENEK
     KAKSLEADLM QLQEDLAAAE RARKQADLEK EELAEELASS LSGRNALQDE KRRLEARIAQ
     LEEELEEEQG NMEAMSDRVR KATQQAEQLS NELATERSTA QKNESARQQL ERQNKELKSK
     LQEMEGAVKS KFKSTIAALE AKIAQLEEQV EQEAREKQAA AKALKQRDKK LKEMLLQVED
     ERKMAEQYKE QAEKGNAKVK QLKRQLEEAE EESQRINANR RKLQRELDEA TESNEAMGRE
     VNALKSKLRR GNETSFVPTR RSGGRRVIEN ADGSEEEVDA RDADFNGTKS SE