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MYH16_CANLF
ID   MYH16_CANLF             Reviewed;        1930 AA.
AC   F1PT61;
DT   27-MAY-2015, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2012, sequence version 2.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=Myosin-16 {ECO:0000305};
DE   AltName: Full=Myosin heavy chain 16 {ECO:0000305};
GN   Name=MYH16 {ECO:0000250|UniProtKB:Q9H6N6};
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Boxer;
RX   PubMed=16341006; DOI=10.1038/nature04338;
RA   Lindblad-Toh K., Wade C.M., Mikkelsen T.S., Karlsson E.K., Jaffe D.B.,
RA   Kamal M., Clamp M., Chang J.L., Kulbokas E.J. III, Zody M.C., Mauceli E.,
RA   Xie X., Breen M., Wayne R.K., Ostrander E.A., Ponting C.P., Galibert F.,
RA   Smith D.R., deJong P.J., Kirkness E.F., Alvarez P., Biagi T., Brockman W.,
RA   Butler J., Chin C.-W., Cook A., Cuff J., Daly M.J., DeCaprio D., Gnerre S.,
RA   Grabherr M., Kellis M., Kleber M., Bardeleben C., Goodstadt L., Heger A.,
RA   Hitte C., Kim L., Koepfli K.-P., Parker H.G., Pollinger J.P.,
RA   Searle S.M.J., Sutter N.B., Thomas R., Webber C., Baldwin J., Abebe A.,
RA   Abouelleil A., Aftuck L., Ait-Zahra M., Aldredge T., Allen N., An P.,
RA   Anderson S., Antoine C., Arachchi H., Aslam A., Ayotte L., Bachantsang P.,
RA   Barry A., Bayul T., Benamara M., Berlin A., Bessette D., Blitshteyn B.,
RA   Bloom T., Blye J., Boguslavskiy L., Bonnet C., Boukhgalter B., Brown A.,
RA   Cahill P., Calixte N., Camarata J., Cheshatsang Y., Chu J., Citroen M.,
RA   Collymore A., Cooke P., Dawoe T., Daza R., Decktor K., DeGray S.,
RA   Dhargay N., Dooley K., Dooley K., Dorje P., Dorjee K., Dorris L.,
RA   Duffey N., Dupes A., Egbiremolen O., Elong R., Falk J., Farina A., Faro S.,
RA   Ferguson D., Ferreira P., Fisher S., FitzGerald M., Foley K., Foley C.,
RA   Franke A., Friedrich D., Gage D., Garber M., Gearin G., Giannoukos G.,
RA   Goode T., Goyette A., Graham J., Grandbois E., Gyaltsen K., Hafez N.,
RA   Hagopian D., Hagos B., Hall J., Healy C., Hegarty R., Honan T., Horn A.,
RA   Houde N., Hughes L., Hunnicutt L., Husby M., Jester B., Jones C., Kamat A.,
RA   Kanga B., Kells C., Khazanovich D., Kieu A.C., Kisner P., Kumar M.,
RA   Lance K., Landers T., Lara M., Lee W., Leger J.-P., Lennon N., Leuper L.,
RA   LeVine S., Liu J., Liu X., Lokyitsang Y., Lokyitsang T., Lui A.,
RA   Macdonald J., Major J., Marabella R., Maru K., Matthews C., McDonough S.,
RA   Mehta T., Meldrim J., Melnikov A., Meneus L., Mihalev A., Mihova T.,
RA   Miller K., Mittelman R., Mlenga V., Mulrain L., Munson G., Navidi A.,
RA   Naylor J., Nguyen T., Nguyen N., Nguyen C., Nguyen T., Nicol R., Norbu N.,
RA   Norbu C., Novod N., Nyima T., Olandt P., O'Neill B., O'Neill K., Osman S.,
RA   Oyono L., Patti C., Perrin D., Phunkhang P., Pierre F., Priest M.,
RA   Rachupka A., Raghuraman S., Rameau R., Ray V., Raymond C., Rege F.,
RA   Rise C., Rogers J., Rogov P., Sahalie J., Settipalli S., Sharpe T.,
RA   Shea T., Sheehan M., Sherpa N., Shi J., Shih D., Sloan J., Smith C.,
RA   Sparrow T., Stalker J., Stange-Thomann N., Stavropoulos S., Stone C.,
RA   Stone S., Sykes S., Tchuinga P., Tenzing P., Tesfaye S., Thoulutsang D.,
RA   Thoulutsang Y., Topham K., Topping I., Tsamla T., Vassiliev H.,
RA   Venkataraman V., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J.,
RA   Wilson A., Yadav S., Yang S., Yang X., Young G., Yu Q., Zainoun J.,
RA   Zembek L., Zimmer A., Lander E.S.;
RT   "Genome sequence, comparative analysis and haplotype structure of the
RT   domestic dog.";
RL   Nature 438:803-819(2005).
RN   [2]
RP   FUNCTION.
RX   PubMed=15042088; DOI=10.1038/nature02358;
RA   Stedman H.H., Kozyak B.W., Nelson A., Thesier D.M., Su L.T., Low D.W.,
RA   Bridges C.R., Shrager J.B., Minugh-Purvis N., Mitchell M.A.;
RT   "Myosin gene mutation correlates with anatomical changes in the human
RT   lineage.";
RL   Nature 428:415-418(2004).
CC   -!- FUNCTION: May play a role in masticatory muscles contraction.
CC       {ECO:0000303|PubMed:15042088}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril. Note=Thick filaments of the
CC       myofibrils. {ECO:0000305}.
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. {ECO:0000305}.
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}.
CC   -!- CAUTION: Represents a conventional myosin. This protein should not be
CC       confused with the unconventional myosin-XVI (MYO16). {ECO:0000305}.
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DR   EMBL; AAEX03004277; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAEX03004278; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; F1PT61; -.
DR   SMR; F1PT61; -.
DR   STRING; 9615.ENSCAFP00000022286; -.
DR   PaxDb; F1PT61; -.
DR   PRIDE; F1PT61; -.
DR   eggNOG; KOG0161; Eukaryota.
DR   HOGENOM; CLU_000192_4_0_1; -.
DR   InParanoid; F1PT61; -.
DR   OMA; RQRYTNM; -.
DR   TreeFam; TF314375; -.
DR   Proteomes; UP000002254; Unplaced.
DR   GO; GO:0030016; C:myofibril; IEA:UniProtKB-SubCell.
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-KW.
DR   GO; GO:0000146; F:microfilament motor activity; IBA:GO_Central.
DR   Gene3D; 1.20.5.370; -; 4.
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   InterPro; IPR014751; XRCC4-like_C.
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; SSF52540; SSF52540; 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; ATP-binding; Coiled coil; Cytoplasm; Motor protein; Myosin;
KW   Nucleotide-binding; Reference proteome.
FT   CHAIN           1..1930
FT                   /note="Myosin-16"
FT                   /id="PRO_0000433094"
FT   DOMAIN          35..84
FT                   /note="Myosin N-terminal SH3-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01190"
FT   DOMAIN          88..774
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT   DOMAIN          777..806
FT                   /note="IQ"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT   REGION          652..674
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000250|UniProtKB:P12883"
FT   REGION          753..767
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000250|UniProtKB:P12883"
FT   REGION          1116..1137
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          835..1921
FT                   /evidence="ECO:0000255"
FT   BINDING         181..188
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P12883"
SQ   SEQUENCE   1930 AA;  222640 MW;  77984CD38EA22212 CRC64;
     MPGGYKGECG DDVDPMPFLA PPEKERIEAM NKPYDIKKSC WVKDEKEGFI AGEIQSEQGD
     QVTVKTVNNQ TVTVKKDDVQ QMNPPKFYQA SDMADMTFLN EASVLNNLRQ RYTNMRIYTY
     SGLFCVTVNP YKWLPIYGAR VANMYKGKKR TEMPPHLFSI SDNAYHDMLM NRENQSMLIT
     GESGAGKTEN TKKVIQYFAN VGGTGKQSSD GKGQGSLEDQ IIQANPVLEA FGNAKTIRNN
     NSSRFGKFIR IHFGTTGKLA GADIESYLLE KSRVISQQAA ERGYHIFYQI LSNKKPELIE
     SLLLVPNPKE YHWVSQGVTV VENMDDGEEL QITDVAFDVL GFSAEEKIGI YKLTGGIMHF
     GNMKFKQKPR EEQAEVDTTE VADKVSHLMG LNSGELQKGI TRPRVKVGNE FVQKGQNVEQ
     CNNSIGALGK AIYDKMFKWL VVRINKTLDT KMQRQFFIGV LDIAGFEIFE FNSFEQLCIN
     FTNEKLQQFF NHHMFVLEQE EYKREGIEWV FIDFGLDLQA CIDLLEKPMG IFSILEEQCV
     FPKATDATFK AALYDNHLGK SNNFLKPKGG KGKGPEAHFE LVHYAGTVAY NITGWLEKNK
     DPLNETVVGL FQKSSLGLLA LLFKEEEAPA GSKKQKRGSS FMTVSNFYRE QLNKLMATLH
     STAPHFVRCI VPNEFKQSGV VDAHLIMHQL ACNGVLEGIR ICRKGFPNRM QYPEFKQRYQ
     VLNPNVIPQG FVDNKKASEL LLGSIDLDVN EYKIGHTKVF FRAGILAKLE DMRDERLAKI
     MTMLQCRLRG FLMRIEFKKM LERRIGLKVI QRNTRKFLEL RFWGWWKLYN KVKPLLNVAR
     QEEEMKAKEE ELRNAMSKTQ ELLSRVKELE EKMATLSQEK NDLTIQLQAE QENVIDAEER
     LTQMMKTKMD LESQISDMRE RLEEEEGTAA SLSATKRKLE GEMSDLKRDL EGLETTLAKT
     EKEKQALDHR VRTLTGDLSL REDSIAKLQK EKRALEELHQ KTLDDLQAEE DKVNHLTKTN
     SKLSTQIHEL EDNWEQEKKI RAEVEKARRK AESDLKMTID NLNDMERSKL DLEEVVKKRD
     MEINSVNSKY EDEQSLNSTL QRKLKEHQAR IEELEEELEA ERSMRAKVEK QRSDLSRDLE
     DLSDRLEEAG GATSAQIEQN RKREAELLKL RRELEEAALQ SEAAASTLRK KHTDSMAELT
     EHVENLQRVK SKLEKDKQVM KAEIDDLNAS METVQKSKMN AEAHIRKLED SLSEANAKVA
     ELERNQAEIN AVRTRLQAEN GELSREYEES QSRLNQILRI KTSLTSQVDD YKRQLDEESK
     SRSAAMVSLA NTKHDLDLVK EQLEEEQGGK SELQRLVSKL NTEVTTWRTK YETDAIQRTE
     ELEETKRKLA ARLQEAEETA EAAQARAASL EKNKQRLQAE VEDLTIDLEK ANAAAAALDK
     KQRVFDKMLA EWQQKCEELQ VEVDSSQKEC RMYMTESFKI KTAYEESLEH LESVKKENKT
     LQEEIKELID QLGEGGRSVH ELQKLKKKLE IEKEELQVAL EEAESSLEVE ESKVIRIQLE
     LAQVKADIDR RIHEKEEEFE ATRKNHQRAI ESLQASLEAE AKGRAEALRL KKKMETDLNE
     MEIQLDHANK NNSELVKTLK RLQQQIKDLQ VQMDEDARQH EELREQYNLQ ERRLSLLQTE
     LEEVRSGLEG SERSRKLLEQ EVVEITERHN EVNIQNQSLL VVKRKLESDV QRISSEHEEL
     ISEFRSADER AKKAMTDAAR MAEELRQEQD HCMHLEKIKK NYEITIKDLQ AKMEEAEQLA
     LKGGKRTIMK LEARIKELET ELDGEQKQHV ETVKTLRKNE RRLKELVFQT EEDHKTNQRM
     QELVEKLQNK LKVYKRQIEE AEEQANQTLA RYRKTVHELD DAEERAGMAE TALNKLRTRH
     RVAGKGITSV
 
 
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