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