ID B2RWW8_MOUSE Unreviewed; 1937 AA.
AC B2RWW8;
DT 01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 01-JUL-2008, sequence version 1.
DT 22-FEB-2023, entry version 86.
DE SubName: Full=Myosin, heavy polypeptide 8, skeletal muscle, perinatal {ECO:0000313|EMBL:AAI50738.1};
GN Name=Myh8 {ECO:0000313|EMBL:AAI50738.1, ECO:0000313|MGI:MGI:1339712};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090 {ECO:0000313|EMBL:AAI50738.1};
RN [1] {ECO:0000313|EMBL:AAI50738.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain {ECO:0000313|EMBL:AAI50738.1};
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RA Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H.,
RA Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M.,
RA Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M.,
RA Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F.,
RA Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T.,
RA Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F.,
RA Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E.,
RA Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y.,
RA Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E.,
RA Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y.,
RA Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W.,
RA Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J.,
RA Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J.,
RA Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W.,
RA Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J.,
RA Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I.,
RA Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U.,
RA Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A.,
RA Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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; BC150737; AAI50738.1; -; mRNA.
DR PeptideAtlas; B2RWW8; -.
DR AGR; MGI:1339712; -.
DR MGI; MGI:1339712; Myh8.
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:SF35; MYOSIN-8; 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; 4.
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 2: Evidence at transcript level;
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}; Coiled coil {ECO:0000256|ARBA:ARBA00023054};
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}; Thick filament {ECO:0000256|ARBA:ARBA00022433}.
FT DOMAIN 35..84
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 88..781
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 658..680
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1125..1171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1125..1154
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 181..188
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1937 AA; 222695 MW; 01632E43050BE0C3 CRC64;
MSTGSDAEMA IFGEAAPYLR KSEKERIEAQ NKPFDAKTSV FVAEPKESYV KSVIQSKDGG
KVTVKTESGA TLTVKEDQVF PMNPPKYDKI EDMAMMTHLH EPGVLYNLKE RYAAWMIYTY
SGLFCVTVNP YKWLPVYNPE VVAAYRGKKR QEAPPHIFSI SDNAYQFMLT DRENQSILIT
GESGAGKTVN TKRVIQYFAT IAVTGDKKKE ESGKMQGTLE DQIISANPLL EAFGNAKTVR
NDNSSRFGKF IRIHFGTTGK LASADIETYL LEKSRVTFQL KAERSYHIFY QITSNKKPEL
IEMLLITTNP YDYAFVSQGE ITVPSIDDQE ELMATDSAID ILGFSPEEKV SIYKLTGAVM
HYGNMKFKQK QREEQAEPDG TEVADKAAYL QCLNSADLLK ALCYPRVKVG NEYVTKGQTV
QQVYNAVGAL AKAVYEKMFL WMVTRINQQL DTKQPRQYFI GVLDIAGFEI FDFNSLEQLC
INFTNEKLQQ FFNHHMFVLE QEEYKKEGIE WTFIDFGMDL AACIELIEKP LGIFSILEEE
CMFPKATDTS FKNKLYDQHL GKSNNFQKPK PAKGKAEAHF SLVHYAGTVD YNITGWLDKN
KDPLNDTVVG LYQKSAMKTL ASLFSTYASA EADGGAKKGA KKKGSSFQTV SALFRENLNK
LMTNLRSTHP HFVRCIIPNE TKTPGAMEHE LVLHQLRCNG VLEGIRICRK GFPSRILYGD
FKQRYKVLNA SAIPEGQFID SKKASEKLLG SIDIDHTQYK FGHTKVFFKA GLLGLLEEMR
DEKLAQIITR TQAVCRGYLM RVEYQKMLLR RESIFCIQYN VRAFMNVKHW PWMKLFFKIK
PLLKSAETEK EMATMKEEFQ KTKDELAKSE AKRKELEEKM VTLLKEKNDL QLQVQSEADS
LADAEERCEQ LIKNKIQLEA KIKEVTERAE DEEEINAELT AKKRKLEDEC SELKKDIDDL
ELTLAKVEKE KHATENKVKN LTEEMAGLDE TIAKLTKEKK ALQEAHQQTL DDLQAEEDKV
NTLTKAKTKL EQQVDDLEGS LEQEKKLRMD LERAKRKLEG DLKLAQESTM DIENDKQQLD
EKLKKKEFEI SNLISKIEDE QAVEIQLQKK IKELQARIEE LEEEIEAERA SRAKAEKQRS
DLSRELEEIS ERLEEAGGAT SAQVEMNKKR ETEFQKLRRD LEEATLQHEA TAAALRKKHA
DSVAELGEQI DNLQRVKQKL EKEKSELKME IDDLSSNAEA IAKAKGNLEK MCRTLEDQVS
ELKSKEEEQQ RLINELTAQR ARLQTEAGEY SRQLDEKDAL VSQLSRSKQA STQQIEELKR
QLEEETKAKN ALAHALQSSR HDCDLLREQY EEEQEGKAEL QRALSKANSE VAQWRTKYET
DAIQRTEELE EAKKKLAQRL QAAEEHVEAV NAKCASLEKT KQRLQNEVED LMIDVERTNA
ACAALDKKQR NFDKVLSEWR QKYEETQAEL ESCQKESRTL STELFKVKNA YEESLDHLET
LRRENKNLQQ EISDLTEQIA EGGKHIHELE KIKKQVEQEK CEIQAALEEA EASLEHEEGK
ILRIQLELNQ VKSEIDRKIA EKDEEIDQLK RNHIRVVESM QSTLDAEIRS RNDALRVKKK
MEGDLNEMEI QLNHANRLAA ESLRNYRNTQ GILKDTQLHL DDALRGQEDL KEQLAIVERR
ANLLQAEIEE LRATLEQTER SRKIAEQELL DASERVQLLH TQNTSLINTK KKLENDVSQL
QSEVEEVIQE SRNAEEKAKK AITDAAMMAE ELKKEQDTSA HLERMKKNME QTVKDLQHRL
DEAEQLALKG GKKQIQKLEA RVRELEGEVE NEQKRNAEAV KGLRKHERRV KELTYQTEED
RKNVLRLQDL VDKLQAKVKS YKRQAEEAEE QSNANLAKFR KLQHELEEAE ERADIAESQV
NKLRVKSREV HTKISAE
//
