MYH1B_CHICK
ID MYH1B_CHICK Reviewed; 1940 AA.
AC P02565;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 3.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Myosin-1B;
DE AltName: Full=Myosin heavy chain 1B, skeletal muscle;
DE AltName: Full=Myosin heavy chain 3;
DE Short=Myosin-3;
DE AltName: Full=Myosin heavy chain, fast skeletal muscle, embryonic;
GN Name=MYH1B; Synonyms=MYH3;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3571266; DOI=10.1016/s0021-9258(18)48267-1;
RA Molina M.I., Kropp K.E., Gulick J., Robbins J.;
RT "The sequence of an embryonic myosin heavy chain gene and isolation of its
RT corresponding cDNA.";
RL J. Biol. Chem. 262:6478-6488(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1502-1940.
RX PubMed=6833296; DOI=10.1016/s0021-9258(18)32558-4;
RA Kavinsky C.J., Umeda P.K., Sinha A.M., Elzinga M., Tong S.W., Zak R.,
RA Jakovcic S., Rabinowitz M.;
RT "Cloned mRNA sequences for two types of embryonic myosin heavy chains from
RT chick skeletal muscle. I. DNA and derived amino acid sequence of light
RT meromyosin.";
RL J. Biol. Chem. 258:5196-5205(1983).
RN [3]
RP PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2997212; DOI=10.1016/s0021-9258(17)38599-x;
RA Gulick J., Kropp K., Robbins J.;
RT "The structure of two fast-white myosin heavy chain promoters. A
RT comparative study.";
RL J. Biol. Chem. 260:14513-14520(1985).
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: Cytoplasm, myofibril. Note=Thick filaments of the
CC 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; V00430; CAA23712.1; -; mRNA.
DR EMBL; J02714; AAA48972.1; -; Genomic_DNA.
DR PIR; A29320; A29320.
DR AlphaFoldDB; P02565; -.
DR SMR; P02565; -.
DR STRING; 9031.ENSGALP00000041897; -.
DR iPTMnet; P02565; -.
DR PaxDb; P02565; -.
DR PRIDE; P02565; -.
DR VEuPathDB; HostDB:geneid_417306; -.
DR eggNOG; KOG0161; Eukaryota.
DR InParanoid; P02565; -.
DR PhylomeDB; P02565; -.
DR Proteomes; UP000000539; 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:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0000146; F:microfilament motor activity; IBA:GO_Central.
DR GO; GO:0006936; P:muscle contraction; 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 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 Reference proteome; Thick filament.
FT CHAIN 1..1940
FT /note="Myosin-1B"
FT /id="PRO_0000123397"
FT DOMAIN 33..82
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01190"
FT DOMAIN 86..783
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 786..815
FT /note="IQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT REGION 660..682
FT /note="Actin-binding"
FT REGION 762..776
FT /note="Actin-binding"
FT REGION 1912..1940
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 844..1940
FT /evidence="ECO:0000255"
FT BINDING 179..186
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT MOD_RES 130
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000255"
FT VARIANT 379
FT /note="G -> D"
FT CONFLICT 1547
FT /note="T -> A (in Ref. 2; CAA23712)"
FT /evidence="ECO:0000305"
FT CONFLICT 1913..1915
FT /note="ERA -> GRT (in Ref. 2; CAA23712)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1940 AA; 222817 MW; C34833D75B04DFF2 CRC64;
MATDADMAIF GEAAPYLRKS EKERIEAQNK PFDAKSSVFV VHAKESYVKS TIQSKESGKV
TVKTEGGETL TVKEDQIFSM NPPKYDKIED MAMMTHLHEP AVLYNLKERY AAWMIYTYSG
LFCVTVNPYK WLPVYNPEVV LAYRGKKRQE APPHIFSISD NAYQFMLTDR ENQSILITGE
SGAGKTVNTK RVIQYFATIA ASGDKKKEEQ PAGKMQGTLE DQIISANPLL EAFGNAKTVR
NDNSSRFGKF IRIHFGATGK LASADIETYL LEKSRVTFQL KAERSYHIFY QIMSNKKPEL
IEMLLITTNP YDYQYVSQGE ITVPSINDQE ELMATDSAID ILGFTPDEKT AIYKLTGAVM
HYGNLKFKQK QREEQAEPGG TEVADKAAYL MGLNSADLLK ALCYPRVKVG NEYVTKGQTV
QQVYNSVGAL AKSVFEKMFL WMVVRINQQL DTKQPRQYFI GVLDIAGFEI FDFNSLEQLC
INFTNEKLQQ FFNHHMFVLE QEEYKKEGIE WEFIDFGMDL AACIELIEKP MGIFSILEEE
CMFPKATDTS FKNKLYDQHL GKSNNFQKPK PGKGKAEAHF SLVHYAGTVD YNITGWLEKN
KDPLNETVVG LYQKSSLKTL ALLFASVGGA EAESGAGGKK GGKKKGSSFQ TVSALFRENL
NKLMSNLRST HPHFVRCLIP NETKTPGAME HELVLHQLRC NGVLEGIRIC RKGFPIRILY
ADFKQRYKVL NASAIPEGQF IDSKKASEKL LGSIDVDHTQ YKFGHTKVFF KAGLLGLLEE
MRDEKLAQLI TRTQARCRGF LMRVEFKKMM ERRESIFCIQ YNVRAFMNVK HWPWMKLFFK
IKPLLKSAES EKEMANMKEE FEKTKEELAK SEAKRKELEE KMVSLLQEKN DLQLQVQAEA
DGLADAEERC DQLIKTKIQL EAKIKELTER AEDEEEMNAE LTAKKRKLED ECSELKKDID
DLELTLAKVE KEKHATENKV KNLTEEMAAL DETIAKLTKE KKALQEAHQQ TLDDLQAEED
KVNTLTKAKT KLEQQVDDLE GSLEQEKKLR MDLERAKRKL EGDLKMTQES TMDLENDKQQ
LDEKLKKKDF EISQIQSKIE DEQALGMQLQ KKIKELQARI EELEEEIEAE RTSRAKAEKH
RADLSRELEE ISERLEEAGG ATAAQIDMNK KREAEFQKMR RDLEEATLQH EATAAALRKK
HADSTADVGE QIDNLQRVKQ KLEKEKSELK MEIDDLASNM ESVSKAKANL EKMCRSLEDQ
LSEIKTKEEE QQRTINDISA QKARLQTESG EYSRQVEEKD ALISQLSRGK QAFTQQIEEL
KRHLEEEIKA KKCPAHALQS ARHDCDLLRE QYEEEQEAKG ELQRALSKAN SEVAQWRTKY
ETDAIQRTEE LEEAKKKLAQ RLQDAEEHVE AVNSKCASLE KTKQRLQNEV EDLMIDVERS
NAACAALDKK QKNFDKILSE WKQKYEETQA ELEASQKESR SLSTELFKMK NAYEESLDHL
ETLKRENKNL QQEISDLTEQ IAEGGKAIHE LEKVKKQIEQ EKSELQTALE EAEASLEHEE
GKILRVQLEL NQVKSDIDRK IAEKDEEIDQ LKRNHLRVVD SMQSTLDAEI RSRNEALRLK
KKMEGDLNEI EIQLSHANRQ AAEAQKNLRN TQGVLKDTQI HLDDALRSQE DLKEQVAMVE
RRANLLQAEI EELRAALEQT ERSRKVAEQE LLDASERVQL LHTQNTSLIN TKKKLESDIS
QIQSEMEDTI QEARNAEEKA KKAITDAAMM AEELKKEQDT SAHLERMKKN LDQTVKDLQH
RLDEAEQLAL KGGKKQIQKL EARVRELEGE VDAEQKRSAE AVKGVRKYER RVKELTYQSE
EDRKNVLRLQ DLVDKLQMKV KSYKRQAEEA EELSNVNLSK FRKIQHELEE AEERADIAES
QVNKLRAKSR EIGKKAESEE
