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MYOM1_BOVIN
ID   MYOM1_BOVIN             Reviewed;         340 AA.
AC   P80473;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=Myomesin-1;
DE   AltName: Full=190 kDa titin-associated protein;
DE   AltName: Full=Myomesin family member 1;
DE   Flags: Fragments;
GN   Name=MYOM1;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Skeletal muscle;
RX   PubMed=7588733; DOI=10.1111/j.1432-1033.1995.110_1.x;
RA   Obermann W.M.J., Plessmann U., Weber K., Fuerst D.O.;
RT   "Purification and biochemical characterization of myomesin, a myosin-
RT   binding and titin-binding protein, from bovine skeletal muscle.";
RL   Eur. J. Biochem. 233:110-115(1995).
CC   -!- FUNCTION: Major component of the vertebrate myofibrillar M band. Binds
CC       myosin, titin, and light meromyosin. This binding is dose dependent.
CC   -!- SUBUNIT: Homodimer. Interacts with TTN/titin and PNKD. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, M line
CC       {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Seems to be expressed in all cardiac and skeletal
CC       fibers.
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DR   PRIDE; P80473; -.
DR   InParanoid; P80473; -.
DR   OrthoDB; 57219at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0031430; C:M band; IDA:CAFA.
DR   GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR   GO; GO:0019900; F:kinase binding; IBA:GO_Central.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR   GO; GO:0006936; P:muscle contraction; IBA:GO_Central.
PE   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; Muscle protein; Reference proteome.
FT   CHAIN           <1..>340
FT                   /note="Myomesin-1"
FT                   /id="PRO_0000096671"
FT   REGION          178..212
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_CONS        14..15
FT                   /evidence="ECO:0000305"
FT   NON_CONS        49..50
FT                   /evidence="ECO:0000305"
FT   NON_CONS        82..83
FT                   /evidence="ECO:0000305"
FT   NON_CONS        105..106
FT                   /evidence="ECO:0000305"
FT   NON_CONS        120..121
FT                   /evidence="ECO:0000305"
FT   NON_CONS        134..135
FT                   /evidence="ECO:0000305"
FT   NON_CONS        158..159
FT                   /evidence="ECO:0000305"
FT   NON_CONS        203..204
FT                   /evidence="ECO:0000305"
FT   NON_CONS        220..221
FT                   /evidence="ECO:0000305"
FT   NON_CONS        232..233
FT                   /evidence="ECO:0000305"
FT   NON_CONS        270..271
FT                   /evidence="ECO:0000305"
FT   NON_CONS        283..284
FT                   /evidence="ECO:0000305"
FT   NON_CONS        287..288
FT                   /evidence="ECO:0000305"
FT   NON_CONS        306..307
FT                   /evidence="ECO:0000305"
FT   NON_CONS        317..318
FT                   /evidence="ECO:0000305"
FT   NON_TER         1
FT   NON_TER         340
SQ   SEQUENCE   340 AA;  37307 MW;  509383C7A2E22067 CRC64;
     QSMSTLHQEE AFEKADQLSL KKTLEETEAF HKKLNEDHLL HAPEPVIKPG TAYKNQVPIN
     VQAHPGKYII ESRYGVHTLE INDDTRFHSG ASTLPPSXYA SRFEIHFQPE IQXYRNGVPI
     DAEXXGAPAI PKYNDYIIIT XKQPAVDGGS PILGYFIDVG IGXPSRVSEP VAALDPAEKA
     RLKSRPSAPX TGQIIVTEEE PSEEAGTENX QRVNTELPVK XSNNAGVXEP EETGGAEITG
     YYVNYREVID GVPGRXREAN IKAISDEAYK XEEXTIAVPG PPHMTFKNRA RVVGGLPDVV
     TIQEGKLLAS DEHXNLKYGS EISDFTVSVF IPEEEARSVA
 
 
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