ID   TPM1_CHEAU              Reviewed;         284 AA.
AC   P84335;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   25-MAY-2022, entry version 39.
DE   RecName: Full=Tropomyosin alpha-1 chain;
DE   AltName: Full=Alpha-tropomyosin;
DE   AltName: Full=Tropomyosin-1;
OS   Chelon auratus (Golden grey mullet) (Liza aurata).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Mugilomorphae; Mugilidae; Chelon.
OX   NCBI_TaxID=48191;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, AND MASS SPECTROMETRY.
RC   TISSUE=Skeletal muscle {ECO:0000269|Ref.1};
RA   Ghedira R.;
RT   "Characterization of tropomyosin of Liza aurata.";
RL   Thesis (2004), ISBM, Tunisia.
CC   -!- FUNCTION: Binds to actin filaments in muscle and non-muscle cells.
CC       Plays a central role, in association with the troponin complex, in the
CC       calcium dependent regulation of vertebrate striated muscle contraction.
CC       Smooth muscle contraction is regulated by interaction with caldesmon.
CC       In non-muscle cells is implicated in stabilizing cytoskeleton actin
CC       filaments. {ECO:0000250|UniProtKB:P09493, ECO:0000269|Ref.1}.
CC   -!- SUBUNIT: Homodimer. Heterodimer of an alpha (TPM1, TPM3 or TPM4) and a
CC       beta (TPM2) chain. {ECO:0000250|UniProtKB:P04692}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000250|UniProtKB:P04692}. Note=Associates with F-actin stress
CC       fibers. {ECO:0000250|UniProtKB:P04692}.
CC   -!- DOMAIN: The molecule is in a coiled coil structure that is formed by 2
CC       polypeptide chains. The sequence exhibits a prominent seven-residues
CC       periodicity. {ECO:0000305}.
CC   -!- MASS SPECTROMETRY: Mass=32781; Method=MALDI;
CC       Evidence={ECO:0000269|Ref.1};
CC   -!- SIMILARITY: Belongs to the tropomyosin family. {ECO:0000255}.
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DR   AlphaFoldDB; P84335; -.
DR   SMR; P84335; -.
DR   GO; GO:0015629; C:actin cytoskeleton; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0051015; F:actin filament binding; ISS:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR   GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR   InterPro; IPR000533; Tropomyosin.
DR   Pfam; PF00261; Tropomyosin; 1.
DR   PRINTS; PR00194; TROPOMYOSIN.
DR   PROSITE; PS00326; TROPOMYOSIN; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Actin-binding; Coiled coil; Cytoplasm; Cytoskeleton;
KW   Direct protein sequencing; Muscle protein.
FT   CHAIN           1..284
FT                   /note="Tropomyosin alpha-1 chain"
FT                   /id="PRO_0000205640"
FT   REGION          1..40
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1..284
FT                   /evidence="ECO:0000250"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:P04268"
SQ   SEQUENCE   284 AA;  32730 MW;  ACB56A38A54CFACE CRC64;
     MDAIKKKMQM LKLDKENALD RAEQAESDKK ASEDRSKQLE DDLVALQKKL KGTEDELDKY
     SEALKDAQEK LELAEKKATD AEGDVASLNR RIQLVEEELD RAQERLATAL TKLEEAEKAA
     DESERGMKVI ENRAMKDEEK MELQEIQLKE AKHIAEEADR KYEEVARKLV IIEGDLERTE
     ERAELSESKC SELEEELKTV TNNLKSLEAQ AEKYSQKEDK YEEEIKVLTD KLKEAETRAE
     FAERSVAKLE KTIDDLEDEL YAQKLKYKAI SEELDHALND MTSI