ID   TPM1_RANTE              Reviewed;         284 AA.
AC   P13105;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   25-MAY-2022, entry version 69.
DE   RecName: Full=Tropomyosin alpha-1 chain;
DE   AltName: Full=Alpha-tropomyosin;
DE   AltName: Full=Tropomyosin-1;
GN   Name=tpm1;
OS   Rana temporaria (European common frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Rana; Rana.
OX   NCBI_TaxID=8407;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2788276; DOI=10.1073/pnas.86.15.5673;
RA   Ohara O., Dorit R.L., Gilbert W.;
RT   "One-sided polymerase chain reaction: the amplification of cDNA.";
RL   Proc. Natl. Acad. Sci. U.S.A. 86:5673-5677(1989).
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}.
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.
CC   -!- SIMILARITY: Belongs to the tropomyosin 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; M24634; AAA18096.1; -; mRNA.
DR   AlphaFoldDB; P13105; -.
DR   BMRB; P13105; -.
DR   SMR; P13105; -.
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   2: Evidence at transcript level;
KW   Actin-binding; Coiled coil; Cytoplasm; Cytoskeleton; Muscle protein.
FT   CHAIN           1..284
FT                   /note="Tropomyosin alpha-1 chain"
FT                   /id="PRO_0000205641"
FT   REGION          1..40
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1..284
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   284 AA;  32665 MW;  D036806D9FC32D55 CRC64;
     MDAIKKKMQM LKLDKENALD RAEQAEADKK GAEDKSKQLE DELVAMQKKM KGTEDELDKY
     SEALKDAQEK LELAEKKATD AEADVASLNR RIQLVEEELD RAQERLATAL QKLEEAEKAA
     DESERGMKVI ENRALKDEEK IELQEIQLKE AKHIAEEADR KYEEVARKLV IIEGDLERAE
     ERAELSESKC AELEEELKTV TNNLKSLEAQ AEKYSQKEDK YEEEIKVLTD KLKEAETRAE
     FAERTVAKLE KSIDDLEDEL YAQKLKYKAI SEELDHALND MTSI