ID   TPM1_XENLA              Reviewed;         284 AA.
AC   Q01173; Q01174;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Tropomyosin alpha-1 chain;
DE   AltName: Full=Alpha-tropomyosin;
DE   AltName: Full=Tropomyosin-1;
GN   Name=tpm1;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Embryo, and Oocyte;
RX   PubMed=1840524; DOI=10.1111/j.1432-1033.1991.tb16392.x;
RA   Hardy S., Fishman M., Obsorne H.B., Thiebaud P.;
RT   "Characterization of muscle and non muscle Xenopus laevis tropomyosin mRNAs
RT   transcribed from the same gene. Developmental and tissue-specific
RT   expression.";
RL   Eur. J. Biochem. 202:431-440(1991).
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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=Muscle;
CC         IsoId=Q01173-1; Sequence=Displayed;
CC       Name=2; Synonyms=non-muscle;
CC         IsoId=Q01173-2; Sequence=VSP_006612, VSP_006613, VSP_006614;
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; X61273; CAA43577.1; -; mRNA.
DR   EMBL; X61272; CAA43576.1; -; mRNA.
DR   PIR; S19690; S19690.
DR   PIR; S19691; S19691.
DR   RefSeq; NP_001128548.1; NM_001135076.1. [Q01173-1]
DR   AlphaFoldDB; Q01173; -.
DR   SMR; Q01173; -.
DR   BioGRID; 932828; 1.
DR   DNASU; 100189579; -.
DR   GeneID; 100189579; -.
DR   KEGG; xla:100189579; -.
DR   CTD; 100189579; -.
DR   Xenbase; XB-GENE-865564; tpm1.L.
DR   OrthoDB; 1576041at2759; -.
DR   Proteomes; UP000186698; Chromosome 3L.
DR   Bgee; 100189579; Expressed in heart and 19 other tissues.
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; Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton;
KW   Muscle protein; Reference proteome.
FT   CHAIN           1..284
FT                   /note="Tropomyosin alpha-1 chain"
FT                   /id="PRO_0000205642"
FT   REGION          1..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1..284
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         1..80
FT                   /note="MDAIKKKMQMLKLDKENALDRAEQAEADKKGAEDKSKQLEDELVALQKKLKG
FT                   TEDELDKYSEALKDAQEKLELSDKKATD -> MAGITSLEAVKRKIKCLQDQADEAEER
FT                   AEKLQRERDMERKLREA (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:1840524"
FT                   /id="VSP_006612"
FT   VAR_SEQ         189..211
FT                   /note="KCAELEEELKTVTNNLKSLEAQA -> HYRQLEDQQRIMDQTLKTLIASE
FT                   (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:1840524"
FT                   /id="VSP_006613"
FT   VAR_SEQ         258..284
FT                   /note="DELYAQKLKYKAISEELDHALNDMTSI -> EKVAHAKEENLNMHQMLDQTL
FT                   LELNNM (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:1840524"
FT                   /id="VSP_006614"
SQ   SEQUENCE   284 AA;  32651 MW;  B7F6844D9900FE69 CRC64;
     MDAIKKKMQM LKLDKENALD RAEQAEADKK GAEDKSKQLE DELVALQKKL KGTEDELDKY
     SEALKDAQEK LELSDKKATD AEGDVASLNR RIQLVEEELD RAQERLSTAL QKLEEAEKAA
     DESERGMKVI ENRALKDEEK MELQEIQLKE AKHIAEEADR KYEEVARKLV IIEGDLERAE
     ERAELSESKC AELEEELKTV TNNLKSLEAQ AEKYSQKEDK YEEEIKVLTD KLKEAETRAE
     FAERTVAKLE KSIDDLEDEL YAQKLKYKAI SEELDHALND MTSI