ID   TPM1_DANRE              Reviewed;         284 AA.
AC   P13104;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=Tropomyosin alpha-1 chain;
DE   AltName: Full=Alpha-tropomyosin;
DE   AltName: Full=Tropomyosin-1;
GN   Name=tpma; Synonyms=tpm1;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=11002340;
RX   DOI=10.1002/1097-0177(2000)9999:9999<::aid-dvdy1043>3.3.co;2-9;
RA   Xu Y., He J., Wang X., Lim T.M., Gong Z.;
RT   "Asynchronous activation of 10 muscle-specific protein (MSP) genes during
RT   zebrafish somitogenesis.";
RL   Dev. Dyn. 219:201-215(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=AB;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; M24635; AAA50021.1; -; mRNA.
DR   EMBL; AF180892; AAF78475.1; -; mRNA.
DR   EMBL; BC062870; AAH62870.1; -; mRNA.
DR   PIR; I51731; I51731.
DR   RefSeq; NP_571180.1; NM_131105.2.
DR   AlphaFoldDB; P13104; -.
DR   SMR; P13104; -.
DR   STRING; 7955.ENSDARP00000039656; -.
DR   PaxDb; P13104; -.
DR   PRIDE; P13104; -.
DR   Ensembl; ENSDART00000173453; ENSDARP00000142967; ENSDARG00000033683.
DR   GeneID; 30324; -.
DR   KEGG; dre:30324; -.
DR   CTD; 30324; -.
DR   ZFIN; ZDB-GENE-990415-269; tpma.
DR   eggNOG; KOG1003; Eukaryota.
DR   GeneTree; ENSGT01030000234542; -.
DR   HOGENOM; CLU_055027_0_0_1; -.
DR   InParanoid; P13104; -.
DR   OMA; DEASRMC; -.
DR   OrthoDB; 1576041at2759; -.
DR   PhylomeDB; P13104; -.
DR   TreeFam; TF351519; -.
DR   PRO; PR:P13104; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 7.
DR   Bgee; ENSDARG00000033683; Expressed in bone element and 33 other tissues.
DR   ExpressionAtlas; P13104; baseline and differential.
DR   GO; GO:0015629; C:actin cytoskeleton; ISS:UniProtKB.
DR   GO; GO:0005884; C:actin filament; IBA:GO_Central.
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   GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR   GO; GO:0006936; P:muscle contraction; IBA:GO_Central.
DR   GO; GO:0061515; P:myeloid cell development; IMP:ZFIN.
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;
KW   Reference proteome.
FT   CHAIN           1..284
FT                   /note="Tropomyosin alpha-1 chain"
FT                   /id="PRO_0000205639"
FT   REGION          1..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1..284
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   284 AA;  32723 MW;  7B6403B873CEE6BD CRC64;
     MDAIKKKMQM LKLDKENALD RAEQAETDKK AAEERSKQLE DDLVALQKKL KATEDELDKY
     SEALKDAQEK LELAEKKATD AEGDVASLNR RIQLVEEELD RAQERLATAL QKLEEAEKAA
     DESERGMKVI ENRALKDEEK MELQEIQLKE AKHIAEEADR KYEEVARKLV IVEGELERTE
     ERAELNEGKC SELEEELKTV TNNMKSLEAQ AEKYSAKEDK YEEEIKVLTD KLKEAETRAE
     FAERSVAKLE KTIDDLEDEL YAQKLKYKAI SEELDHALND MTSI