ID   TPM3_PIG                Reviewed;         284 AA.
AC   A1XQV4;
DT   12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   24-JAN-2024, entry version 71.
DE   RecName: Full=Tropomyosin alpha-3 chain;
DE   AltName: Full=Gamma-tropomyosin;
DE   AltName: Full=Tropomyosin-3;
GN   Name=TPM3;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Longissimus dorsi muscle;
RA   Cai G., Chen Y., Wang C., Li J., Peng G., Zhang H.;
RT   "Generation and analysis of cDNA sequences derived from a porcine skeletal
RT   muscle library.";
RL   Submitted (MAY-2006) 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 (By similarity). Interacts with TMOD1 (By
CC       similarity). Interacts with TNNT1 (By similarity).
CC       {ECO:0000250|UniProtKB:P04692, ECO:0000250|UniProtKB:P06753}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}.
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; DQ629176; ABK55660.1; -; mRNA.
DR   RefSeq; NP_001302554.1; NM_001315625.1.
DR   RefSeq; XP_003361668.3; XM_003361620.4.
DR   AlphaFoldDB; A1XQV4; -.
DR   SMR; A1XQV4; -.
DR   STRING; 9823.ENSSSCP00000074135; -.
DR   iPTMnet; A1XQV4; -.
DR   PeptideAtlas; A1XQV4; -.
DR   GeneID; 100620599; -.
DR   InParanoid; A1XQV4; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   Proteomes; UP000694570; Unplaced.
DR   Proteomes; UP000694571; Unplaced.
DR   Proteomes; UP000694720; Unplaced.
DR   Proteomes; UP000694722; Unplaced.
DR   Proteomes; UP000694723; Unplaced.
DR   Proteomes; UP000694724; Unplaced.
DR   Proteomes; UP000694725; Unplaced.
DR   Proteomes; UP000694726; Unplaced.
DR   Proteomes; UP000694727; Unplaced.
DR   Proteomes; UP000694728; Unplaced.
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; IBA:GO_Central.
DR   GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR   GO; GO:0006936; P:muscle contraction; IBA:GO_Central.
DR   Gene3D; 1.20.5.170; -; 2.
DR   Gene3D; 1.20.5.340; -; 1.
DR   InterPro; IPR000533; Tropomyosin.
DR   PANTHER; PTHR19269; TROPOMYOSIN; 1.
DR   PANTHER; PTHR19269:SF38; TROPOMYOSIN ALPHA-3 CHAIN; 1.
DR   Pfam; PF00261; Tropomyosin; 1.
DR   PRINTS; PR00194; TROPOMYOSIN.
DR   SUPFAM; SSF57997; Tropomyosin; 1.
DR   PROSITE; PS00326; TROPOMYOSIN; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Actin-binding; Coiled coil; Cytoplasm; Cytoskeleton;
KW   Muscle protein; Phosphoprotein; Reference proteome.
FT   CHAIN           1..284
FT                   /note="Tropomyosin alpha-3 chain"
FT                   /id="PRO_0000289990"
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:P58776"
FT   MOD_RES         53
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P07951"
FT   MOD_RES         61
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P58774"
FT   MOD_RES         87
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P06753"
FT   MOD_RES         108
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P07951"
FT   MOD_RES         252
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P07951"
FT   MOD_RES         261
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P58775"
FT   MOD_RES         271
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P21107"
FT   MOD_RES         282
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P07951"
FT   MOD_RES         283
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P21107"
SQ   SEQUENCE   284 AA;  33058 MW;  D976F4916D301198 CRC64;
     MEAIKKKMQM LKLDKENALD RAEQAEAEQK QAEERSKQLE DELAAMQKKL KGTEDELDKY
     SEALKDAQEK LELAEKKAAD AEAEVASLNR RIQLVEEELD RAQERLATAL QKLEEAEKAA
     DESERGMKVI ENRALKDEEK MELQEIQLKE AKHIAEEADR KYEEVARKLV IIEGDLERTE
     ERAELAEFKC FELEEELKNV TNNLKFLEAQ AEKYFQKKDK YEEEIKILTD KLKEAETRAE
     FAERSVAKLE KTIDDLEDEL YAQKLKYKAI SEELDHALND MTSI
//