TPM1_PIG
ID TPM1_PIG Reviewed; 284 AA.
AC P42639; A1XQV3; Q9TRA2;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 2.
DT 25-MAY-2022, entry version 112.
DE RecName: Full=Tropomyosin alpha-1 chain;
DE AltName: Full=Alpha-tropomyosin;
DE AltName: Full=Tropomyosin-1;
GN Name=TPM1;
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 [MRNA], AND X-RAY CRYSTALLOGRAPHY (9.0 ANGSTROMS).
RC TISSUE=Heart muscle;
RX PubMed=1404362; DOI=10.1016/0022-2836(92)90899-u;
RA Whitby F.G., Kent H.M., Stewart F., Stewart M., Xie X., Hatch V., Cohen C.,
RA Phillips G.N. Jr.;
RT "Structure of tropomyosin at 9-A resolution.";
RL J. Mol. Biol. 227:441-452(1992).
RN [2]
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.
RN [3]
RP PROTEIN SEQUENCE OF 2-16, AND INDUCTION.
RC TISSUE=Endothelial cell;
RX PubMed=7943254; DOI=10.1152/ajplung.1994.267.3.l271;
RA Rao U.J.S.P., Denslow N.D., Block E.R.;
RT "Hypoxia induces the synthesis of tropomyosin in cultured porcine pulmonary
RT artery endothelial cells.";
RL Am. J. Physiol. 267:L271-L281(1994).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (7.0 ANGSTROMS).
RX PubMed=10651038;
RX DOI=10.1002/(sici)1097-0134(20000101)38:1<49::aid-prot6>3.0.co;2-b;
RA Whitby F.G., Phillips G.N. Jr.;
RT "Crystal structure of tropomyosin at 7-A resolution.";
RL Proteins 38:49-59(2000).
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. Interacts with HRG (via the HRR domain); the
CC interaction contributes to the antiangiogenic properties of the
CC histidine/proline-rich region (HRR) of HRG. Interacts (via N-terminus)
CC with LMOD2 (via N-terminus) and TMOD1 (via N-terminus).
CC {ECO:0000250|UniProtKB:P04268, ECO:0000250|UniProtKB:P04692,
CC ECO:0000250|UniProtKB:P09493}.
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=1;
CC Comment=A number of isoforms may be produced.;
CC Name=1;
CC IsoId=P42639-1; Sequence=Displayed;
CC -!- INDUCTION: Induced by hypoxia. This induction is reversed by exposure
CC to normal levels of oxygen. {ECO:0000269|PubMed:7943254}.
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 -!- PTM: Phosphorylated at Ser-283 by DAPK1 in response to oxidative stress
CC and this phosphorylation enhances stress fiber formation in endothelial
CC cells. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the tropomyosin family. {ECO:0000305}.
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DR EMBL; X66274; CAA46986.1; -; mRNA.
DR EMBL; DQ629175; ABK55659.1; -; mRNA.
DR PIR; S24972; S24972.
DR RefSeq; NP_001090952.1; NM_001097483.2. [P42639-1]
DR PDB; 1C1G; X-ray; 7.00 A; A/B/C/D=1-284.
DR PDB; 7KO4; EM; 8.00 A; P/Q/R/S/W/X/Y/Z=1-284.
DR PDB; 7KO5; EM; 7.80 A; P/Q/R/S/W/X/Y/Z=1-284.
DR PDB; 7KO7; EM; 8.30 A; P/Q/R/S/W/X/Y/Z=1-284.
DR PDB; 7KON; EM; 8.10 A; P/Q/R/S/W/X/Y/Z=1-284.
DR PDB; 7KOR; EM; 7.80 A; P/Q/R/S/W/X/Y/Z=1-284.
DR PDBsum; 1C1G; -.
DR PDBsum; 7KO4; -.
DR PDBsum; 7KO5; -.
DR PDBsum; 7KO7; -.
DR PDBsum; 7KON; -.
DR PDBsum; 7KOR; -.
DR AlphaFoldDB; P42639; -.
DR BMRB; P42639; -.
DR SMR; P42639; -.
DR BioGRID; 1151508; 1.
DR STRING; 9823.ENSSSCP00000004929; -.
DR BindingDB; P42639; -.
DR iPTMnet; P42639; -.
DR PaxDb; P42639; -.
DR PeptideAtlas; P42639; -.
DR PRIDE; P42639; -.
DR GeneID; 100037999; -.
DR KEGG; ssc:100037999; -.
DR CTD; 7168; -.
DR eggNOG; KOG1003; Eukaryota.
DR InParanoid; P42639; -.
DR OrthoDB; 1576041at2759; -.
DR EvolutionaryTrace; P42639; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
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:0060048; P:cardiac muscle contraction; IBA:GO_Central.
DR GO; GO:0006936; P:muscle contraction; IBA:GO_Central.
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 3D-structure; Acetylation; Actin-binding; Alternative splicing;
KW Coiled coil; Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW Muscle protein; Phosphoprotein; Reference proteome.
FT CHAIN 1..284
FT /note="Tropomyosin alpha-1 chain"
FT /id="PRO_0000205622"
FT REGION 13..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 53..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 116..141
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:P09493"
FT MOD_RES 45
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04692"
FT MOD_RES 174
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09493"
FT MOD_RES 186
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P58771"
FT MOD_RES 206
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P58771"
FT MOD_RES 252
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P58771"
FT MOD_RES 261
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P04692"
FT MOD_RES 271
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P58771"
FT MOD_RES 283
FT /note="Phosphoserine; by DAPK1"
FT /evidence="ECO:0000250|UniProtKB:P09493"
FT CONFLICT 23..24
FT /note="EQ -> DE (in Ref. 1; CAA46986)"
FT /evidence="ECO:0000305"
FT CONFLICT 38
FT /note="R -> Q (in Ref. 1; CAA46986)"
FT /evidence="ECO:0000305"
FT CONFLICT 64
FT /note="P -> L (in Ref. 1; CAA46986)"
FT /evidence="ECO:0000305"
FT CONFLICT 95
FT /note="V -> F (in Ref. 1; CAA46986)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 284 AA; 32707 MW; F1D5501010908173 CRC64;
MDAIKKKMQM LKLDKENALD RAEQAEADKK AAEDRSKRLE DELVSLQKKL KATEDELDKY
SEAPKDAQEK LELAEKKATD AEADVASLNR RIQLVEEELD RAQERLATAL QKLEEAEKAA
DESERGMKVI ESRAQKDEEK MEIQEIQLKE AKHIAEDADR KYEEVARKLV IIESDLERAE
ERAELSEGKC AELEEELKTV TNNLKSLEAQ AEKYSQKEDK YEEEIKVLSD KLKEAETRAE
FAERSVTKLE KSIDDLEDEL YAQKLKYKAI SEELDHALND MTSI
