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Tropomyosin alpha-1 chain (Alpha-tropomyosin) (Tropomyosin-1)

 TPM1_RABIT              Reviewed;         284 AA.
P58772; P02558; P46902; P99034;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
25-OCT-2017, entry version 102.
RecName: Full=Tropomyosin alpha-1 chain;
AltName: Full=Alpha-tropomyosin;
AltName: Full=Tropomyosin-1;
Name=TPM1; Synonyms=TPMA;
Oryctolagus cuniculus (Rabbit).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae;
Oryctolagus.
NCBI_TaxID=9986;
[1]
PROTEIN SEQUENCE, AND ACETYLATION AT MET-1.
TISSUE=Skeletal muscle;
PubMed=624724;
Stone D., Smillie L.B.;
"The amino acid sequence of rabbit skeletal alpha-tropomyosin. The
NH2-terminal half and complete sequence.";
J. Biol. Chem. 253:1137-1148(1978).
[2]
PROTEIN SEQUENCE, AND ACETYLATION AT MET-1.
TISSUE=Heart muscle;
PubMed=6993480;
Lewis W.G., Smillie L.B.;
"The amino acid sequence of rabbit cardiac tropomyosin.";
J. Biol. Chem. 255:6854-6859(1980).
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND ACETYLATION AT MET-1.
STRAIN=New Zealand white; TISSUE=Skeletal muscle;
PubMed=7622625; DOI=10.1007/BF00122528;
Kluwe L., Maeda K., Miegel A., Fujita-Becker S., Maeda Y., Talbo G.,
Houthaeve T., Kellner R.;
"Rabbit skeletal muscle alpha alpha-tropomyosin expressed in
baculovirus-infected insect cells possesses the authentic N-terminus
structure and functions.";
J. Muscle Res. Cell Motil. 16:103-110(1995).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 103-146.
PubMed=6687628; DOI=10.1038/302718a0;
Putney S.D., Herlihy W.C., Schimmel P.R.;
"A new troponin T and cDNA clones for 13 different muscle proteins,
found by shotgun sequencing.";
Nature 302:718-721(1983).
[5]
PHOSPHORYLATION AT SER-283.
TISSUE=Skeletal muscle;
PubMed=278975; DOI=10.1073/pnas.75.8.3588;
Mak A.S., Smillie L.B., Barany M.;
"Specific phosphorylation at serine-283 of alpha tropomyosin from frog
skeletal and rabbit skeletal and cardiac muscle.";
Proc. Natl. Acad. Sci. U.S.A. 75:3588-3592(1978).
[6]
SUBUNIT.
PubMed=23832280; DOI=10.1007/s10974-013-9353-x;
Janco M., Suphamungmee W., Li X., Lehman W., Lehrer S.S., Geeves M.A.;
"Polymorphism in tropomyosin structure and function.";
J. Muscle Res. Cell Motil. 34:177-187(2013).
[7]
X-RAY CRYSTALLOGRAPHY (15 ANGSTROMS).
PubMed=3820300; DOI=10.1016/0022-2836(86)90469-9;
Phillips G.N. Jr.;
"Construction of an atomic model for tropomyosin and implications for
interactions with actin.";
J. Mol. Biol. 192:128-131(1986).
-!- FUNCTION: Binds to actin filaments in muscle and non-muscle cells.
Plays a central role, in association with the troponin complex, in
the calcium dependent regulation of vertebrate striated muscle
contraction. Smooth muscle contraction is regulated by interaction
with caldesmon. In non-muscle cells is implicated in stabilizing
cytoskeleton actin filaments. {ECO:0000250|UniProtKB:P09493}.
-!- SUBUNIT: Homodimer (PubMed:23832280). Heterodimer of an alpha
(TPM1, TPM3 or TPM4) and a beta (TPM2) chain (By similarity).
Interacts with HRG (via the HRR domain); the interaction
contributes to the antiangiogenic properties of the
histidine/proline-rich region (HRR) of HRG (By similarity).
Interacts (via N-terminus) with LMOD2 (via N-terminus) and TMOD1
(via N-terminus) (By similarity). {ECO:0000250|UniProtKB:P04268,
ECO:0000250|UniProtKB:P04692, ECO:0000250|UniProtKB:P09493,
ECO:0000269|PubMed:23832280}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
{ECO:0000250|UniProtKB:P04692}. Note=Associates with F-actin
stress fibers. {ECO:0000250|UniProtKB:P04692}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=1;
Comment=A number of isoforms may be produced.;
Name=1;
IsoId=P58772-1; Sequence=Displayed;
-!- DOMAIN: The molecule is in a coiled coil structure that is formed
by 2 polypeptide chains. The sequence exhibits a prominent seven-
residues periodicity.
-!- PTM: Phosphorylated at Ser-283 by DAPK1 in response to oxidative
stress and this phosphorylation enhances stress fiber formation in
endothelial cells. {ECO:0000250}.
-!- SIMILARITY: Belongs to the tropomyosin family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; S78854; AAB34957.1; -; mRNA.
EMBL; V00892; CAA24257.1; -; mRNA.
PIR; I47056; TMRBA.
RefSeq; NP_001099158.1; NM_001105688.1. [P58772-1]
UniGene; Ocu.3324; -.
UniGene; Ocu.7353; -.
PDB; 2D3E; X-ray; 2.60 A; A/B/C/D=176-284.
PDB; 2EFR; X-ray; 1.80 A; A/B/C/D=176-273.
PDB; 2EFS; X-ray; 2.00 A; A/B/C/D=176-273.
PDB; 2TMA; X-ray; 15.00 A; A/B=1-284.
PDB; 2W49; EM; 35.00 A; A/B/C/T/U/V/W/X=8-284.
PDB; 2W4U; EM; 35.00 A; A/B/C/T/U/V/W/X=8-284.
PDB; 2Z5H; X-ray; 2.89 A; A/B/C/D/E/F/G/H=254-284, I=1-24.
PDB; 2Z5I; X-ray; 2.10 A; A/B/C/D/E/F/G/H=254-284, I/J=1-24.
PDB; 4A7F; EM; 7.70 A; B/H=98-233.
PDB; 4A7H; EM; 7.80 A; B/H=98-233.
PDB; 4A7L; EM; 8.10 A; B/H=98-233.
PDBsum; 2D3E; -.
PDBsum; 2EFR; -.
PDBsum; 2EFS; -.
PDBsum; 2TMA; -.
PDBsum; 2W49; -.
PDBsum; 2W4U; -.
PDBsum; 2Z5H; -.
PDBsum; 2Z5I; -.
PDBsum; 4A7F; -.
PDBsum; 4A7H; -.
PDBsum; 4A7L; -.
ProteinModelPortal; P58772; -.
SMR; P58772; -.
BioGrid; 1172720; 1.
DIP; DIP-46098N; -.
IntAct; P58772; 3.
MINT; MINT-1500045; -.
iPTMnet; P58772; -.
GeneID; 100125989; -.
KEGG; ocu:100125989; -.
CTD; 7168; -.
HOGENOM; HOG000231521; -.
HOVERGEN; HBG107404; -.
InParanoid; P58772; -.
KO; K10373; -.
EvolutionaryTrace; P58772; -.
PMAP-CutDB; P58772; -.
Proteomes; UP000001811; Unplaced.
GO; GO:0015629; C:actin cytoskeleton; ISS:UniProtKB.
GO; GO:0005884; C:actin filament; IMP:CAFA.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
GO; GO:0051015; F:actin filament binding; ISS:UniProtKB.
GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
GO; GO:0031013; F:troponin I binding; IPI:CAFA.
InterPro; IPR000533; Tropomyosin.
Pfam; PF00261; Tropomyosin; 1.
PRINTS; PR00194; TROPOMYOSIN.
PROSITE; PS00326; TROPOMYOSIN; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Actin-binding; Alternative splicing;
Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton;
Direct protein sequencing; Muscle protein; Phosphoprotein;
Reference proteome.
CHAIN 1 284 Tropomyosin alpha-1 chain.
/FTId=PRO_0000205623.
COILED 1 284 {ECO:0000250}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000269|PubMed:624724,
ECO:0000269|PubMed:6993480,
ECO:0000269|PubMed:7622625}.
MOD_RES 45 45 Phosphoserine.
{ECO:0000250|UniProtKB:P04692}.
MOD_RES 53 53 Phosphothreonine.
{ECO:0000250|UniProtKB:P07951}.
MOD_RES 61 61 Phosphoserine.
{ECO:0000250|UniProtKB:P58774}.
MOD_RES 79 79 Phosphothreonine.
{ECO:0000250|UniProtKB:P07951}.
MOD_RES 87 87 Phosphoserine.
{ECO:0000250|UniProtKB:P06753}.
MOD_RES 108 108 Phosphothreonine.
{ECO:0000250|UniProtKB:P07951}.
MOD_RES 174 174 Phosphoserine.
{ECO:0000250|UniProtKB:P09493}.
MOD_RES 186 186 Phosphoserine.
{ECO:0000250|UniProtKB:P58771}.
MOD_RES 206 206 Phosphoserine.
{ECO:0000250|UniProtKB:P58771}.
MOD_RES 215 215 Phosphoserine.
{ECO:0000250|UniProtKB:P58775}.
MOD_RES 252 252 Phosphoserine.
{ECO:0000250|UniProtKB:P58771}.
MOD_RES 261 261 Phosphotyrosine.
{ECO:0000250|UniProtKB:P04692}.
MOD_RES 271 271 Phosphoserine.
{ECO:0000250|UniProtKB:P58771}.
MOD_RES 282 282 Phosphothreonine.
{ECO:0000250|UniProtKB:P07951}.
MOD_RES 283 283 Phosphoserine; by DAPK1.
{ECO:0000269|PubMed:278975}.
HELIX 2 24 {ECO:0000244|PDB:2Z5I}.
HELIX 176 273 {ECO:0000244|PDB:2EFR}.
SEQUENCE 284 AA; 32681 MW; E25609F597A72F4D CRC64;
MDAIKKKMQM LKLDKENALD RAEQAEADKK AAEDRSKQLE DELVSLQKKL KGTEDELDKY
SEALKDAQEK LELAEKKATD AEADVASLNR RIQLVEEELD RAQERLATAL QKLEEAEKAA
DESERGMKVI ESRAQKDEEK MEIQEIQLKE AKHIAEDADR KYEEVARKLV IIESDLERAE
ERAELSEGKC AELEEELKTV TNNLKSLEAQ AEKYSQKEDK YEEEIKVLSD KLKEAETRAE
FAERSVTKLE KSIDDLEDEL YAQKLKYKAI SEELDHALND MTSI


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