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

 TPM1_RAT                Reviewed;         284 AA.
P04692; P06469; P18342; P18343; P18344; P19354; Q53X09; Q63582;
Q63608; Q63609;
13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
04-APR-2006, sequence version 3.
12-SEP-2018, entry version 161.
RecName: Full=Tropomyosin alpha-1 chain;
AltName: Full=Alpha-tropomyosin;
AltName: Full=Tropomyosin-1;
Name=Tpm1; Synonyms=Alpha-tm, Tpma;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
PubMed=3838802; DOI=10.1038/315067a0;
Ruiz-Opazo N., Weinberger J., Nadal-Ginard B.;
"Comparison of alpha-tropomyosin sequences from smooth and striated
muscle.";
Nature 315:67-70(1985).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING.
PubMed=3558368;
Ruiz-Opazo N., Nadal-Ginard B.;
"Alpha-tropomyosin gene organization. Alternative splicing of
duplicated isotype-specific exons accounts for the production of
smooth and striated muscle isoforms.";
J. Biol. Chem. 262:4755-4765(1987).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING.
PubMed=3352602; DOI=10.1128/MCB.8.2.679;
Wieczorek D.F., Smith C.W., Nadal-Ginard B.;
"The rat alpha-tropomyosin gene generates a minimum of six different
mRNAs coding for striated, smooth, and nonmuscle isoforms by
alternative splicing.";
Mol. Cell. Biol. 8:679-694(1988).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 3; 4 AND 5).
TISSUE=Brain;
PubMed=2320008; DOI=10.1128/MCB.10.4.1729;
Lees-Miller J.P., Goodwin L.O., Helfman D.M.;
"Three novel brain tropomyosin isoforms are expressed from the rat
alpha-tropomyosin gene through the use of alternative promoters and
alternative RNA processing.";
Mol. Cell. Biol. 10:1729-1742(1990).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 6; 7 AND 8).
PubMed=2022655;
Goodwin L.O., Lees-Miller J.P., Leonard M.A., Cheley S.B.,
Helfman D.M.;
"Four fibroblast tropomyosin isoforms are expressed from the rat
alpha-tropomyosin gene via alternative RNA splicing and the use of two
promoters.";
J. Biol. Chem. 266:8408-8415(1991).
[6]
PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
PubMed=6179945;
Garfinkel L.I., Periasamy M., Nadal-Ginard B.;
"Cloning and characterization of cDNA sequences corresponding to
myosin light chains 1, 2, and 3, troponin-C, troponin-T, alpha-
tropomyosin, and alpha-actin.";
J. Biol. Chem. 257:11078-11086(1982).
[7]
PROTEIN SEQUENCE OF 92-101; 141-149; 218-226 AND 251-270, PARTIAL
PROTEIN SEQUENCE (ISOFORMS 4/5/7/8), AND IDENTIFICATION BY MASS
SPECTROMETRY.
STRAIN=Sprague-Dawley; TISSUE=Brain, Hippocampus, and Spinal cord;
Lubec G., Afjehi-Sadat L., Diao W., Kang S.U., Lubec S.;
Submitted (SEP-2007) to UniProtKB.
[8]
FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
PubMed=7568216; DOI=10.1073/pnas.92.21.9776;
Gimona M., Watakabe A., Helfman D.M.;
"Specificity of dimer formation in tropomyosins: influence of
alternatively spliced exons on homodimer and heterodimer assembly.";
Proc. Natl. Acad. Sci. U.S.A. 92:9776-9780(1995).
[9]
FUNCTION, AND SUBUNIT.
PubMed=22812662; DOI=10.1021/bi300340r;
Kalyva A., Schmidtmann A., Geeves M.A.;
"In vitro formation and characterization of the skeletal muscle
alpha.beta tropomyosin heterodimers.";
Biochemistry 51:6388-6399(2012).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45; SER-174; SER-252 AND
TYR-261, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: Binds to actin filaments in muscle and non-muscle cells
(PubMed:7568216, PubMed:22812662). Plays a central role, in
association with the troponin complex, in the calcium dependent
regulation of vertebrate striated muscle contraction
(PubMed:22812662). Smooth muscle contraction is regulated by
interaction with caldesmon. In non-muscle cells is implicated in
stabilizing cytoskeleton actin filaments.
{ECO:0000269|PubMed:22812662, ECO:0000269|PubMed:7568216}.
-!- SUBUNIT: Homodimer (PubMed:7568216, PubMed:22812662). Heterodimer
of an alpha (TPM1, TPM3 or TPM4) and a beta (TPM2) chain
(PubMed:7568216, PubMed:22812662). 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:P09493,
ECO:0000269|PubMed:22812662, ECO:0000269|PubMed:7568216}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
{ECO:0000269|PubMed:7568216}. Note=Associates with F-actin stress
fibers (PubMed:7568216). {ECO:0000269|PubMed:7568216}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=8;
Comment=Additional isoforms seem to exist.;
Name=1; Synonyms=Skeletal muscle;
IsoId=P04692-1; Sequence=Displayed;
Name=2; Synonyms=Smooth muscle;
IsoId=P04692-2; Sequence=VSP_006582, VSP_006584;
Note=Ref.1 (CAA26258) sequence differs from that shown due to
miscellaneous discrepancy. Ref.1 (CAA26258) sequence is in
conflict in position: 260:V->G. Ref.1 (CAA26258) sequence is in
conflict in position: 275:H->D. {ECO:0000305};
Name=3; Synonyms=Brain TMBr-1;
IsoId=P04692-3; Sequence=VSP_006585;
Name=4; Synonyms=Brain TMBr-2;
IsoId=P04692-4; Sequence=VSP_006581, VSP_006586;
Name=5; Synonyms=Brain TMBr-3;
IsoId=P04692-5; Sequence=VSP_006581, VSP_006585;
Name=6; Synonyms=Fibroblast TM-2;
IsoId=P04692-6; Sequence=VSP_006584;
Note=Ref.5 (AAA42290) sequence is in conflict in position:
275:H->D. {ECO:0000305};
Name=7; Synonyms=Fibroblast 5a;
IsoId=P04692-7; Sequence=VSP_006581, VSP_006584;
Note=Ref.5 (AAA18098) sequence is in conflict in position:
239:H->D. {ECO:0000305};
Name=8; Synonyms=Fibroblast 5b;
IsoId=P04692-8; Sequence=VSP_006581, VSP_006583, VSP_006584;
Note=Ref.5 (AAA18099) sequence is in conflict in position:
239:H->D. {ECO:0000305};
-!- 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; M15474; AAA21801.1; -; Genomic_DNA.
EMBL; M15472; AAA21801.1; JOINED; Genomic_DNA.
EMBL; M15473; AAA21801.1; JOINED; Genomic_DNA.
EMBL; M16432; AAA21801.1; JOINED; Genomic_DNA.
EMBL; M16433; AAA21801.1; JOINED; Genomic_DNA.
EMBL; M18135; AAA21803.1; ALT_TERM; Genomic_DNA.
EMBL; M16432; AAA21803.1; JOINED; Genomic_DNA.
EMBL; M15472; AAA21803.1; JOINED; Genomic_DNA.
EMBL; M16433; AAA21803.1; JOINED; Genomic_DNA.
EMBL; M15473; AAA21803.1; JOINED; Genomic_DNA.
EMBL; M18135; AAA21804.1; -; Genomic_DNA.
EMBL; M16432; AAA21804.1; JOINED; Genomic_DNA.
EMBL; M16433; AAA21804.1; JOINED; Genomic_DNA.
EMBL; M18135; AAA21805.1; -; Genomic_DNA.
EMBL; M16432; AAA21805.1; JOINED; Genomic_DNA.
EMBL; M15472; AAA21805.1; JOINED; Genomic_DNA.
EMBL; M16433; AAA21805.1; JOINED; Genomic_DNA.
EMBL; X02411; CAA26258.1; ALT_SEQ; mRNA.
EMBL; M34135; AAA42252.1; -; mRNA.
EMBL; M34134; AAA42253.1; -; mRNA.
EMBL; M34136; AAA42254.1; -; mRNA.
EMBL; M34137; AAA40773.1; -; Genomic_DNA.
EMBL; M34138; AAA40774.1; -; Genomic_DNA.
EMBL; M60666; AAA42290.1; -; mRNA.
EMBL; M60668; AAA18098.1; -; mRNA.
EMBL; M60669; AAA18099.1; -; mRNA.
EMBL; X02412; CAA26259.1; -; mRNA.
PIR; A34787; A34787.
PIR; A39816; A39816.
PIR; B27407; B27407.
PIR; B34787; B34787.
PIR; C34787; C34787.
PIR; C39816; C39816.
PIR; D39816; D39816.
RefSeq; NP_001029241.1; NM_001034069.1.
RefSeq; NP_001029244.1; NM_001034072.1. [P04692-3]
RefSeq; NP_001029245.1; NM_001034073.1.
RefSeq; NP_001029246.1; NM_001034074.1.
RefSeq; NP_001029247.1; NM_001034075.1.
RefSeq; NP_001288265.1; NM_001301336.1. [P04692-1]
RefSeq; NP_001288665.1; NM_001301736.1. [P04692-5]
RefSeq; NP_062004.1; NM_019131.2. [P04692-4]
UniGene; Rn.87540; -.
PDB; 1IHQ; NMR; -; A/B=206-209.
PDB; 1MV4; NMR; -; A/B=251-284.
PDB; 1TMZ; NMR; -; A/B=1-14.
PDB; 2B9C; X-ray; 2.30 A; A/B=89-208.
PDB; 2G9J; NMR; -; A/B=1-14, C/D=251-284.
PDB; 3AZD; X-ray; 0.98 A; A/B=206-209.
PDBsum; 1IHQ; -.
PDBsum; 1MV4; -.
PDBsum; 1TMZ; -.
PDBsum; 2B9C; -.
PDBsum; 2G9J; -.
PDBsum; 3AZD; -.
ProteinModelPortal; P04692; -.
SMR; P04692; -.
BioGrid; 246968; 4.
DIP; DIP-29020N; -.
IntAct; P04692; 3.
iPTMnet; P04692; -.
PhosphoSitePlus; P04692; -.
SwissPalm; P04692; -.
PRIDE; P04692; -.
Ensembl; ENSRNOT00000024575; ENSRNOP00000024575; ENSRNOG00000018184. [P04692-3]
Ensembl; ENSRNOT00000048044; ENSRNOP00000048499; ENSRNOG00000018184. [P04692-1]
GeneID; 24851; -.
KEGG; rno:24851; -.
CTD; 7168; -.
RGD; 3898; Tpm1.
GeneTree; ENSGT00550000074494; -.
HOVERGEN; HBG107404; -.
InParanoid; P04692; -.
KO; K10373; -.
PhylomeDB; P04692; -.
TreeFam; TF351519; -.
Reactome; R-RNO-390522; Striated Muscle Contraction.
Reactome; R-RNO-445355; Smooth Muscle Contraction.
EvolutionaryTrace; P04692; -.
PRO; PR:P04692; -.
Proteomes; UP000002494; Chromosome 8.
Bgee; ENSRNOG00000018184; Expressed in 10 organ(s), highest expression level in skeletal muscle tissue.
ExpressionAtlas; P04692; baseline and differential.
Genevisible; P04692; RN.
GO; GO:0015629; C:actin cytoskeleton; IDA:UniProtKB.
GO; GO:0005884; C:actin filament; IBA:GO_Central.
GO; GO:0005862; C:muscle thin filament tropomyosin; IBA:GO_Central.
GO; GO:0032991; C:protein-containing complex; IDA:RGD.
GO; GO:0003779; F:actin binding; IDA:RGD.
GO; GO:0051015; F:actin filament binding; IDA:UniProtKB.
GO; GO:0097718; F:disordered domain specific binding; IPI:CAFA.
GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0047485; F:protein N-terminus binding; IDA:RGD.
GO; GO:0008307; F:structural constituent of muscle; IBA:GO_Central.
GO; GO:0051693; P:actin filament capping; IDA:RGD.
GO; GO:0060048; P:cardiac muscle contraction; IDA:RGD.
GO; GO:0006936; P:muscle contraction; TAS:RGD.
GO; GO:0030049; P:muscle filament sliding; IDA:BHF-UCL.
GO; GO:0030336; P:negative regulation of cell migration; IGI:BHF-UCL.
GO; GO:0032781; P:positive regulation of ATPase activity; IDA:BHF-UCL.
GO; GO:0045785; P:positive regulation of cell adhesion; IGI:BHF-UCL.
GO; GO:0051496; P:positive regulation of stress fiber assembly; IGI:BHF-UCL.
GO; GO:0043462; P:regulation of ATPase activity; IDA:RGD.
GO; GO:0031529; P:ruffle organization; IGI:BHF-UCL.
GO; GO:0042060; P:wound healing; IGI:BHF-UCL.
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_0000205624.
COILED 1 284
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:P09493}.
MOD_RES 45 45 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 174 174 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 186 186 Phosphoserine.
{ECO:0000250|UniProtKB:P58771}.
MOD_RES 206 206 Phosphoserine.
{ECO:0000250|UniProtKB:P58771}.
MOD_RES 252 252 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 261 261 Phosphotyrosine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 271 271 Phosphoserine.
{ECO:0000250|UniProtKB:P58771}.
MOD_RES 283 283 Phosphoserine; by DAPK1.
{ECO:0000250|UniProtKB:P09493}.
VAR_SEQ 1 80 MDAIKKKMQMLKLDKENALDRAEQAEADKKAAEDRSKQLED
ELVSLQKKLKGTEDELDKYSEALKDAQEKLELAEKKATD
-> MAGSSSLEAVRRKIRSLQEQADAAEERAGSLQRELDQE
RKLRET (in isoform 4, isoform 5, isoform
7 and isoform 8).
{ECO:0000303|PubMed:2022655,
ECO:0000303|PubMed:2320008}.
/FTId=VSP_006581.
VAR_SEQ 41 80 DELVSLQKKLKGTEDELDKYSEALKDAQEKLELAEKKATD
-> EDISAKEKLLRASEDERDRVLEELHKAEDSLLAADETA
AK (in isoform 2).
{ECO:0000303|PubMed:3838802}.
/FTId=VSP_006582.
VAR_SEQ 189 212 KCAELEEELKTVTNNLKSLEAQAE -> QVRQLEEQLRIMD
QTLKALMAAED (in isoform 8).
{ECO:0000303|PubMed:2022655}.
/FTId=VSP_006583.
VAR_SEQ 258 284 DELYAQKLKYKAISEELDHALNDMTSI -> EKVAHAKEEN
LSMHQMLHQTLLELNNM (in isoform 2, isoform
6, isoform 7 and isoform 8).
{ECO:0000303|PubMed:2022655,
ECO:0000303|PubMed:3838802}.
/FTId=VSP_006584.
VAR_SEQ 259 284 ELYAQKLKYKAISEELDHALNDMTSI -> QLYHQLEQNRR
LTNELKLALNED (in isoform 3 and isoform
5). {ECO:0000303|PubMed:2320008}.
/FTId=VSP_006585.
VAR_SEQ 259 284 ELYAQKLKYKAISEELDHALNDMTSI -> KFLCFSPPKTP
SSSRMSHLSELCICLLSS (in isoform 4).
{ECO:0000303|PubMed:2320008}.
/FTId=VSP_006586.
CONFLICT 52 52 G -> A (in Ref. 4; AAA42252).
{ECO:0000305}.
CONFLICT 279 279 N -> K (in Ref. 2; AAA21801 and 3;
AAA21805). {ECO:0000305}.
HELIX 2 14 {ECO:0000244|PDB:2G9J}.
TURN 95 97 {ECO:0000244|PDB:2B9C}.
HELIX 100 103 {ECO:0000244|PDB:2B9C}.
TURN 104 107 {ECO:0000244|PDB:2B9C}.
HELIX 108 123 {ECO:0000244|PDB:2B9C}.
HELIX 125 209 {ECO:0000244|PDB:2B9C}.
TURN 210 213 {ECO:0000244|PDB:2B9C}.
HELIX 214 225 {ECO:0000244|PDB:2B9C}.
HELIX 254 281 {ECO:0000244|PDB:1MV4}.
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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