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Protein

Tropomyosin alpha-1 chain

Gene

Tpm1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.

GO - Molecular functioni

  • structural constituent of cytoskeleton Source: MGI

GO - Biological processi

  • cardiac muscle contraction Source: BHF-UCL
  • cellular response to reactive oxygen species Source: Ensembl
  • in utero embryonic development Source: MGI
  • positive regulation of heart rate by epinephrine Source: BHF-UCL
  • sarcomere organization Source: Ensembl
  • ventricular cardiac muscle tissue morphogenesis Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Muscle protein

Keywords - Ligandi

Actin-binding

Enzyme and pathway databases

ReactomeiREACT_324232. Smooth Muscle Contraction.
REACT_324616. Striated Muscle Contraction.

Names & Taxonomyi

Protein namesi
Recommended name:
Tropomyosin alpha-1 chain
Alternative name(s):
Alpha-tropomyosin
Tropomyosin-1
Gene namesi
Name:Tpm1
Synonyms:Tpm-1, Tpma
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:98809. Tpm1.

Subcellular locationi

GO - Cellular componenti

  • bleb Source: Ensembl
  • cytoplasm Source: MGI
  • muscle thin filament tropomyosin Source: MGI
  • myofibril Source: MGI
  • ruffle membrane Source: Ensembl
  • stress fiber Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 284284Tropomyosin alpha-1 chainPRO_0000205621Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei53 – 531PhosphothreonineBy similarity
Modified residuei61 – 611PhosphoserineBy similarity
Cross-linki77 – 77Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei79 – 791PhosphothreonineBy similarity
Modified residuei108 – 1081PhosphothreonineBy similarity
Modified residuei174 – 1741PhosphoserineBy similarity
Modified residuei206 – 2061PhosphoserineBy similarity
Modified residuei282 – 2821PhosphothreonineBy similarity
Modified residuei283 – 2831Phosphoserine; by DAPK1By similarity

Post-translational modificationi

Phosphorylated at Ser-283 by DAPK1 in response to oxidative stress and this phosphorylation enhances stress fiber formation in endothelial cells.By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP58771.
PaxDbiP58771.
PRIDEiP58771.

2D gel databases

SWISS-2DPAGEP58771.

PTM databases

PhosphoSiteiP58771.

Expressioni

Inductioni

Induced in stimulated quiescent cells.1 Publication

Gene expression databases

BgeeiP58771.
CleanExiMM_TPM1.
ExpressionAtlasiP58771. baseline and differential.
GenevisibleiP58771. MM.

Interactioni

Subunit structurei

Heterodimer of an alpha and a beta chain. 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

Protein-protein interaction databases

BioGridi204291. 7 interactions.
DIPiDIP-300N.
IntActiP58771. 10 interactions.
MINTiMINT-149814.

Structurei

3D structure databases

ProteinModelPortaliP58771.
SMRiP58771. Positions 8-284.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili1 – 284284By similarityAdd
BLAST

Domaini

The molecule is in a coiled coil structure that is formed by 2 polypeptide chains. The sequence exhibits a prominent seven-residues periodicity.

Sequence similaritiesi

Belongs to the tropomyosin family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG304012.
GeneTreeiENSGT00550000074494.
HOGENOMiHOG000231521.
HOVERGENiHBG107404.
InParanoidiP58771.
KOiK10373.
OrthoDBiEOG7673C8.
PhylomeDBiP58771.
TreeFamiTF351519.

Family and domain databases

InterProiIPR000533. Tropomyosin.
[Graphical view]
PfamiPF00261. Tropomyosin. 1 hit.
[Graphical view]
PRINTSiPR00194. TROPOMYOSIN.
PROSITEiPS00326. TROPOMYOSIN. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Note: Additional isoforms seem to exist.

Isoform 1 (identifier: P58771-1) [UniParc]FASTAAdd to basket

Also known as: Skeletal muscle

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MDAIKKKMQM LKLDKENALD RAEQAEADKK AAEDRSKQLE DELVSLQKKL
60 70 80 90 100
KGTEDELDKY SEALKDAQEK LELAEKKATD AEADVASLNR RIQLVEEELD
110 120 130 140 150
RAQERLATAL QKLEEAEKAA DESERGMKVI ESRAQKDEEK MEIQEIQLKE
160 170 180 190 200
AKHIAEDADR KYEEVARKLV IIESDLERAE ERAELSEGKC AELEEELKTV
210 220 230 240 250
TNNLKSLEAQ AEKYSQKEDK YEEEIKVLSD KLKEAETRAE FAERSVTKLE
260 270 280
KSIDDLEDEL YAQKLKYKAI SEELDHALND MTSI
Length:284
Mass (Da):32,681
Last modified:July 21, 1986 - v1
Checksum:iE25609F597A72F4D
GO
Isoform 2 (identifier: P58771-2) [UniParc]FASTAAdd to basket

Also known as: Fibroblast

The sequence of this isoform differs from the canonical sequence as follows:
     258-284: DELYAQKLKYKAISEELDHALNDMTSI → EKVAHAKEENLSMHQMLDQTLLELNNM

Show »
Length:284
Mass (Da):32,709
Checksum:iCD755ABFAEA04540
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei258 – 28427DELYA…DMTSI → EKVAHAKEENLSMHQMLDQT LLELNNM in isoform 2. 1 PublicationVSP_006580Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X64831 mRNA. Translation: CAA46043.1.
M22479 mRNA. Translation: AAA40483.1.
CCDSiCCDS23311.1. [P58771-2]
CCDS52845.1. [P58771-1]
PIRiA31380. A60597.
RefSeqiNP_001157720.1. NM_001164248.1. [P58771-1]
NP_077745.2. NM_024427.4. [P58771-2]
UniGeneiMm.121878.

Genome annotation databases

EnsembliENSMUST00000113685; ENSMUSP00000109315; ENSMUSG00000032366. [P58771-1]
GeneIDi22003.
KEGGimmu:22003.
UCSCiuc009qfq.2. mouse. [P58771-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X64831 mRNA. Translation: CAA46043.1.
M22479 mRNA. Translation: AAA40483.1.
CCDSiCCDS23311.1. [P58771-2]
CCDS52845.1. [P58771-1]
PIRiA31380. A60597.
RefSeqiNP_001157720.1. NM_001164248.1. [P58771-1]
NP_077745.2. NM_024427.4. [P58771-2]
UniGeneiMm.121878.

3D structure databases

ProteinModelPortaliP58771.
SMRiP58771. Positions 8-284.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi204291. 7 interactions.
DIPiDIP-300N.
IntActiP58771. 10 interactions.
MINTiMINT-149814.

PTM databases

PhosphoSiteiP58771.

2D gel databases

SWISS-2DPAGEP58771.

Proteomic databases

MaxQBiP58771.
PaxDbiP58771.
PRIDEiP58771.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000113685; ENSMUSP00000109315; ENSMUSG00000032366. [P58771-1]
GeneIDi22003.
KEGGimmu:22003.
UCSCiuc009qfq.2. mouse. [P58771-1]

Organism-specific databases

CTDi7168.
MGIiMGI:98809. Tpm1.

Phylogenomic databases

eggNOGiNOG304012.
GeneTreeiENSGT00550000074494.
HOGENOMiHOG000231521.
HOVERGENiHBG107404.
InParanoidiP58771.
KOiK10373.
OrthoDBiEOG7673C8.
PhylomeDBiP58771.
TreeFamiTF351519.

Enzyme and pathway databases

ReactomeiREACT_324232. Smooth Muscle Contraction.
REACT_324616. Striated Muscle Contraction.

Miscellaneous databases

ChiTaRSiTpm1. mouse.
NextBioi301732.
PROiP58771.
SOURCEiSearch...

Gene expression databases

BgeeiP58771.
CleanExiMM_TPM1.
ExpressionAtlasiP58771. baseline and differential.
GenevisibleiP58771. MM.

Family and domain databases

InterProiIPR000533. Tropomyosin.
[Graphical view]
PfamiPF00261. Tropomyosin. 1 hit.
[Graphical view]
PRINTSiPR00194. TROPOMYOSIN.
PROSITEiPS00326. TROPOMYOSIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Subtractive cDNA cloning as a tool to analyse secondary effects of a muscle disease. Characterization of affected genes in the myotonic ADR mouse."
    Schleef M., Zuehlke C., Schoeffl F., Jockusch H.
    Neuromuscul. Disord. 4:205-217(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Strain: A2G.
    Tissue: Fast-twitch skeletal muscle.
  2. "Isolation and characterization of a cDNA that encodes mouse fibroblast tropomyosin isoform 2."
    Takenaga K., Nakamura Y., Tokunaga K., Kageyama H., Sakiyama S.
    Mol. Cell. Biol. 8:5561-5565(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
  3. "Coordinate induction of fibronectin, fibronectin receptor, tropomyosin, and actin genes in serum-stimulated fibroblasts."
    Ryseck R.P., MacDonald-Bravo H., Zerial M., Bravo R.
    Exp. Cell Res. 180:537-545(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  4. "A proteomics approach to identify the ubiquitinated proteins in mouse heart."
    Jeon H.B., Choi E.S., Yoon J.H., Hwang J.H., Chang J.W., Lee E.K., Choi H.W., Park Z.-Y., Yoo Y.J.
    Biochem. Biophys. Res. Commun. 357:731-736(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-77.
    Tissue: Heart.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiTPM1_MOUSE
AccessioniPrimary (citable) accession number: P58771
Secondary accession number(s): P02558
, P19354, P46902, P99034
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: July 22, 2015
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

The sequences of cardiac and skeletal muscles are identical.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.