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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
  • negative regulation of vascular associated smooth muscle cell migration Source: Ensembl
  • negative regulation of vascular smooth muscle cell proliferation Source: Ensembl
  • positive regulation of heart rate by epinephrine Source: BHF-UCL
  • regulation of cell shape Source: Ensembl
  • 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

ReactomeiR-MMU-390522. Striated Muscle Contraction.
R-MMU-445355. Smooth 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
Proteomesi
  • UP000000589 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)DescriptionActionsGraphical viewLength
ChainiPRO_00002056211 – 284Tropomyosin alpha-1 chainAdd BLAST284

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineBy similarity1
Modified residuei45PhosphoserineBy similarity1
Modified residuei53PhosphothreonineBy similarity1
Modified residuei61PhosphoserineBy similarity1
Modified residuei79PhosphothreonineBy similarity1
Modified residuei87PhosphoserineBy similarity1
Modified residuei108PhosphothreonineBy similarity1
Modified residuei174PhosphoserineCombined sources1
Modified residuei186PhosphoserineCombined sources1
Modified residuei206PhosphoserineCombined sources1
Modified residuei215PhosphoserineBy similarity1
Modified residuei252PhosphoserineCombined sources1
Modified residuei261PhosphotyrosineBy similarity1
Modified residuei271PhosphoserineCombined sources1
Modified residuei282PhosphothreonineBy similarity1
Modified residuei283PhosphoserineCombined sources1

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, Phosphoprotein

Proteomic databases

PeptideAtlasiP58771.
PRIDEiP58771.

2D gel databases

SWISS-2DPAGEP58771.

PTM databases

iPTMnetiP58771.
PhosphoSitePlusiP58771.

Expressioni

Inductioni

Induced in stimulated quiescent cells.1 Publication

Gene expression databases

BgeeiENSMUSG00000032366.
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). Interacts (via N-terminus) with LMOD2 (via N-terminus) and TMOD1 (via N-terminus) (By similarity).By similarity

Protein-protein interaction databases

BioGridi204291. 103 interactors.
DIPiDIP-300N.
IntActiP58771. 107 interactors.
MINTiMINT-149814.

Structurei

3D structure databases

ProteinModelPortaliP58771.
SMRiP58771.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili1 – 284By similarityAdd BLAST284

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

GeneTreeiENSGT00550000074494.
HOGENOMiHOG000231521.
HOVERGENiHBG107404.
InParanoidiP58771.
KOiK10373.
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)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_006580258 – 284DELYA…DMTSI → EKVAHAKEENLSMHQMLDQT LLELNNM in isoform 2. 1 PublicationAdd BLAST27

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]
ENSMUST00000113707; ENSMUSP00000109337; ENSMUSG00000032366. [P58771-2]
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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi204291. 103 interactors.
DIPiDIP-300N.
IntActiP58771. 107 interactors.
MINTiMINT-149814.

PTM databases

iPTMnetiP58771.
PhosphoSitePlusiP58771.

2D gel databases

SWISS-2DPAGEP58771.

Proteomic databases

PeptideAtlasiP58771.
PRIDEiP58771.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000113685; ENSMUSP00000109315; ENSMUSG00000032366. [P58771-1]
ENSMUST00000113707; ENSMUSP00000109337; ENSMUSG00000032366. [P58771-2]
GeneIDi22003.
KEGGimmu:22003.
UCSCiuc009qfq.2. mouse. [P58771-1]

Organism-specific databases

CTDi7168.
MGIiMGI:98809. Tpm1.

Phylogenomic databases

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

Enzyme and pathway databases

ReactomeiR-MMU-390522. Striated Muscle Contraction.
R-MMU-445355. Smooth Muscle Contraction.

Miscellaneous databases

ChiTaRSiTpm1. mouse.
PROiP58771.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000032366.
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...

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: November 30, 2016
This is version 124 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

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 one 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.