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P58771 (TPM1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tropomyosin alpha-1 chain
Alternative name(s):
Alpha-tropomyosin
Tropomyosin-1
Gene names
Name:Tpm1
Synonyms:Tpm-1, Tpma
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length284 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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.

Subunit structure

Heterodimer of an alpha and a beta 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.

Subcellular location

Cytoplasmcytoskeleton.

Induction

Induced in stimulated quiescent cells. Ref.3

Domain

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

Post-translational modification

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

Miscellaneous

The sequences of cardiac and skeletal muscles are identical.

Sequence similarities

Belongs to the tropomyosin family.

Ontologies

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform 1 (identifier: P58771-1)

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.
Isoform 2 (identifier: P58771-2)

Also known as: Fibroblast;

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 284284Tropomyosin alpha-1 chain
PRO_0000205621

Regions

Coiled coil1 – 284284 By similarity

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue2831Phosphoserine; by DAPK1 By similarity
Cross-link77Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.4

Natural variations

Alternative sequence258 – 28427DELYA…DMTSI → EKVAHAKEENLSMHQMLDQT LLELNNM in isoform 2.
VSP_006580

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Skeletal muscle) [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: E25609F597A72F4D

FASTA28432,681
        10         20         30         40         50         60 
MDAIKKKMQM LKLDKENALD RAEQAEADKK AAEDRSKQLE DELVSLQKKL KGTEDELDKY 

        70         80         90        100        110        120 
SEALKDAQEK LELAEKKATD AEADVASLNR RIQLVEEELD RAQERLATAL QKLEEAEKAA 

       130        140        150        160        170        180 
DESERGMKVI ESRAQKDEEK MEIQEIQLKE AKHIAEDADR KYEEVARKLV IIESDLERAE 

       190        200        210        220        230        240 
ERAELSEGKC AELEEELKTV TNNLKSLEAQ AEKYSQKEDK YEEEIKVLSD KLKEAETRAE 

       250        260        270        280 
FAERSVTKLE KSIDDLEDEL YAQKLKYKAI SEELDHALND MTSI 

« Hide

Isoform 2 (Fibroblast) [UniParc].

Checksum: CD755ABFAEA04540
Show »

FASTA28432,709

References

« Hide 'large scale' references
[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]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X64831 mRNA. Translation: CAA46043.1.
M22479 mRNA. Translation: AAA40483.1.
CCDSCCDS23311.1. [P58771-2]
CCDS52845.1. [P58771-1]
PIRA60597. A31380.
RefSeqNP_001157720.1. NM_001164248.1. [P58771-1]
NP_077745.2. NM_024427.4. [P58771-2]
UniGeneMm.121878.

3D structure databases

ProteinModelPortalP58771.
SMRP58771. Positions 8-284.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid204291. 7 interactions.
DIPDIP-300N.
IntActP58771. 9 interactions.
MINTMINT-149814.

PTM databases

PhosphoSiteP58771.

2D gel databases

SWISS-2DPAGEP58771.

Proteomic databases

MaxQBP58771.
PaxDbP58771.
PRIDEP58771.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000113685; ENSMUSP00000109315; ENSMUSG00000032366. [P58771-1]
ENSMUST00000113707; ENSMUSP00000109337; ENSMUSG00000032366. [P58771-2]
GeneID22003.
KEGGmmu:22003.
UCSCuc009qfq.2. mouse. [P58771-1]

Organism-specific databases

CTD7168.
MGIMGI:98809. Tpm1.

Phylogenomic databases

eggNOGNOG304012.
HOGENOMHOG000231521.
HOVERGENHBG107404.
KOK10373.
OrthoDBEOG7673C8.
PhylomeDBP58771.
TreeFamTF351519.

Gene expression databases

ArrayExpressP58771.
BgeeP58771.
CleanExMM_TPM1.
GenevestigatorP58771.

Family and domain databases

InterProIPR000533. Tropomyosin.
[Graphical view]
PfamPF00261. Tropomyosin. 1 hit.
[Graphical view]
PRINTSPR00194. TROPOMYOSIN.
PROSITEPS00326. TROPOMYOSIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTPM1. mouse.
NextBio301732.
PROP58771.
SOURCESearch...

Entry information

Entry nameTPM1_MOUSE
AccessionPrimary (citable) accession number: P58771
Secondary accession number(s): P02558 expand/collapse secondary AC list , P19354, P46902, P99034
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: July 9, 2014
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot