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P58772 (TPM1_RABIT) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 83. 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:TPMA
OrganismOryctolagus cuniculus (Rabbit) [Reference proteome]
Taxonomic identifier9986 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus

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.

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. Ref.5

Sequence similarities

Belongs to the tropomyosin family.

Ontologies

Keywords
   Cellular componentCytoplasm
Cytoskeleton
   Coding sequence diversityAlternative splicing
   DomainCoiled coil
   LigandActin-binding
   Molecular functionMuscle protein
   PTMAcetylation
Isopeptide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-KW

cytoskeleton

Inferred from electronic annotation. Source: UniProtKB-SubCell

Complete GO annotation...

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms may be produced.
Isoform 1 (identifier: P58772-1)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 284284Tropomyosin alpha-1 chain
PRO_0000205623

Regions

Coiled coil1 – 284284 By similarity

Amino acid modifications

Modified residue11N-acetylmethionine Ref.3
Modified residue2831Phosphoserine; by DAPK1 Ref.5
Cross-link77Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Secondary structure

..... 284
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [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

References

[1]"The amino acid sequence of rabbit skeletal alpha-tropomyosin. The NH2-terminal half and complete sequence."
Stone D., Smillie L.B.
J. Biol. Chem. 253:1137-1148(1978) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE.
Tissue: Skeletal muscle.
[2]"The amino acid sequence of rabbit cardiac tropomyosin."
Lewis W.G., Smillie L.B.
J. Biol. Chem. 255:6854-6859(1980) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE.
Tissue: Heart muscle.
[3]"Rabbit skeletal muscle alpha alpha-tropomyosin expressed in baculovirus-infected insect cells possesses the authentic N-terminus structure and functions."
Kluwe L., Maeda K., Miegel A., Fujita-Becker S., Maeda Y., Talbo G., Houthaeve T., Kellner R.
J. Muscle Res. Cell Motil. 16:103-110(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: New Zealand white.
Tissue: Skeletal muscle.
[4]"A new troponin T and cDNA clones for 13 different muscle proteins, found by shotgun sequencing."
Putney S.D., Herlihy W.C., Schimmel P.R.
Nature 302:718-721(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 103-146.
[5]"Specific phosphorylation at serine-283 of alpha tropomyosin from frog skeletal and rabbit skeletal and cardiac muscle."
Mak A.S., Smillie L.B., Barany M.
Proc. Natl. Acad. Sci. U.S.A. 75:3588-3592(1978) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-283.
Tissue: Skeletal muscle.
[6]"Construction of an atomic model for tropomyosin and implications for interactions with actin."
Phillips G.N. Jr.
J. Mol. Biol. 192:128-131(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (15 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
S78854 mRNA. Translation: AAB34957.1.
V00892 mRNA. Translation: CAA24257.1.
PIRTMRBA. I47056.
RefSeqNP_001099158.1. NM_001105688.1.
UniGeneOcu.3324.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2D3EX-ray2.60A/B/C/D176-284[»]
2EFRX-ray1.80A/B/C/D176-273[»]
2EFSX-ray2.00A/B/C/D176-273[»]
2TMAX-ray15.00A/B1-284[»]
2W49electron microscopy35.00A/B/C/T/U/V/W/X8-284[»]
2W4Uelectron microscopy35.00A/B/C/T/U/V/W/X8-284[»]
2Z5HX-ray2.89A/B/C/D/E/F/G/H254-284[»]
I1-24[»]
2Z5IX-ray2.10A/B/C/D/E/F/G/H254-284[»]
I/J1-24[»]
4A7Felectron microscopy7.70B/H98-233[»]
4A7Helectron microscopy7.80B/H98-233[»]
4A7Lelectron microscopy8.10B/H98-233[»]
ProteinModelPortalP58772.
SMRP58772. Positions 8-284.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid1172720. 1 interaction.
DIPDIP-46098N.
IntActP58772. 2 interactions.
MINTMINT-1500045.

Proteomic databases

PRIDEP58772.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100125989.

Phylogenomic databases

eggNOGNOG304012.
HOGENOMHOG000231521.
HOVERGENHBG107404.
OrthoDBEOG7673C8.

Family and domain databases

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

Other

EvolutionaryTraceP58772.
PMAP-CutDBP58772.

Entry information

Entry nameTPM1_RABIT
AccessionPrimary (citable) accession number: P58772
Secondary accession number(s): P02558, P46902, P99034
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: February 19, 2014
This is version 83 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references