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Protein

Tropomyosin alpha-1 chain

Gene

TPM1

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed-Annotation score: Annotation score: 4 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.

Keywords - Molecular functioni

Muscle protein

Keywords - Ligandi

Actin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Tropomyosin alpha-1 chain
Alternative name(s):
Alpha-tropomyosin
Tropomyosin-1
Gene namesi
Name:TPM1
Synonyms:TPMA
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
ProteomesiUP000001811 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. cytoskeleton Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 284284Tropomyosin alpha-1 chainPRO_0000205623Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei53 – 531PhosphothreonineBy similarity
Modified residuei61 – 611PhosphoserineBy similarity
Cross-linki77 – 77Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei79 – 791PhosphothreonineBy similarity
Modified residuei108 – 1081PhosphothreonineBy similarity
Modified residuei174 – 1741PhosphoserineBy similarity
Modified residuei206 – 2061PhosphoserineBy similarity
Modified residuei282 – 2821PhosphothreonineBy similarity
Modified residuei283 – 2831Phosphoserine; by DAPK11 Publication

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

PRIDEiP58772.

Miscellaneous databases

PMAP-CutDBP58772.

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

BioGridi1172720. 1 interaction.
DIPiDIP-46098N.
IntActiP58772. 2 interactions.
MINTiMINT-1500045.

Structurei

Secondary structure

1
284
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi2 – 2423Combined sources
Helixi176 – 27398Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP58772.
SMRiP58772. Positions 8-284.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP58772.

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.
HOGENOMiHOG000231521.
HOVERGENiHBG107404.
InParanoidiP58772.
KOiK10373.
OrthoDBiEOG7673C8.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

This entry describes 1 isoform i produced by alternative splicing. AlignAdd to basket

Note: A number of isoforms may be produced.

Isoform 1 (identifier: P58772-1) [UniParc]FASTAAdd to basket

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S78854 mRNA. Translation: AAB34957.1.
V00892 mRNA. Translation: CAA24257.1.
PIRiI47056. TMRBA.
RefSeqiNP_001099158.1. NM_001105688.1. [P58772-1]
UniGeneiOcu.3324.

Genome annotation databases

GeneIDi100125989.
KEGGiocu:100125989.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S78854 mRNA. Translation: AAB34957.1.
V00892 mRNA. Translation: CAA24257.1.
PIRiI47056. TMRBA.
RefSeqiNP_001099158.1. NM_001105688.1. [P58772-1]
UniGeneiOcu.3324.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP58772.
SMRiP58772. Positions 8-284.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi1172720. 1 interaction.
DIPiDIP-46098N.
IntActiP58772. 2 interactions.
MINTiMINT-1500045.

Proteomic databases

PRIDEiP58772.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100125989.
KEGGiocu:100125989.

Organism-specific databases

CTDi7168.

Phylogenomic databases

eggNOGiNOG304012.
HOGENOMiHOG000231521.
HOVERGENiHBG107404.
InParanoidiP58772.
KOiK10373.
OrthoDBiEOG7673C8.

Miscellaneous databases

EvolutionaryTraceiP58772.
PMAP-CutDBP58772.

Family and domain databases

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

Publicationsi

  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(1977) [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(1979) [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(1994) [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(1982) [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(1977) [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(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (15 ANGSTROMS).

Entry informationi

Entry nameiTPM1_RABIT
AccessioniPrimary (citable) accession number: P58772
Secondary accession number(s): P02558, P46902, P99034
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: March 4, 2015
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.