Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Tropomyosin alpha-1 chain

Gene

TPM1

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed-Annotation score: Annotation score: 3 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
Proteomesi
  • UP000001811 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002056231 – 284Tropomyosin alpha-1 chainAdd BLAST284

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionine3 Publications1
Modified residuei45PhosphoserineBy similarity1
Modified residuei53PhosphothreonineBy similarity1
Modified residuei61PhosphoserineBy similarity1
Modified residuei79PhosphothreonineBy similarity1
Modified residuei87PhosphoserineBy similarity1
Modified residuei108PhosphothreonineBy similarity1
Modified residuei174PhosphoserineBy similarity1
Modified residuei186PhosphoserineBy similarity1
Modified residuei206PhosphoserineBy similarity1
Modified residuei215PhosphoserineBy similarity1
Modified residuei252PhosphoserineBy similarity1
Modified residuei261PhosphotyrosineBy similarity1
Modified residuei271PhosphoserineBy similarity1
Modified residuei282PhosphothreonineBy similarity1
Modified residuei283Phosphoserine; by DAPK11 Publication1

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

PTM databases

iPTMnetiP58772.

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

Protein-protein interaction databases

BioGridi1172720. 1 interactor.
DIPiDIP-46098N.
IntActiP58772. 2 interactors.
MINTiMINT-1500045.

Structurei

Secondary structure

1284
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi2 – 24Combined sources23
Helixi176 – 273Combined sources98

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP58772.

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

HOGENOMiHOG000231521.
HOVERGENiHBG107404.
InParanoidiP58772.
KOiK10373.

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.
Ocu.7353.

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.
Ocu.7353.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi1172720. 1 interactor.
DIPiDIP-46098N.
IntActiP58772. 2 interactors.
MINTiMINT-1500045.

PTM databases

iPTMnetiP58772.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100125989.
KEGGiocu:100125989.

Organism-specific databases

CTDi7168.

Phylogenomic databases

HOGENOMiHOG000231521.
HOVERGENiHBG107404.
InParanoidiP58772.
KOiK10373.

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...

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: November 30, 2016
This is version 99 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

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.