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Protein

Tropomyosin alpha-1 chain

Gene

TPM1

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: -Experimental evidence at transcript 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.By similarity

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionActin-binding, Muscle protein

Names & Taxonomyi

Protein namesi
Recommended name:
Tropomyosin alpha-1 chain
Alternative name(s):
Alpha-tropomyosin
Tropomyosin-1
Gene namesi
Name:TPM1
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Unplaced

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002837161 – 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 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 DAPK1By similarity1

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

PaxDbiQ5KR49
PeptideAtlasiQ5KR49
PRIDEiQ5KR49

Interactioni

Subunit structurei

Homodimer. Heterodimer of an alpha (TPM1, TPM3 or TPM4) and a beta (TPM2) chain. Interacts with HRG (via the HRR domain); the interaction contributes to the antiangiogenic properties of the histidine/proline-rich region (HRR) of HRG. Interacts (via N-terminus) with LMOD2 (via N-terminus) and TMOD1 (via N-terminus).By similarity

GO - Molecular functioni

Protein-protein interaction databases

IntActiQ5KR49, 3 interactors
MINTiQ5KR49
STRINGi9913.ENSBTAP00000042255

Structurei

3D structure databases

ProteinModelPortaliQ5KR49
SMRiQ5KR49
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

HOGENOMiHOG000231521
HOVERGENiHBG107404
InParanoidiQ5KR49
KOiK10373

Family and domain databases

InterProiView protein in InterPro
IPR000533 Tropomyosin
PfamiView protein in Pfam
PF00261 Tropomyosin, 1 hit
PRINTSiPR00194 TROPOMYOSIN
PROSITEiView protein in PROSITE
PS00326 TROPOMYOSIN, 1 hit

Sequencei

Sequence statusi: Complete.

Q5KR49-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDAIKKKMQM LKLDKENALD RAEQAEADKK AAEDRSKQLE DELVSLQKKL
60 70 80 90 100
KATEDELDKY 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):32,695
Last modified:February 15, 2005 - v1
Checksum:i18DBC129191DC4E3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB198070 mRNA Translation: BAD86590.1
BC102909 mRNA Translation: AAI02910.1
RefSeqiNP_001013608.1, NM_001013590.2
UniGeneiBt.109484

Genome annotation databases

GeneIDi281544
KEGGibta:281544

Similar proteinsi

Entry informationi

Entry nameiTPM1_BOVIN
AccessioniPrimary (citable) accession number: Q5KR49
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: February 15, 2005
Last modified: February 28, 2018
This is version 85 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
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Main funding by: National Institutes of Health