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Protein

Tropomyosin alpha-1 chain

Gene

Tpm1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Binds to actin filaments in muscle and non-muscle cells (PubMed:7568216, PubMed:22812662). Plays a central role, in association with the troponin complex, in the calcium dependent regulation of vertebrate striated muscle contraction (PubMed:22812662). Smooth muscle contraction is regulated by interaction with caldesmon. In non-muscle cells is implicated in stabilizing cytoskeleton actin filaments.2 Publications

GO - Molecular functioni

  • actin binding Source: RGD
  • actin filament binding Source: UniProtKB
  • disordered domain specific binding Source: CAFA
  • identical protein binding Source: UniProtKB
  • protein heterodimerization activity Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • protein N-terminus binding Source: RGD
  • structural constituent of muscle Source: GO_Central

GO - Biological processi

  • actin filament capping Source: RGD
  • cardiac muscle contraction Source: RGD
  • muscle contraction Source: RGD
  • muscle filament sliding Source: BHF-UCL
  • negative regulation of cell migration Source: BHF-UCL
  • positive regulation of ATPase activity Source: BHF-UCL
  • positive regulation of cell adhesion Source: BHF-UCL
  • positive regulation of stress fiber assembly Source: BHF-UCL
  • regulation of ATPase activity Source: RGD
  • ruffle organization Source: BHF-UCL
  • wound healing Source: BHF-UCL

Keywordsi

Molecular functionActin-binding, Muscle protein

Enzyme and pathway databases

ReactomeiR-RNO-390522. Striated Muscle Contraction.
R-RNO-445355. Smooth Muscle Contraction.

Names & Taxonomyi

Protein namesi
Recommended name:
Tropomyosin alpha-1 chain
Alternative name(s):
Alpha-tropomyosin
Tropomyosin-1
Gene namesi
Name:Tpm1
Synonyms:Alpha-tm, Tpma
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 8

Organism-specific databases

RGDi3898. Tpm1.

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_00002056241 – 284Tropomyosin alpha-1 chainAdd BLAST284

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineBy similarity1
Modified residuei45PhosphoserineCombined sources1
Modified residuei53PhosphothreonineBy similarity1
Modified residuei61PhosphoserineBy similarity1
Modified residuei79PhosphothreonineBy similarity1
Modified residuei87PhosphoserineBy similarity1
Modified residuei108PhosphothreonineBy similarity1
Modified residuei174PhosphoserineCombined sources1
Modified residuei186PhosphoserineBy similarity1
Modified residuei206PhosphoserineBy similarity1
Modified residuei215PhosphoserineBy similarity1
Modified residuei252PhosphoserineCombined sources1
Modified residuei261PhosphotyrosineCombined sources1
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

PRIDEiP04692.

PTM databases

iPTMnetiP04692.
PhosphoSitePlusiP04692.

Expressioni

Gene expression databases

BgeeiENSRNOG00000018184.
ExpressionAtlasiP04692. baseline and differential.
GenevisibleiP04692. RN.

Interactioni

Subunit structurei

Homodimer (PubMed:7568216, PubMed:22812662). Heterodimer of an alpha (TPM1, TPM3 or TPM4) and a beta (TPM2) chain (PubMed:7568216, PubMed:22812662). 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 similarity2 Publications

GO - Molecular functioni

  • actin binding Source: RGD
  • actin filament binding Source: UniProtKB
  • disordered domain specific binding Source: CAFA
  • identical protein binding Source: UniProtKB
  • protein heterodimerization activity Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • protein N-terminus binding Source: RGD

Protein-protein interaction databases

BioGridi246968. 4 interactors.
DIPiDIP-29020N.
IntActiP04692. 3 interactors.

Structurei

Secondary structure

1284
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi2 – 14Combined sources13
Turni95 – 97Combined sources3
Helixi100 – 103Combined sources4
Turni104 – 107Combined sources4
Helixi108 – 123Combined sources16
Helixi125 – 208Combined sources84
Helixi254 – 281Combined sources28

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1IHQNMR-A/B206-209[»]
1MV4NMR-A/B251-284[»]
1TMZNMR-A/B1-14[»]
2B9CX-ray2.30A/B89-208[»]
2G9JNMR-A/B1-14[»]
C/D251-284[»]
3AZDX-ray0.98A/B206-209[»]
ProteinModelPortaliP04692.
SMRiP04692.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04692.

Family & Domainsi

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili1 – 284Add 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

GeneTreeiENSGT00550000074494.
HOVERGENiHBG107404.
InParanoidiP04692.
KOiK10373.
PhylomeDBiP04692.
TreeFamiTF351519.

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.

Sequences (8)i

Sequence statusi: Complete.

This entry describes 8 isoformsi produced by alternative splicing. AlignAdd to basket

Note: Additional isoforms seem to exist.
Isoform 1 (identifier: P04692-1) [UniParc]FASTAAdd to basket
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.

« 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:April 4, 2006 - v3
Checksum:iE25609F597A72F4D
GO
Isoform 2 (identifier: P04692-2) [UniParc]FASTAAdd to basket
Also known as: Smooth muscle

The sequence of this isoform differs from the canonical sequence as follows:
     41-80: DELVSLQKKL...LELAEKKATD → EDISAKEKLL...LLAADETAAK
     258-284: DELYAQKLKYKAISEELDHALNDMTSI → EKVAHAKEENLSMHQMLHQTLLELNNM

Show »
Length:284
Mass (Da):32,676
Checksum:i35056246C3FFA678
GO
Isoform 3 (identifier: P04692-3) [UniParc]FASTAAdd to basket
Also known as: Brain TMBr-1

The sequence of this isoform differs from the canonical sequence as follows:
     259-284: ELYAQKLKYKAISEELDHALNDMTSI → QLYHQLEQNRRLTNELKLALNED

Show »
Length:281
Mass (Da):32,495
Checksum:iE8CA06AF0B96E230
GO
Isoform 4 (identifier: P04692-4) [UniParc]FASTAAdd to basket
Also known as: Brain TMBr-2

The sequence of this isoform differs from the canonical sequence as follows:
     1-80: MDAIKKKMQM...LELAEKKATD → MAGSSSLEAV...LDQERKLRET
     259-284: ELYAQKLKYKAISEELDHALNDMTSI → KFLCFSPPKTPSSSRMSHLSELCICLLSS

Show »
Length:251
Mass (Da):28,704
Checksum:iC361AFDF972CC474
GO
Isoform 5 (identifier: P04692-5) [UniParc]FASTAAdd to basket
Also known as: Brain TMBr-3

The sequence of this isoform differs from the canonical sequence as follows:
     1-80: MDAIKKKMQM...LELAEKKATD → MAGSSSLEAV...LDQERKLRET
     259-284: ELYAQKLKYKAISEELDHALNDMTSI → QLYHQLEQNRRLTNELKLALNED

Show »
Length:245
Mass (Da):28,343
Checksum:iFD9E17F1B920550F
GO
Isoform 6 (identifier: P04692-6) [UniParc]FASTAAdd to basket
Also known as: Fibroblast TM-2

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

Show »
Length:284
Mass (Da):32,731
Checksum:iCD7A66BFAEA04540
GO
Isoform 7 (identifier: P04692-7) [UniParc]FASTAAdd to basket
Also known as: Fibroblast 5a

The sequence of this isoform differs from the canonical sequence as follows:
     1-80: MDAIKKKMQM...LELAEKKATD → MAGSSSLEAV...LDQERKLRET
     258-284: DELYAQKLKYKAISEELDHALNDMTSI → EKVAHAKEENLSMHQMLHQTLLELNNM

Show »
Length:248
Mass (Da):28,579
Checksum:i3D2B523AFAB11BF2
GO
Isoform 8 (identifier: P04692-8) [UniParc]FASTAAdd to basket
Also known as: Fibroblast 5b

The sequence of this isoform differs from the canonical sequence as follows:
     1-80: MDAIKKKMQM...LELAEKKATD → MAGSSSLEAV...LDQERKLRET
     189-212: KCAELEEELKTVTNNLKSLEAQAE → QVRQLEEQLRIMDQTLKALMAAED
     258-284: DELYAQKLKYKAISEELDHALNDMTSI → EKVAHAKEENLSMHQMLHQTLLELNNM

Show »
Length:248
Mass (Da):28,718
Checksum:i1AC7D77131E5F251
GO

Sequence cautioni

Isoform 2: The sequence CAA26258 differs from that shown. miscellaneous discrepancyCurated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti52G → A in AAA42252 (PubMed:2320008).Curated1
Sequence conflicti279N → K in AAA21801 (PubMed:3558368).Curated1
Sequence conflicti279N → K in AAA21805 (PubMed:3352602).Curated1
Isoform 7 (identifier: P04692-7)
Sequence conflicti239H → D in AAA18098 (PubMed:2022655).Curated1
Isoform 8 (identifier: P04692-8)
Sequence conflicti239H → D in AAA18099 (PubMed:2022655).Curated1
Isoform 2 (identifier: P04692-2)
Sequence conflicti260V → G in CAA26258 (PubMed:3838802).Curated1
Sequence conflicti275H → D in CAA26258 (PubMed:3838802).Curated1
Isoform 6 (identifier: P04692-6)
Sequence conflicti275H → D in AAA42290 (PubMed:2022655).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0065811 – 80MDAIK…KKATD → MAGSSSLEAVRRKIRSLQEQ ADAAEERAGSLQRELDQERK LRET in isoform 4, isoform 5, isoform 7 and isoform 8. 2 PublicationsAdd BLAST80
Alternative sequenceiVSP_00658241 – 80DELVS…KKATD → EDISAKEKLLRASEDERDRV LEELHKAEDSLLAADETAAK in isoform 2. 1 PublicationAdd BLAST40
Alternative sequenceiVSP_006583189 – 212KCAEL…EAQAE → QVRQLEEQLRIMDQTLKALM AAED in isoform 8. 1 PublicationAdd BLAST24
Alternative sequenceiVSP_006584258 – 284DELYA…DMTSI → EKVAHAKEENLSMHQMLHQT LLELNNM in isoform 2, isoform 6, isoform 7 and isoform 8. 2 PublicationsAdd BLAST27
Alternative sequenceiVSP_006585259 – 284ELYAQ…DMTSI → QLYHQLEQNRRLTNELKLAL NED in isoform 3 and isoform 5. 1 PublicationAdd BLAST26
Alternative sequenceiVSP_006586259 – 284ELYAQ…DMTSI → KFLCFSPPKTPSSSRMSHLS ELCICLLSS in isoform 4. 1 PublicationAdd BLAST26

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M15474
, M15472, M15473, M16432, M16433 Genomic DNA. Translation: AAA21801.1.
M18135
, M16432, M15472, M16433, M15473 Genomic DNA. Translation: AAA21803.1. Different termination.
M18135, M16432, M16433 Genomic DNA. Translation: AAA21804.1.
M18135
, M16432, M15472, M16433 Genomic DNA. Translation: AAA21805.1.
X02411 mRNA. Translation: CAA26258.1. Sequence problems.
M34135 mRNA. Translation: AAA42252.1.
M34134 mRNA. Translation: AAA42253.1.
M34136 mRNA. Translation: AAA42254.1.
M34137 Genomic DNA. Translation: AAA40773.1.
M34138 Genomic DNA. Translation: AAA40774.1.
M60666 mRNA. Translation: AAA42290.1.
M60668 mRNA. Translation: AAA18098.1.
M60669 mRNA. Translation: AAA18099.1.
X02412 mRNA. Translation: CAA26259.1.
PIRiA34787.
A39816.
B27407.
B34787.
C34787.
C39816.
D39816.
RefSeqiNP_001029241.1. NM_001034069.1.
NP_001029244.1. NM_001034072.1. [P04692-3]
NP_001029245.1. NM_001034073.1.
NP_001029246.1. NM_001034074.1.
NP_001029247.1. NM_001034075.1.
NP_001288265.1. NM_001301336.1. [P04692-1]
NP_001288665.1. NM_001301736.1. [P04692-5]
NP_062004.1. NM_019131.2. [P04692-4]
UniGeneiRn.87540.

Genome annotation databases

EnsembliENSRNOT00000024575; ENSRNOP00000024575; ENSRNOG00000018184. [P04692-3]
ENSRNOT00000048044; ENSRNOP00000048499; ENSRNOG00000018184. [P04692-1]
GeneIDi24851.
KEGGirno:24851.

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Entry informationi

Entry nameiTPM1_RAT
AccessioniPrimary (citable) accession number: P04692
Secondary accession number(s): P06469
, P18342, P18343, P18344, P19354, Q53X09, Q63582, Q63608, Q63609
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: April 4, 2006
Last modified: October 25, 2017
This is version 156 of the entry and version 3 of the sequence. See 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