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Protein

Tropomyosin alpha-1 chain

Gene

Tpm1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -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 residuei174PhosphoserineCombined sources1
Modified residuei186PhosphoserineBy similarity1
Modified residuei206PhosphoserineBy similarity1
Modified residuei252PhosphoserineCombined sources1
Modified residuei261PhosphotyrosineCombined sources1
Modified residuei271PhosphoserineBy 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
SwissPalmiP04692

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 – 209Combined sources85
Turni210 – 213Combined sources4
Helixi214 – 225Combined sources12
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: June 20, 2018
This is version 160 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

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