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P04692 (TPM1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 124. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tropomyosin alpha-1 chain
Alternative name(s):
Alpha-tropomyosin
Tropomyosin-1
Gene names
Name:Tpm1
Synonyms:Alpha-tm, Tpma
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length284 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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. Ref.8

Subcellular location

Cytoplasmcytoskeleton.

Domain

The molecule is in a coiled coil structure that is formed by 2 polypeptide chains. The sequence exhibits a prominent seven-residues periodicity.

Post-translational modification

Phosphorylated at Ser-283 by DAPK1 in response to oxidative stress and this phosphorylation enhances stress fiber formation in endothelial cells By similarity.

Sequence similarities

Belongs to the tropomyosin family.

Sequence caution

Isoform 2: The sequence CAA26258.1 differs from that shown. Reason: miscellaneous discrepancy

Alternative products

This entry describes 8 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform 1 (identifier: P04692-1)

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.
Isoform 2 (identifier: P04692-2)

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
Isoform 3 (identifier: P04692-3)

Also known as: Brain TMBr-1;

The sequence of this isoform differs from the canonical sequence as follows:
     259-284: ELYAQKLKYKAISEELDHALNDMTSI → QLYHQLEQNRRLTNELKLALNED
Isoform 4 (identifier: P04692-4)

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
Isoform 5 (identifier: P04692-5)

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
Isoform 6 (identifier: P04692-6)

Also known as: Fibroblast TM-2;

The sequence of this isoform differs from the canonical sequence as follows:
     258-284: DELYAQKLKYKAISEELDHALNDMTSI → EKVAHAKEENLSMHQMLHQTLLELNNM
Isoform 7 (identifier: P04692-7)

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
Isoform 8 (identifier: P04692-8)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 284284Tropomyosin alpha-1 chain
PRO_0000205624

Regions

Coiled coil1 – 284284

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue2831Phosphoserine; by DAPK1 By similarity
Cross-link77Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Natural variations

Alternative sequence1 – 8080MDAIK…KKATD → MAGSSSLEAVRRKIRSLQEQ ADAAEERAGSLQRELDQERK LRET in isoform 4, isoform 5, isoform 7 and isoform 8.
VSP_006581
Alternative sequence41 – 8040DELVS…KKATD → EDISAKEKLLRASEDERDRV LEELHKAEDSLLAADETAAK in isoform 2.
VSP_006582
Alternative sequence189 – 21224KCAEL…EAQAE → QVRQLEEQLRIMDQTLKALM AAED in isoform 8.
VSP_006583
Alternative sequence258 – 28427DELYA…DMTSI → EKVAHAKEENLSMHQMLHQT LLELNNM in isoform 2, isoform 6, isoform 7 and isoform 8.
VSP_006584
Alternative sequence259 – 28426ELYAQ…DMTSI → QLYHQLEQNRRLTNELKLAL NED in isoform 3 and isoform 5.
VSP_006585
Alternative sequence259 – 28426ELYAQ…DMTSI → KFLCFSPPKTPSSSRMSHLS ELCICLLSS in isoform 4.
VSP_006586

Experimental info

Sequence conflict521G → A in AAA42252. Ref.4
Sequence conflict2791N → K in AAA21801. Ref.2
Sequence conflict2791N → K in AAA21805. Ref.3
Isoform 2:
Sequence conflict2601V → G in CAA26258. Ref.1
Sequence conflict2751H → D in CAA26258. Ref.1
Isoform 6:
Sequence conflict2751H → D in AAA42290. Ref.5
Isoform 7:
Sequence conflict2391H → D in AAA18098. Ref.5
Isoform 8:
Sequence conflict2391H → D in AAA18099. Ref.5

Secondary structure

........... 284
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Skeletal muscle) [UniParc].

Last modified April 4, 2006. Version 3.
Checksum: E25609F597A72F4D

FASTA28432,681
        10         20         30         40         50         60 
MDAIKKKMQM LKLDKENALD RAEQAEADKK AAEDRSKQLE DELVSLQKKL KGTEDELDKY 

        70         80         90        100        110        120 
SEALKDAQEK LELAEKKATD AEADVASLNR RIQLVEEELD RAQERLATAL QKLEEAEKAA 

       130        140        150        160        170        180 
DESERGMKVI ESRAQKDEEK MEIQEIQLKE AKHIAEDADR KYEEVARKLV IIESDLERAE 

       190        200        210        220        230        240 
ERAELSEGKC AELEEELKTV TNNLKSLEAQ AEKYSQKEDK YEEEIKVLSD KLKEAETRAE 

       250        260        270        280 
FAERSVTKLE KSIDDLEDEL YAQKLKYKAI SEELDHALND MTSI 

« Hide

Isoform 2 (Smooth muscle) [UniParc].

Checksum: 35056246C3FFA678
Show »

FASTA28432,676
Isoform 3 (Brain TMBr-1) [UniParc].

Checksum: E8CA06AF0B96E230
Show »

FASTA28132,495
Isoform 4 (Brain TMBr-2) [UniParc].

Checksum: C361AFDF972CC474
Show »

FASTA25128,704
Isoform 5 (Brain TMBr-3) [UniParc].

Checksum: FD9E17F1B920550F
Show »

FASTA24528,343
Isoform 6 (Fibroblast TM-2) [UniParc].

Checksum: CD7A66BFAEA04540
Show »

FASTA28432,731
Isoform 7 (Fibroblast 5a) [UniParc].

Checksum: 3D2B523AFAB11BF2
Show »

FASTA24828,579
Isoform 8 (Fibroblast 5b) [UniParc].

Checksum: 1AC7D77131E5F251
Show »

FASTA24828,718

References

[1]"Comparison of alpha-tropomyosin sequences from smooth and striated muscle."
Ruiz-Opazo N., Weinberger J., Nadal-Ginard B.
Nature 315:67-70(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
[2]"Alpha-tropomyosin gene organization. Alternative splicing of duplicated isotype-specific exons accounts for the production of smooth and striated muscle isoforms."
Ruiz-Opazo N., Nadal-Ginard B.
J. Biol. Chem. 262:4755-4765(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING.
[3]"The rat alpha-tropomyosin gene generates a minimum of six different mRNAs coding for striated, smooth, and nonmuscle isoforms by alternative splicing."
Wieczorek D.F., Smith C.W., Nadal-Ginard B.
Mol. Cell. Biol. 8:679-694(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING.
[4]"Three novel brain tropomyosin isoforms are expressed from the rat alpha-tropomyosin gene through the use of alternative promoters and alternative RNA processing."
Lees-Miller J.P., Goodwin L.O., Helfman D.M.
Mol. Cell. Biol. 10:1729-1742(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 3; 4 AND 5).
Tissue: Brain.
[5]"Four fibroblast tropomyosin isoforms are expressed from the rat alpha-tropomyosin gene via alternative RNA splicing and the use of two promoters."
Goodwin L.O., Lees-Miller J.P., Leonard M.A., Cheley S.B., Helfman D.M.
J. Biol. Chem. 266:8408-8415(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 6; 7 AND 8).
[6]"Cloning and characterization of cDNA sequences corresponding to myosin light chains 1, 2, and 3, troponin-C, troponin-T, alpha-tropomyosin, and alpha-actin."
Garfinkel L.I., Periasamy M., Nadal-Ginard B.
J. Biol. Chem. 257:11078-11086(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[7]Lubec G., Afjehi-Sadat L., Diao W., Kang S.U., Lubec S.
Submitted (SEP-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 92-101; 141-149; 218-226 AND 251-270, PARTIAL PROTEIN SEQUENCE (ISOFORMS 4/5/7/8), IDENTIFICATION BY MASS SPECTROMETRY.
Strain: Sprague-Dawley.
Tissue: Brain, Hippocampus and Spinal cord.
[8]"Specificity of dimer formation in tropomyosins: influence of alternatively spliced exons on homodimer and heterodimer assembly."
Gimona M., Watakabe A., Helfman D.M.
Proc. Natl. Acad. Sci. U.S.A. 92:9776-9780(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M15474 expand/collapse EMBL AC list , M15472, M15473, M16432, M16433 Genomic DNA. Translation: AAA21801.1.
M18135 expand/collapse EMBL AC list , M16432, M15472, M16433, M15473 Genomic DNA. Translation: AAA21803.1. Different termination.
M18135, M16432, M16433 Genomic DNA. Translation: AAA21804.1.
M18135 expand/collapse EMBL AC list , 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.
PIRA34787.
A39816.
B27407.
B34787.
C34787.
C39816.
D39816.
RefSeqNP_001029241.1. NM_001034069.1.
NP_001029244.1. NM_001034072.1.
NP_001029245.1. NM_001034073.1.
NP_001029246.1. NM_001034074.1.
NP_001029247.1. NM_001034075.1.
NP_062004.1. NM_019131.2.
XP_006243449.1. XM_006243387.1.
XP_006243456.1. XM_006243394.1.
UniGeneRn.87540.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1IHQNMR-A/B206-209[»]
1MV4NMR-A/B251-284[»]
1TMZNMR-A/B1-14[»]
2B9CX-ray2.30A/B89-207[»]
2G9JNMR-A/B1-14[»]
C/D251-284[»]
3AZDX-ray0.98A/B206-209[»]
ProteinModelPortalP04692.
SMRP04692. Positions 8-284.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid246968. 4 interactions.
DIPDIP-29020N.
IntActP04692. 2 interactions.

PTM databases

PhosphoSiteP04692.

Proteomic databases

PaxDbP04692.
PRIDEP04692.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000024575; ENSRNOP00000024575; ENSRNOG00000018184. [P04692-3]
ENSRNOT00000024617; ENSRNOP00000024617; ENSRNOG00000018184.
ENSRNOT00000048044; ENSRNOP00000048499; ENSRNOG00000018184. [P04692-1]
GeneID24851.
KEGGrno:24851.

Organism-specific databases

CTD7168.
RGD3898. Tpm1.

Phylogenomic databases

eggNOGNOG304012.
GeneTreeENSGT00550000074494.
HOVERGENHBG107404.
KOK10373.
PhylomeDBP04692.
TreeFamTF351519.

Gene expression databases

ArrayExpressP04692.
GenevestigatorP04692.

Family and domain databases

InterProIPR000533. Tropomyosin.
[Graphical view]
PfamPF00261. Tropomyosin. 1 hit.
[Graphical view]
PRINTSPR00194. TROPOMYOSIN.
PROSITEPS00326. TROPOMYOSIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP04692.
NextBio604620.

Entry information

Entry nameTPM1_RAT
AccessionPrimary (citable) accession number: P04692
Secondary accession number(s): P06469 expand/collapse secondary AC list , P18342, P18343, P18344, P19354, Q53X09, Q63582, Q63608, Q63609
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: April 4, 2006
Last modified: April 16, 2014
This is version 124 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references