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P04268 (TPM1_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 109. 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·Interactions·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
OrganismGallus gallus (Chicken) [Reference proteome]
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus

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 By similarity. Interacts with HRG (via the HRR domain); the interaction contributes to the antiangiogenic properties of the histidine/proline-rich region (HRR) of HRG. Ref.9 Ref.10

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.

Sequence similarities

Belongs to the tropomyosin family.

Ontologies

Keywords
   Cellular componentCytoplasm
Cytoskeleton
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCoiled coil
   LigandActin-binding
   Molecular functionMuscle protein
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-KW

cytoskeleton

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionprotein binding

Inferred from physical interaction Ref.10. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Smtnl1Q99LM33EBI-8073544,EBI-8073484From a different organism.

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform 1 (identifier: P04268-1)

Also known as: Fast-twitch skeletal muscle; CTm7;

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: P04268-2)

Also known as: Smooth muscle;

The sequence of this isoform differs from the canonical sequence as follows:
     42-80: ELVALQKKLK...LELADKKATD → DIVQLEKQLR...LLFAEENAAK
     258-284: DELYAQKLKYKAISEELDHALNDMTSI → EKVAHAKEENLNMHQMLDQTLLELNNM
Isoform 4 (identifier: P04268-4)

Also known as: Fibroblast F1;

The sequence of this isoform differs from the canonical sequence as follows:
     189-212: KCAELEEELKTVTNNLKSLEAQAE → QVRQLEEQLRIMDQTLKALMAAED
     258-284: DELYAQKLKYKAISEELDHALNDMTSI → EKVAHAKEENLNMHQMLDQTLLELNNM
Isoform 5 (identifier: P04268-5)

Also known as: Fibroblast F2;

The sequence of this isoform differs from the canonical sequence as follows:
     258-284: DELYAQKLKYKAISEELDHALNDMTSI → EKVAHAKEENLNMHQMLDQTLLELNNM
Isoform 6 (identifier: P04268-6)

Also known as: Brain major;

The sequence of this isoform differs from the canonical sequence as follows:
     1-80: MDAIKKKMQM...LELADKKATD → MAALSSLEAV...VDQERALREE
     259-284: ELYAQKLKYKAISEELDHALNDMTSI → QLYQQLEQNSRLTNELKLALNED
Isoform 7 (identifier: P04268-7)

Also known as: Brain minor;

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 284284Tropomyosin alpha-1 chain
PRO_0000205625

Regions

Coiled coil1 – 284284 By similarity

Amino acid modifications

Modified residue11N-acetylmethionine

Natural variations

Alternative sequence1 – 8080MDAIK…KKATD → MAALSSLEAVRKKIRSLQEQ ADAAEERAGKLQREVDQERA LREE in isoform 6.
VSP_006587
Alternative sequence42 – 8039ELVAL…KKATD → DIVQLEKQLRVTEDSRDQVL EELHKSEDSLLFAEENAAK in isoform 2.
VSP_006588
Alternative sequence189 – 21224KCAEL…EAQAE → QVRQLEEQLRIMDQTLKALM AAED in isoform 4.
VSP_006589
Alternative sequence258 – 28427DELYA…DMTSI → EKVAHAKEENLNMHQMLDQT LLELNNM in isoform 2, isoform 4 and isoform 5.
VSP_006590
Alternative sequence259 – 28426ELYAQ…DMTSI → QLYQQLEQNSRLTNELKLAL NED in isoform 6 and isoform 7.
VSP_006591
Natural variant1711I → V.
Natural variant1751D → E.

Experimental info

Sequence conflict341E → D AA sequence Ref.1
Sequence conflict451A → S AA sequence Ref.1
Sequence conflict631S → A AA sequence Ref.1
Sequence conflict751D → E AA sequence Ref.1
Sequence conflict83 – 842SE → AD AA sequence Ref.1
Sequence conflict1321N → S AA sequence Ref.1
Sequence conflict1571E → D AA sequence Ref.1
Sequence conflict1651V → A in AAA48610. Ref.2
Sequence conflict1721I → L AA sequence Ref.1
Sequence conflict1741G → S AA sequence Ref.1
Sequence conflict1881S → G AA sequence Ref.1
Sequence conflict2291T → S AA sequence Ref.1

Secondary structure

.... 284
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Fast-twitch skeletal muscle) (CTm7) [UniParc].

Last modified August 13, 1987. Version 2.
Checksum: DBBBD3DB7F36DACB

FASTA28432,766
        10         20         30         40         50         60 
MDAIKKKMQM LKLDKENALD RAEQAEADKK AAEERSKQLE DELVALQKKL KGTEDELDKY 

        70         80         90        100        110        120 
SESLKDAQEK LELADKKATD AESEVASLNR RIQLVEEELD RAQERLATAL QKLEEAEKAA 

       130        140        150        160        170        180 
DESERGMKVI ENRAQKDEEK MEIQEIQLKE AKHIAEEADR KYEEVARKLV IIEGDLERAE 

       190        200        210        220        230        240 
ERAELSESKC AELEEELKTV TNNLKSLEAQ AEKYSQKEDK YEEEIKVLTD KLKEAETRAE 

       250        260        270        280 
FAERSVTKLE KSIDDLEDEL YAQKLKYKAI SEELDHALND MTSI 

« Hide

Isoform 2 (Smooth muscle) [UniParc].

Checksum: C29E05F9DEA8F27F
Show »

FASTA28432,926
Isoform 4 (Fibroblast F1) [UniParc].

Checksum: E94405DA8D65597F
Show »

FASTA28432,960
Isoform 5 (Fibroblast F2) [UniParc].

Checksum: CEA880914631B0DC
Show »

FASTA28432,821
Isoform 6 (Brain major) [UniParc].

Checksum: 0F45465ECA0AD748
Show »

FASTA24528,361
Isoform 7 (Brain minor) [UniParc].

Checksum: 862297483A4C684C
Show »

FASTA28132,502

References

« Hide 'large scale' references
[1]"Amino acid sequence of chicken gizzard gamma-tropomyosin."
Lau S.Y.M., Sanders C., Smillie L.B.
J. Biol. Chem. 260:7257-7263(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE (ISOFORM 1).
[2]"Complete nucleotide sequence of the fast-twitch isoform of chicken skeletal muscle alpha-tropomyosin."
Gooding C., Reinach F.C., Macleod A.R.
Nucleic Acids Res. 15:8105-8105(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE (ISOFORM 1).
[3]"The chicken gene encoding the alpha isoform of tropomyosin of fast-twitch muscle fibers: organization, expression and identification of the major proteins synthesized."
Lemonnier M., Balvay L., Mouly V., Libri D., Fiszman M.Y.
Gene 107:229-240(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE (ISOFORMS 1; 2; 4; 5; 6 AND 7).
[4]"Differential regulation of skeletal muscle myosin-II and brush border myosin-I enzymology and mechanochemistry by bacterially produced tropomyosin isoforms."
Fanning A.S., Wolenski J.S., Mooseker M.S., Izant J.G.
Cell Motil. Cytoskeleton 29:29-45(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 4).
Tissue: Body wall.
[5]"Identification, characterization, and expression of a novel alpha-tropomyosin isoform in cardiac tissues in developing chicken."
Denz C.R., Zajdel R.W., Dube S., Dube D.K.
Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Heart and Skeletal muscle.
[6]"Sequence and comparative analysis of the chicken genome provide unique perspectives on vertebrate evolution."
Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P., Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B., Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C., Fulton R.S., Graves T.A. expand/collapse author list , Kremitzki C., Layman D., Magrini V., McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O., Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W., Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D., Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K., Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L., Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B., Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M., Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K., Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E., Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M., Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M., Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S., Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M., Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M., Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A., Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S., Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J., Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J., Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E., Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M., Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A., Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M., Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O., Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E., Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S., Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E., Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R., Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R., Wilson R.K.
Nature 432:695-716(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Red jungle fowl.
[7]"Distinct alpha-tropomyosin mRNA sequences in chicken skeletal muscle."
McLeod A.R.
Eur. J. Biochem. 126:293-297(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 24-284 (ISOFORM 1).
[8]"Chick alpha tropomyosin gene contains three sets of mutually exclusive alternatively spliced exons."
Lemonnier M., Libri D., Fiszman M.Y.
Nucleic Acids Res. 17:5400-5400(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE OF 189-213 (ISOFORM 4).
Tissue: Muscle.
[9]"Peptides derived from the histidine-proline domain of the histidine-proline-rich glycoprotein bind to tropomyosin and have antiangiogenic and antitumor activities."
Donate F., Juarez J.C., Guan X., Shipulina N.V., Plunkett M.L., Tel-Tsur Z., Shaw D.E., Morgan W.T., Mazar A.P.
Cancer Res. 64:5812-5817(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HRG.
[10]"Histidine-proline rich glycoprotein (HPRG) binds and transduces anti-angiogenic signals through cell surface tropomyosin on endothelial cells."
Guan X., Juarez J.C., Qi X., Shipulina N.V., Shaw D.E., Morgan W.T., McCrae K.R., Mazar A.P., Donate F.
Thromb. Haemost. 92:403-412(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HRG.
[11]"Deciphering the design of the tropomyosin molecule."
Brown J.H., Kim K.H., Jun G., Greenfield N.J., Dominguez R., Volkmann N., Hitchcock-DeGregori S.E., Cohen C.
Proc. Natl. Acad. Sci. U.S.A. 98:8496-8501(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-81.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M32441 mRNA. Translation: AAA48610.1.
X57991 expand/collapse EMBL AC list , X57993, X57994, X57995 Genomic DNA. Translation: CAA41056.1.
M69144 expand/collapse EMBL AC list , M69140, M69142, M69143 Genomic DNA. Translation: AAA48577.1.
X16090 Genomic DNA. Translation: CAA34217.1. Sequence problems.
X57991 expand/collapse EMBL AC list , X57993, X57994, X57996 Genomic DNA. Translation: CAA41059.1.
X57991 expand/collapse EMBL AC list , X57993, X57994, X57996 Genomic DNA. Translation: CAA41058.1.
X57991 expand/collapse EMBL AC list , X57993, X57994, X57996 Genomic DNA. Translation: CAA41057.1.
M36336 mRNA. Translation: AAA65120.1.
M36337 mRNA. Translation: AAA65121.1.
AY150210 mRNA. Translation: AAN75276.1.
AADN02040437 Genomic DNA. No translation available.
AADN02040438 Genomic DNA. No translation available.
J00910 mRNA. Translation: AAA49113.1.
PIRTMCHA. S24399.
TMCHS2. S24400.
S24401.
S24402.
RefSeqNP_990732.1. NM_205401.1. [P04268-4]
UniGeneGga.4108.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1IC2X-ray2.00A/B/C/D1-80[»]
3MTUX-ray2.10A/B/C/D1-29[»]
E/F257-284[»]
3MUDX-ray2.20A/B246-257[»]
C/D1-29[»]
3U1AX-ray2.00A/B/C/D1-81[»]
3U1CX-ray1.80A/B1-98[»]
ProteinModelPortalP04268.
SMRP04268. Positions 1-284.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP04268. 1 interaction.

Proteomic databases

PaxDbP04268.
PRIDEP04268.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSGALT00000039589; ENSGALP00000038799; ENSGALG00000003521. [P04268-4]
GeneID396366.
KEGGgga:396366.

Organism-specific databases

CTD7168.

Phylogenomic databases

eggNOGNOG304012.
GeneTreeENSGT00550000074494.
HOVERGENHBG107404.
KOK10373.
OMAEASAEKY.
OrthoDBEOG7673C8.
PhylomeDBP04268.
TreeFamTF351519.

Family and domain databases

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

Other

EvolutionaryTraceP04268.
NextBio20816411.
PROP04268.

Entry information

Entry nameTPM1_CHICK
AccessionPrimary (citable) accession number: P04268
Secondary accession number(s): P02559 expand/collapse secondary AC list , P08942, P18441, P18442, P49436, P49438, P49439, Q540N4
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: August 13, 1987
Last modified: June 11, 2014
This is version 109 of the entry and version 2 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