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Protein

Tropomyosin alpha-1 chain

Gene

TPM1

Organism
Gallus gallus (Chicken)
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. 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.

Keywords - Molecular functioni

Muscle protein

Keywords - Ligandi

Actin-binding

Enzyme and pathway databases

ReactomeiREACT_303305. Striated Muscle Contraction.
REACT_327184. Smooth Muscle Contraction.

Names & Taxonomyi

Protein namesi
Recommended name:
Tropomyosin alpha-1 chain
Alternative name(s):
Alpha-tropomyosin
Tropomyosin-1
Gene namesi
Name:TPM1
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
ProteomesiUP000000539 Componenti: Chromosome 10

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 284284Tropomyosin alpha-1 chainPRO_0000205625Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP04268.
PRIDEiP04268.

Expressioni

Gene expression databases

ExpressionAtlasiP04268. baseline.

Interactioni

Subunit structurei

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.By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Smtnl1Q99LM33EBI-8073544,EBI-8073484From a different organism.

Protein-protein interaction databases

IntActiP04268. 1 interaction.

Structurei

Secondary structure

284
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi1 – 9696Combined sources
Helixi257 – 28327Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP04268.
SMRiP04268. Positions 1-284.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04268.

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili1 – 284284By similarityAdd
BLAST

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

eggNOGiNOG304012.
GeneTreeiENSGT00550000074494.
HOVERGENiHBG107404.
InParanoidiP04268.
KOiK10373.
OMAiLTICETE.
OrthoDBiEOG7673C8.
PhylomeDBiP04268.
TreeFamiTF351519.

Family and domain databases

InterProiIPR000533. Tropomyosin.
[Graphical view]
PfamiPF00261. Tropomyosin. 1 hit.
[Graphical view]
PRINTSiPR00194. TROPOMYOSIN.
PROSITEiPS00326. TROPOMYOSIN. 1 hit.
[Graphical view]

Sequences (6)i

Sequence statusi: Complete.

This entry describes 6 isoformsi produced by alternative splicing. AlignAdd to basket

Note: Additional isoforms seem to exist.

Isoform 1 (identifier: P04268-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MDAIKKKMQM LKLDKENALD RAEQAEADKK AAEERSKQLE DELVALQKKL
60 70 80 90 100
KGTEDELDKY SESLKDAQEK LELADKKATD AESEVASLNR RIQLVEEELD
110 120 130 140 150
RAQERLATAL QKLEEAEKAA DESERGMKVI ENRAQKDEEK MEIQEIQLKE
160 170 180 190 200
AKHIAEEADR KYEEVARKLV IIEGDLERAE ERAELSESKC AELEEELKTV
210 220 230 240 250
TNNLKSLEAQ AEKYSQKEDK YEEEIKVLTD KLKEAETRAE FAERSVTKLE
260 270 280
KSIDDLEDEL YAQKLKYKAI SEELDHALND MTSI
Length:284
Mass (Da):32,766
Last modified:August 13, 1987 - v2
Checksum:iDBBBD3DB7F36DACB
GO
Isoform 2 (identifier: P04268-2) [UniParc]FASTAAdd to basket

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

Show »
Length:284
Mass (Da):32,926
Checksum:iC29E05F9DEA8F27F
GO
Isoform 4 (identifier: P04268-4) [UniParc]FASTAAdd to basket

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

Show »
Length:284
Mass (Da):32,960
Checksum:iE94405DA8D65597F
GO
Isoform 5 (identifier: P04268-5) [UniParc]FASTAAdd to basket

Also known as: Fibroblast F2

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

Show »
Length:284
Mass (Da):32,821
Checksum:iCEA880914631B0DC
GO
Isoform 6 (identifier: P04268-6) [UniParc]FASTAAdd to basket

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

Show »
Length:245
Mass (Da):28,361
Checksum:i0F45465ECA0AD748
GO
Isoform 7 (identifier: P04268-7) [UniParc]FASTAAdd to basket

Also known as: Brain minor

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

Show »
Length:281
Mass (Da):32,502
Checksum:i862297483A4C684C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti34 – 341E → D AA sequence (PubMed:3997866).Curated
Sequence conflicti45 – 451A → S AA sequence (PubMed:3997866).Curated
Sequence conflicti63 – 631S → A AA sequence (PubMed:3997866).Curated
Sequence conflicti75 – 751D → E AA sequence (PubMed:3997866).Curated
Sequence conflicti83 – 842SE → AD AA sequence (PubMed:3997866).Curated
Sequence conflicti132 – 1321N → S AA sequence (PubMed:3997866).Curated
Sequence conflicti157 – 1571E → D AA sequence (PubMed:3997866).Curated
Sequence conflicti165 – 1651V → A in AAA48610 (PubMed:3671073).Curated
Sequence conflicti172 – 1721I → L AA sequence (PubMed:3997866).Curated
Sequence conflicti174 – 1741G → S AA sequence (PubMed:3997866).Curated
Sequence conflicti188 – 1881S → G AA sequence (PubMed:3997866).Curated
Sequence conflicti229 – 2291T → S AA sequence (PubMed:3997866).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti171 – 1711I → V.
Natural varianti175 – 1751D → E.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 8080MDAIK…KKATD → MAALSSLEAVRKKIRSLQEQ ADAAEERAGKLQREVDQERA LREE in isoform 6. CuratedVSP_006587Add
BLAST
Alternative sequencei42 – 8039ELVAL…KKATD → DIVQLEKQLRVTEDSRDQVL EELHKSEDSLLFAEENAAK in isoform 2. CuratedVSP_006588Add
BLAST
Alternative sequencei189 – 21224KCAEL…EAQAE → QVRQLEEQLRIMDQTLKALM AAED in isoform 4. 1 PublicationVSP_006589Add
BLAST
Alternative sequencei258 – 28427DELYA…DMTSI → EKVAHAKEENLNMHQMLDQT LLELNNM in isoform 2, isoform 4 and isoform 5. 1 PublicationVSP_006590Add
BLAST
Alternative sequencei259 – 28426ELYAQ…DMTSI → QLYQQLEQNSRLTNELKLAL NED in isoform 6 and isoform 7. CuratedVSP_006591Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M32441 mRNA. Translation: AAA48610.1.
X57991
, X57993, X57994, X57995 Genomic DNA. Translation: CAA41056.1.
M69144
, M69140, M69142, M69143 Genomic DNA. Translation: AAA48577.1.
X16090 Genomic DNA. Translation: CAA34217.1. Sequence problems.
X57991
, X57993, X57994, X57996 Genomic DNA. Translation: CAA41059.1.
X57991
, X57993, X57994, X57996 Genomic DNA. Translation: CAA41058.1.
X57991
, 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.
PIRiS24399. TMCHA.
S24400. TMCHS2.
S24401.
S24402.
RefSeqiNP_990732.1. NM_205401.1. [P04268-4]
UniGeneiGga.4108.

Genome annotation databases

EnsembliENSGALT00000039589; ENSGALP00000038799; ENSGALG00000003521. [P04268-4]
GeneIDi396366.
KEGGigga:396366.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M32441 mRNA. Translation: AAA48610.1.
X57991
, X57993, X57994, X57995 Genomic DNA. Translation: CAA41056.1.
M69144
, M69140, M69142, M69143 Genomic DNA. Translation: AAA48577.1.
X16090 Genomic DNA. Translation: CAA34217.1. Sequence problems.
X57991
, X57993, X57994, X57996 Genomic DNA. Translation: CAA41059.1.
X57991
, X57993, X57994, X57996 Genomic DNA. Translation: CAA41058.1.
X57991
, 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.
PIRiS24399. TMCHA.
S24400. TMCHS2.
S24401.
S24402.
RefSeqiNP_990732.1. NM_205401.1. [P04268-4]
UniGeneiGga.4108.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP04268.
SMRiP04268. Positions 1-284.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP04268. 1 interaction.

Proteomic databases

PaxDbiP04268.
PRIDEiP04268.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSGALT00000039589; ENSGALP00000038799; ENSGALG00000003521. [P04268-4]
GeneIDi396366.
KEGGigga:396366.

Organism-specific databases

CTDi7168.

Phylogenomic databases

eggNOGiNOG304012.
GeneTreeiENSGT00550000074494.
HOVERGENiHBG107404.
InParanoidiP04268.
KOiK10373.
OMAiLTICETE.
OrthoDBiEOG7673C8.
PhylomeDBiP04268.
TreeFamiTF351519.

Enzyme and pathway databases

ReactomeiREACT_303305. Striated Muscle Contraction.
REACT_327184. Smooth Muscle Contraction.

Miscellaneous databases

EvolutionaryTraceiP04268.
NextBioi20816411.
PROiP04268.

Gene expression databases

ExpressionAtlasiP04268. baseline.

Family and domain databases

InterProiIPR000533. Tropomyosin.
[Graphical view]
PfamiPF00261. Tropomyosin. 1 hit.
[Graphical view]
PRINTSiPR00194. TROPOMYOSIN.
PROSITEiPS00326. TROPOMYOSIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-81.

Entry informationi

Entry nameiTPM1_CHICK
AccessioniPrimary (citable) accession number: P04268
Secondary accession number(s): P02559
, P08942, P18441, P18442, P49436, P49438, P49439, Q540N4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: August 13, 1987
Last modified: July 22, 2015
This is version 117 of the entry and version 2 of the sequence. [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

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.