SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P04268

- TPM1_CHICK

UniProt

P04268 - TPM1_CHICK

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Tropomyosin alpha-1 chain
Gene
TPM1
Organism
Gallus gallus (Chicken)
Status
Reviewed - 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.

GO - Molecular functioni

  1. protein binding Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Muscle protein

Keywords - Ligandi

Actin-binding

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus
ProteomesiUP000000539: Chromosome 10

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. cytoskeleton Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 284284Tropomyosin alpha-1 chain
PRO_0000205625Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP04268.
PRIDEiP04268.

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.2 Publications

Binary interactionsi

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

Protein-protein interaction databases

IntActiP04268. 1 interaction.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

Miscellaneous databases

EvolutionaryTraceiP04268.

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili1 – 284284 By similarity
Add
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.

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG304012.
GeneTreeiENSGT00550000074494.
HOVERGENiHBG107404.
KOiK10373.
OMAiEASAEKY.
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. Align

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

MDAIKKKMQM LKLDKENALD RAEQAEADKK AAEERSKQLE DELVALQKKL    50
KGTEDELDKY SESLKDAQEK LELADKKATD AESEVASLNR RIQLVEEELD 100
RAQERLATAL QKLEEAEKAA DESERGMKVI ENRAQKDEEK MEIQEIQLKE 150
AKHIAEEADR KYEEVARKLV IIEGDLERAE ERAELSESKC AELEEELKTV 200
TNNLKSLEAQ AEKYSQKEDK YEEEIKVLTD KLKEAETRAE FAERSVTKLE 250
KSIDDLEDEL YAQKLKYKAI SEELDHALND MTSI 284
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

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.
VSP_006587Add
BLAST
Alternative sequencei42 – 8039ELVAL…KKATD → DIVQLEKQLRVTEDSRDQVL EELHKSEDSLLFAEENAAK in isoform 2.
VSP_006588Add
BLAST
Alternative sequencei189 – 21224KCAEL…EAQAE → QVRQLEEQLRIMDQTLKALM AAED in isoform 4.
VSP_006589Add
BLAST
Alternative sequencei258 – 28427DELYA…DMTSI → EKVAHAKEENLNMHQMLDQT LLELNNM in isoform 2, isoform 4 and isoform 5.
VSP_006590Add
BLAST
Alternative sequencei259 – 28426ELYAQ…DMTSI → QLYQQLEQNSRLTNELKLAL NED in isoform 6 and isoform 7.
VSP_006591Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti34 – 341E → D AA sequence 1 Publication
Sequence conflicti45 – 451A → S AA sequence 1 Publication
Sequence conflicti63 – 631S → A AA sequence 1 Publication
Sequence conflicti75 – 751D → E AA sequence 1 Publication
Sequence conflicti83 – 842SE → AD AA sequence 1 Publication
Sequence conflicti132 – 1321N → S AA sequence 1 Publication
Sequence conflicti157 – 1571E → D AA sequence 1 Publication
Sequence conflicti165 – 1651V → A in AAA48610. 1 Publication
Sequence conflicti172 – 1721I → L AA sequence 1 Publication
Sequence conflicti174 – 1741G → S AA sequence 1 Publication
Sequence conflicti188 – 1881S → G AA sequence 1 Publication
Sequence conflicti229 – 2291T → S AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
PIRi S24399. TMCHA.
S24400. TMCHS2.
S24401.
S24402.
RefSeqi NP_990732.1. NM_205401.1. [P04268-4 ]
UniGenei Gga.4108.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1IC2 X-ray 2.00 A/B/C/D 1-80 [» ]
3MTU X-ray 2.10 A/B/C/D 1-29 [» ]
E/F 257-284 [» ]
3MUD X-ray 2.20 A/B 246-257 [» ]
C/D 1-29 [» ]
3U1A X-ray 2.00 A/B/C/D 1-81 [» ]
3U1C X-ray 1.80 A/B 1-98 [» ]
ProteinModelPortali P04268.
SMRi P04268. Positions 1-284.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P04268. 1 interaction.

Proteomic databases

PaxDbi P04268.
PRIDEi P04268.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSGALT00000039589 ; ENSGALP00000038799 ; ENSGALG00000003521 . [P04268-4 ]
GeneIDi 396366.
KEGGi gga:396366.

Organism-specific databases

CTDi 7168.

Phylogenomic databases

eggNOGi NOG304012.
GeneTreei ENSGT00550000074494.
HOVERGENi HBG107404.
KOi K10373.
OMAi EASAEKY.
OrthoDBi EOG7673C8.
PhylomeDBi P04268.
TreeFami TF351519.

Miscellaneous databases

EvolutionaryTracei P04268.
NextBioi 20816411.
PROi P04268.

Family and domain databases

InterProi IPR000533. Tropomyosin.
[Graphical view ]
Pfami PF00261. Tropomyosin. 1 hit.
[Graphical view ]
PRINTSi PR00194. TROPOMYOSIN.
PROSITEi PS00326. TROPOMYOSIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: June 11, 2014
This is version 109 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