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P58773

- TPM1_COTJA

UniProt

P58773 - TPM1_COTJA

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Protein
Tropomyosin alpha-1 chain
Gene
TPM1
Organism
Coturnix coturnix japonica (Japanese quail) (Coturnix japonica)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at transcript 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

Names & Taxonomyi

Protein namesi
Recommended name:
Tropomyosin alpha-1 chain
Alternative name(s):
Alpha-tropomyosin
Tropomyosin-1
Gene namesi
Name:TPM1
OrganismiCoturnix coturnix japonica (Japanese quail) (Coturnix japonica)
Taxonomic identifieri93934 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePerdicinaeCoturnix

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_0000205626Add
BLAST

Proteomic databases

PRIDEiP58773.

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 similarity.

Structurei

3D structure databases

ProteinModelPortaliP58773.
SMRiP58773. Positions 1-284.

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

HOVERGENiHBG107404.

Family and domain databases

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

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Note: Additional isoforms seem to exist.

Isoform 1 (identifier: P58773-1) [UniParc]FASTAAdd to Basket

Also known as: Skeletal muscle, cC402, SK74

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 - v1
Checksum:iDBBBD3DB7F36DACB
GO
Isoform 2 (identifier: P58773-2) [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...LLSAEEIAAK
     258-284: DELYAQKLKYKAISEELDHALNDMTSI → EKVAHAKEENLNMHQMLDQTLLELNNM

Show »
Length:284
Mass (Da):32,865
Checksum:i180403F2D27453D7
GO
Isoform 3 (identifier: P58773-3) [UniParc]FASTAAdd to Basket

Also known as: Fibroblast, cC401

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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei42 – 8039ELVAL…KKATD → DIVQLEKQLRVTEDSRDQVL EELHKSEDSLLSAEEIAAK in isoform 2.
VSP_006592Add
BLAST
Alternative sequencei258 – 28427DELYA…DMTSI → EKVAHAKEENLNMHQMLDQT LLELNNM in isoform 2 and isoform 3.
VSP_006593Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X16230
, X16236, X16237, X16238, X16239, X16240 Genomic DNA. Translation: CAA34344.1.
X16230
, X16236, X16237, X16238, X16241 Genomic DNA. Translation: CAA34343.1.
X04690 mRNA. Translation: CAA28393.1.
M15043 mRNA. Translation: AAA49511.1.
M17914 mRNA. Translation: AAA49510.1.
M15044 mRNA. Translation: AAA49508.1.
PIRiA28499.
B28499. A26113.
S05445.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X16230
, X16236 , X16237 , X16238 , X16239 , X16240 Genomic DNA. Translation: CAA34344.1 .
X16230
, X16236 , X16237 , X16238 , X16241 Genomic DNA. Translation: CAA34343.1 .
X04690 mRNA. Translation: CAA28393.1 .
M15043 mRNA. Translation: AAA49511.1 .
M17914 mRNA. Translation: AAA49510.1 .
M15044 mRNA. Translation: AAA49508.1 .
PIRi A28499.
B28499. A26113.
S05445.

3D structure databases

ProteinModelPortali P58773.
SMRi P58773. Positions 1-284.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi P58773.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

HOVERGENi HBG107404.

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

  1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2).
  2. "A novel hybrid alpha-tropomyosin in fibroblasts is produced by alternative splicing of transcripts from the skeletal muscle alpha-tropomyosin gene."
    Pearson-White S.H., Emerson C.P. Jr.
    J. Biol. Chem. 262:15998-16010(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3).
  3. "Analysis of tropomyosin cDNAs isolated from skeletal and smooth muscle mRNA."
    Flach J.E., Lindquester G.J., Berish S., Hickman K.H., Devlin R.
    Nucleic Acids Res. 14:9193-9211(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  4. "Closely related alpha-tropomyosin mRNAs in quail fibroblasts and skeletal muscle cells."
    Hallauer P.L., Hastings K.E.M., Baldwin A.S. Jr., Pearson-White S.H., Merrifield P.A., Emerson C.P. Jr.
    J. Biol. Chem. 262:3590-3596(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3).

Entry informationi

Entry nameiTPM1_COTJA
AccessioniPrimary (citable) accession number: P58773
Secondary accession number(s): P02559
, P08942, P18442, P49437
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: August 13, 1987
Last modified: June 26, 2013
This is version 52 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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