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.

A2V735

- TPM_CHIOP

UniProt

A2V735 - TPM_CHIOP

(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
Gene
TM1
Organism
Chionoecetes opilio (Crab-beetle)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

Functioni

Tropomyosin, in association with the troponin complex, plays a central role in the calcium dependent regulation of muscle contraction By similarity.By similarity

Names & Taxonomyi

Protein namesi
Recommended name:
Tropomyosin
Alternative name(s):
Tropomyosin, slow-tonic isoform
Short name:
Tm-Chio-tonic
Gene namesi
Name:TM1
OrganismiChionoecetes opilio (Crab-beetle)
Taxonomic identifieri41210 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaCrustaceaMalacostracaEumalacostracaEucaridaDecapodaPleocyemataBrachyuraEubrachyuraMajoideaMajidaeChionoecetes

Pathology & Biotechi

Allergenic propertiesi

Causes an allergic reaction in human.2 Publications

Keywords - Diseasei

Allergen

Protein family/group databases

Allergomei3807. Chi o 1.
4087. Chi o 1.0101.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 284284Tropomyosin
PRO_0000398787Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication

Keywords - PTMi

Acetylation

Expressioni

Tissue specificityi

Expressed in leg muscle and chest protection muscle (at protein level).1 Publication

Interactioni

Subunit structurei

Homodimer.1 Publication

Structurei

3D structure databases

ProteinModelPortaliA2V735.
SMRiA2V735. Positions 1-283.

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili1 – 284284 By similarityBy 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, Repeat

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

A2V735-1 [UniParc]FASTAAdd to Basket

« Hide

MDAIKKKMQA MKLEKDNAMD KADTLEQQNK EANLRAEKTE EEIRANQKKS    50
QLVENELDHA QEQLSAATHK LVEKEKAFAN AEGEVAALNR RIQLLEEDLE 100
RSEERLNTAT TKLAEASQAA DESERMRKVL ENRSLSDEER MDALENQLKE 150
ARFLAEEADR KYDEVARKLA MVEADLERAE ERAESGESKI VELEEELRVV 200
GNNLKSLEVS EEKANQREET YKEQIKTLAN KLKAAEARAE FAERSVQKLQ 250
KEVDRLEDEL VNEKEKYKNI ADEMDQAFSE LSGF 284
Length:284
Mass (Da):32,675
Last modified:March 20, 2007 - v1
Checksum:i357A164032C6B96E
GO

Mass spectrometryi

Molecular mass is 32733±6.5 Da from positions 1 - 284. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB270634 mRNA. Translation: BAF47267.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB270634 mRNA. Translation: BAF47267.1 .

3D structure databases

ProteinModelPortali A2V735.
SMRi A2V735. Positions 1-283.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

Allergomei 3807. Chi o 1.
4087. Chi o 1.0101.

Protocols and materials databases

Structural Biology Knowledgebase Search...

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. "Molecular cloning of tropomyosins identified as allergens in six species of crustaceans."
    Motoyama K., Suma Y., Ishizaki S., Nagashima Y., Shiomi K.
    J. Agric. Food Chem. 55:985-991(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, ALLERGEN.
    Tissue: Muscle.
  2. "Characterization and de novo sequencing of snow crab tropomyosin enzymatic peptides by both electrospary ionization and matrix-assisted laser desorption ionization QqToF tandemmass spectrometry."
    Abdel Rahman A.M., Lopata A.L., O'Hehir R.E., Robinson J.J., Banoub J.H., Helleur R.J.
    J. Mass Spectrom. 45:372-381(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 8-284, SUBUNIT, MASS SPECTROMETRY, ALLERGENICITY, ACETYLATION AT MET-1.
    Tissue: Muscle.

Entry informationi

Entry nameiTPM_CHIOP
AccessioniPrimary (citable) accession number: A2V735
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: March 20, 2007
Last modified: October 31, 2012
This is version 19 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi