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A2V735

- TPM_CHIOP

UniProt

A2V735 - TPM_CHIOP

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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

Names & Taxonomyi

Protein namesi
Recommended name:
Tropomyosin1 Publication
Alternative name(s):
Tropomyosin, slow-tonic isoformImported1 Publication
Short name:
Tm-Chio-tonicImported
Gene namesi
Name:TM1By similarity
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 – 284284TropomyosinPRO_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.
ModBaseiSearch...
MobiDBiSearch...

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.Curated

Sequence similaritiesi

Belongs to the tropomyosin family.Sequence Analysis

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

        10         20         30         40         50
MDAIKKKMQA MKLEKDNAMD KADTLEQQNK EANLRAEKTE EEIRANQKKS
60 70 80 90 100
QLVENELDHA QEQLSAATHK LVEKEKAFAN AEGEVAALNR RIQLLEEDLE
110 120 130 140 150
RSEERLNTAT TKLAEASQAA DESERMRKVL ENRSLSDEER MDALENQLKE
160 170 180 190 200
ARFLAEEADR KYDEVARKLA MVEADLERAE ERAESGESKI VELEEELRVV
210 220 230 240 250
GNNLKSLEVS EEKANQREET YKEQIKTLAN KLKAAEARAE FAERSVQKLQ
260 270 280
KEVDRLEDEL VNEKEKYKNI ADEMDQAFSE LSGF
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:
EMBLi
GenBanki
DDBJi
Links Updated
AB270634 mRNA. Translation: BAF47267.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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: Muscle1 Publication.
  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: Muscle1 Publication.

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 1, 2014
This is version 20 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