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P02620 (PRVB_MERME) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Protein attributes

Sequence length108 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

In muscle, parvalbumin is thought to be involved in relaxation after contraction. It binds two calcium ions.

Miscellaneous

This is the major hake parvalbumin.

This parvalbumin has an isoelectric point of 4.36.

Is regarded as an important allergen.

Sequence similarities

Belongs to the parvalbumin family.

Contains 2 EF-hand domains.

Mass spectrometry

Molecular mass is 11329.746±0.0013 Da from positions 1 - 108. Determined by ESI. Ref.2

Ontologies

Keywords
   DiseaseAllergen
   DomainRepeat
   LigandCalcium
Metal-binding
   Molecular functionMuscle protein
   PTMAcetylation
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Molecular_functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 108108Parvalbumin beta
PRO_0000073614

Regions

Domain38 – 7336EF-hand 1
Domain77 – 10832EF-hand 2
Calcium binding51 – 62121 By similarity
Calcium binding90 – 101122 By similarity

Amino acid modifications

Modified residue11N-acetylalanine Ref.1 Ref.2

Sequences

Sequence LengthMass (Da)Tools
P02620 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: E5526ACBF3DC3B64

FASTA10811,295
        10         20         30         40         50         60 
AFAGILADAD ITAALAACKA EGSFKHGEFF TKIGLKGKSA ADIKKVFGII DQDKSDFVEE 

        70         80         90        100 
DELKLFLQNF SAGARALTDA ETATFLKAGD SDGDGKIGVE EFAAMVKG 

« Hide

References

[1]"The primary structure of the major parvalbumin from hake muscle. Overlapping peptides obtained with chemical and enzymatic methods. The complete amino-acid sequence."
Capony J.-P., Ryden L., Demaille J.G., Pechere J.-F.
Eur. J. Biochem. 32:97-108(1973) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE.
[2]"Extensive de novo sequencing of new parvalbumin isoforms using a novel combination of bottom-up proteomics, accurate molecular mass measurement by FTICR-MS, and selected MS/MS ion monitoring."
Carrera M., Canas B., Vazquez J., Gallardo J.M.
J. Proteome Res. 9:4393-4406(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE, MASS SPECTROMETRY, ACETYLATION AT ALA-1.
Tissue: Muscle.

Cross-references

Sequence databases

PIRPVHK. A03055.

3D structure databases

ProteinModelPortalP02620.
SMRP02620. Positions 1-108.
ModBaseSearch...

Protein family/group databases

Allergome7643. Mer mr 1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG107490.

Family and domain databases

Gene3D1.10.238.10. 1 hit.
InterProIPR011992. EF-hand-like_dom.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR008080. Parvalbumin.
[Graphical view]
PANTHERPTHR11653. PTHR11653. 1 hit.
PfamPF13499. EF_hand_5. 1 hit.
[Graphical view]
SMARTSM00054. EFh. 2 hits.
[Graphical view]
PROSITEPS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePRVB_MERME
AccessionPrimary (citable) accession number: P02620
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: May 1, 2013
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families