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Protein

Parvalbumin alpha

Gene
N/A
Organism
Esox lucius (Northern pike)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi50 – 61121PROSITE-ProRule annotationAdd
BLAST
Calcium bindingi89 – 100122PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Muscle protein

Keywords - Ligandi

Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Parvalbumin alpha
Alternative name(s):
Parvalbumin III
Parvalbumin pI 5.0
Parvalbumin-3
OrganismiEsox lucius (Northern pike)
Taxonomic identifieri8010 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiProtacanthopterygiiEsociformesEsocidaeEsox

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 108108Parvalbumin alphaPRO_0000073595Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Acetylation

Structurei

Secondary structure

108
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi1 – 44Combined sources
Helixi7 – 1610Combined sources
Turni18 – 214Combined sources
Helixi25 – 317Combined sources
Turni33 – 364Combined sources
Helixi39 – 4911Combined sources
Beta strandi54 – 574Combined sources
Helixi59 – 635Combined sources
Helixi65 – 684Combined sources
Helixi78 – 8811Combined sources
Beta strandi93 – 964Combined sources
Helixi98 – 1069Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PVAX-ray1.65A/B1-108[»]
2PASNMR-A1-108[»]
3PATNMR-A1-108[»]
DisProtiDP00550.
ProteinModelPortaliP02628.
SMRiP02628. Positions 1-108.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02628.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini37 – 7236EF-hand 1PROSITE-ProRule annotationAdd
BLAST
Domaini76 – 10833EF-hand 2PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the parvalbumin family.Curated
Contains 2 EF-hand domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

HOVERGENiHBG107490.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
InterProiIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR008080. Parvalbumin.
[Graphical view]
PANTHERiPTHR11653. PTHR11653. 1 hit.
PfamiPF13499. EF-hand_7. 1 hit.
[Graphical view]
SMARTiSM00054. EFh. 2 hits.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 1 hit.
PROSITEiPS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P02628-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
AKDLLKADDI KKALDAVKAE GSFNHKKFFA LVGLKAMSAN DVKKVFKAID
60 70 80 90 100
ADASGFIEEE ELKFVLKSFA ADGRDLTDAE TKAFLKAADK DGDGKIGIDE

FETLVHEA
Length:108
Mass (Da):11,707
Last modified:July 21, 1986 - v1
Checksum:i8737BD351BA4ABC3
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti11 – 111K → KL in alpha-2. 1 Publication
Natural varianti27 – 271K → A in alpha-2. 1 Publication
Natural varianti31 – 311L → K in alpha-2. 1 Publication

Sequence databases

PIRiA67143. PVPK.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

PIRiA67143. PVPK.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PVAX-ray1.65A/B1-108[»]
2PASNMR-A1-108[»]
3PATNMR-A1-108[»]
DisProtiDP00550.
ProteinModelPortaliP02628.
SMRiP02628. Positions 1-108.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG107490.

Miscellaneous databases

EvolutionaryTraceiP02628.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
InterProiIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR008080. Parvalbumin.
[Graphical view]
PANTHERiPTHR11653. PTHR11653. 1 hit.
PfamiPF13499. EF-hand_7. 1 hit.
[Graphical view]
SMARTiSM00054. EFh. 2 hits.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 1 hit.
PROSITEiPS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The amino acid sequence of the pike (Esox lucius) parvalbumin 3."
    Frankenne F., Joassin L., Gerday C.
    FEBS Lett. 35:145-147(1973) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE, ACETYLATION AT ALA-1.
  2. Gerday C.
    Submitted (JAN-1975) to the PIR data bank
    Cited for: SEQUENCE REVISION.
  3. "Sequence microheterogeneity of parvalbumin pI 5.0 of pike: a mass spectrometric study."
    Permyakov S.E., Karnoup A.S., Bakunts A.G., Permyakov E.A.
    Biochim. Biophys. Acta 1794:129-136(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE, IDENTIFICATION BY MASS SPECTROMETRY, VARIANTS LEU-11 INS; ALA-27 AND LYS-31.
    Tissue: White muscle.
  4. "Two-dimensional 1H nuclear magnetic resonance study of pike pI 5.0 parvalbumin (Esox lucius). Sequential resonance assignments and folding of the polypeptide chain."
    Padilla A., Cave A., Parello J.
    J. Mol. Biol. 204:995-1017(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
  5. Erratum
    Padilla A., Cave A., Parello J.
    J. Mol. Biol. 208:723-724(1989)
  6. "Symmetrical rearrangement of the cation-binding sites of parvalbumin upon Ca2+/Mg2+ exchange. A study by 1H 2D NMR."
    Blancuzzi Y., Padilla A., Parello J., Cave A.
    Biochemistry 32:1302-1309(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
  7. "Assignment of 13C resonances and analysis of relaxation properties and internal dynamics of pike parvalbumin by 13C-NMR at natural abundance."
    Alattia T., Padilla A., Cave A.
    Eur. J. Biochem. 237:561-574(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.

Entry informationi

Entry nameiPRVA_ESOLU
AccessioniPrimary (citable) accession number: P02628
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: March 16, 2016
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

This is the major component, having an isoelectric point of 5.0.

Caution

This protein is more closely related to beta-type parvalbumins then to alpha-type.Curated

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.