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Protein

Parvalbumin beta

Gene
N/A
Organism
Merlangius merlangus (Whiting) (Gadus merlangus)
Status
Reviewed-Annotation score: Annotation score: 4 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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi51 – 511Calcium 1Combined sources1 Publication
Metal bindingi53 – 531Calcium 1Combined sources1 Publication
Metal bindingi55 – 551Calcium 1Combined sources1 Publication
Metal bindingi57 – 571Calcium 1; via carbonyl oxygenCombined sources1 Publication
Metal bindingi59 – 591Calcium 1Combined sources1 Publication
Metal bindingi62 – 621Calcium 1Combined sources1 Publication
Metal bindingi90 – 901Calcium 2Combined sources1 Publication
Metal bindingi92 – 921Calcium 2Combined sources1 Publication
Metal bindingi94 – 941Calcium 2Combined sources1 Publication
Metal bindingi96 – 961Calcium 2; via carbonyl oxygenCombined sources1 Publication
Metal bindingi101 – 1011Calcium 2Combined sources1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi51 – 62121PROSITE-ProRule annotationCombined sources1 PublicationAdd
BLAST
Calcium bindingi90 – 101122PROSITE-ProRule annotationCombined sources1 PublicationAdd
BLAST

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Muscle protein

Keywords - Ligandi

Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Parvalbumin beta
OrganismiMerlangius merlangus (Whiting) (Gadus merlangus)
Taxonomic identifieri8058 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiNeoteleosteiAcanthomorphataZeiogadariaGadariaeGadiformesGadoideiGadidaeMerlangius

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 108108Parvalbumin betaPRO_0000073615Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylalanine1 Publication
Disulfide bondi11 ↔ 33Combined sources1 Publication

Keywords - PTMi

Acetylation, Disulfide bond

Structurei

Secondary structure

1
108
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni3 – 64Combined sources
Helixi9 – 179Combined sources
Helixi26 – 327Combined sources
Helixi40 – 5011Combined sources
Beta strandi55 – 595Combined sources
Helixi60 – 634Combined sources
Helixi66 – 705Combined sources
Helixi79 – 8911Combined sources
Beta strandi94 – 974Combined sources
Helixi99 – 1068Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A75X-ray1.90A/B1-108[»]
ProteinModelPortaliP02621.
SMRiP02621. Positions 1-108.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02621.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini38 – 7336EF-hand 1PROSITE-ProRule annotationAdd
BLAST
Domaini77 – 10832EF-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.

P02621-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
AFAGILADAD CAAAVKACEA ADSFSYKAFF AKCGLSGKSA DDIKKAFVFI
60 70 80 90 100
DQDKSGFIEE DELKLFLQVF KAGARALTDA ETKAFLKAGD SDGDGAIGVE

EWVALVKA
Length:108
Mass (Da):11,323
Last modified:July 15, 1998 - v2
Checksum:i4AA2ACDD29334FB2
GO

Sequence databases

PIRiA03056. PVWI.

Cross-referencesi

Sequence databases

PIRiA03056. PVWI.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A75X-ray1.90A/B1-108[»]
ProteinModelPortaliP02621.
SMRiP02621. Positions 1-108.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG107490.

Miscellaneous databases

EvolutionaryTraceiP02621.

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 major parvalbumin of the whiting (Gadus merlangus)."
    Joassin L., Gerday C.
    Comp. Biochem. Physiol. 57B:159-161(1977) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE, ACETYLATION AT ALA-1.
    Tissue: Muscle.
  2. "Fluorescence studies of the calcium binding to whiting (Gadus merlangus) parvalbumin."
    Permyakov E.A., Yarmolenko V.V., Emelyanenko V.I., Burstein E.A., Closset J., Gerday C.
    Eur. J. Biochem. 109:307-315(1980) [PubMed] [Europe PMC] [Abstract]
    Cited for: CALCIUM-BINDING.
  3. "Kinetic mechanism of calcium binding to whiting parvalbumin."
    White H.D.
    Biochemistry 27:3357-3365(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: CALCIUM-BINDING DATA.
  4. Declercq J.P., Baneres J.L., Rambaud J., Parello J.
    Submitted (MAR-1998) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), SEQUENCE REVISION TO 11-12.
    Tissue: Muscle.

Entry informationi

Entry nameiPRVB_MERMR
AccessioniPrimary (citable) accession number: P02621
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 15, 1998
Last modified: March 16, 2016
This is version 99 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

This parvalbumin has an isoelectric point of 4.50.

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.