Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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)DescriptionActionsGraphical viewLength
Metal bindingi51Calcium 1Combined sources1 Publication1
Metal bindingi53Calcium 1Combined sources1 Publication1
Metal bindingi55Calcium 1Combined sources1 Publication1
Metal bindingi57Calcium 1; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi59Calcium 1Combined sources1 Publication1
Metal bindingi62Calcium 1Combined sources1 Publication1
Metal bindingi90Calcium 2Combined sources1 Publication1
Metal bindingi92Calcium 2Combined sources1 Publication1
Metal bindingi94Calcium 2Combined sources1 Publication1
Metal bindingi96Calcium 2; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi101Calcium 2Combined sources1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Calcium bindingi51 – 621PROSITE-ProRule annotationCombined sources1 PublicationAdd BLAST12
Calcium bindingi90 – 1012PROSITE-ProRule annotationCombined sources1 PublicationAdd BLAST12

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)DescriptionActionsGraphical viewLength
ChainiPRO_00000736151 – 108Parvalbumin betaAdd BLAST108

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylalanine1 Publication1
Disulfide bondi11 ↔ 33Combined sources1 Publication

Keywords - PTMi

Acetylation, Disulfide bond

Structurei

Secondary structure

1108
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni3 – 6Combined sources4
Helixi9 – 17Combined sources9
Helixi26 – 32Combined sources7
Helixi40 – 50Combined sources11
Beta strandi55 – 59Combined sources5
Helixi60 – 63Combined sources4
Helixi66 – 70Combined sources5
Helixi79 – 89Combined sources11
Beta strandi94 – 97Combined sources4
Helixi99 – 106Combined sources8

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP02621.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini38 – 73EF-hand 1PROSITE-ProRule annotationAdd BLAST36
Domaini77 – 108EF-hand 2PROSITE-ProRule annotationAdd BLAST32

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

CDDicd00051. EFh. 1 hit.
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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A75X-ray1.90A/B1-108[»]
ProteinModelPortaliP02621.
SMRiP02621.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG107490.

Miscellaneous databases

EvolutionaryTraceiP02621.

Family and domain databases

CDDicd00051. EFh. 1 hit.
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...

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: November 30, 2016
This is version 102 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.