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Protein

Parvalbumin beta

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi50 – 501Calcium 1By similarity
Metal bindingi52 – 521Calcium 1By similarity
Metal bindingi54 – 541Calcium 1By similarity
Metal bindingi56 – 561Calcium 1; via carbonyl oxygenBy similarity
Metal bindingi58 – 581Calcium 1By similarity
Metal bindingi61 – 611Calcium 1By similarity
Metal bindingi89 – 891Calcium 2By similarity
Metal bindingi91 – 911Calcium 2By similarity
Metal bindingi93 – 931Calcium 2By similarity
Metal bindingi100 – 1001Calcium 2By similarity

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 beta
Alternative name(s):
Parvalbumin II
Parvalbumin pI 4.10
Parvalbumin-2
OrganismiEsox lucius (Northern pike)
Taxonomic identifieri8010 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiProtacanthopterygiiEsociformesEsocidaeEsox

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 107107Parvalbumin betaPRO_0000073607Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylserine1 Publication

Keywords - PTMi

Acetylation

Structurei

Secondary structure

1
107
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni2 – 43Combined sources
Helixi7 – 1610Combined sources
Helixi25 – 317Combined sources
Helixi34 – 363Combined 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
1PALX-ray1.65A1-107[»]
1PVBX-ray1.75A1-107[»]
2PALX-ray1.80A1-107[»]
2PVBX-ray0.91A1-106[»]
3PALX-ray2.40A1-107[»]
4PALX-ray1.80A1-107[»]
ProteinModelPortaliP02619.
SMRiP02619. Positions 1-107.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02619.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini37 – 7236EF-hand 1PROSITE-ProRule annotationAdd
BLAST
Domaini76 – 10732EF-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.

P02619-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
SFAGLKDADV AAALAACSAA DSFKHKEFFA KVGLASKSLD DVKKAFYVID
60 70 80 90 100
QDKSGFIEED ELKLFLQNFS PSARALTDAE TKAFLADGDK DGDGMIGVDE

FAAMIKA
Length:107
Mass (Da):11,390
Last modified:July 21, 1986 - v1
Checksum:i100674BE1836D28F
GO

Sequence databases

PIRiA03054. PVPK2.

Cross-referencesi

Sequence databases

PIRiA03054. PVPK2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PALX-ray1.65A1-107[»]
1PVBX-ray1.75A1-107[»]
2PALX-ray1.80A1-107[»]
2PVBX-ray0.91A1-106[»]
3PALX-ray2.40A1-107[»]
4PALX-ray1.80A1-107[»]
ProteinModelPortaliP02619.
SMRiP02619. Positions 1-107.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG107490.

Miscellaneous databases

EvolutionaryTraceiP02619.

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...

Entry informationi

Entry nameiPRVB_ESOLU
AccessioniPrimary (citable) accession number: P02619
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: January 20, 2016
This is version 97 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 one of two major parvalbumins found in the white muscle of pike.
This parvalbumin has an isoelectric point of 4.10.

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.