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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...

Publicationsi

  1. "The primary structure of the parvalbumin II of pike (Esox lucius)."
    Gerday C.
    Eur. J. Biochem. 70:305-318(1976) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.
  2. "Comparative study of physiochemical properties of two pike parvalbumins by means of their intrinsic tyrosyl and phenylalanyl fluorescence."
    Permyakov E.A., Medvedkin V.N., Kalinichenko L.P., Burstein E.A.
    Arch. Biochem. Biophys. 227:9-20(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: CALCIUM-BINDING.
  3. "Crystal structure determination and refinement of pike 4.10 parvalbumin (minor component from Esox lucius)."
    Declercq J.-P., Tinant B., Parello J., Etienne G., Huber R.
    J. Mol. Biol. 202:349-353(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS).
  4. "Ionic interactions with parvalbumins. Crystal structure determination of pike 4.10 parvalbumin in four different ionic environments."
    Declercq J.-P., Tinant B., Parello J., Rambaud J.
    J. Mol. Biol. 220:1017-1039(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS).
  5. "X-ray structure of a new crystal form of pike 4.10 beta parvalbumin."
    Declercq J.-P., Tinant B., Parello J.
    Acta Crystallogr. D 52:165-169(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS).
  6. "Crystal structure of the EF-hand parvalbumin at atomic resolution (0.91 A) and at low temperature (100 K). Evidence for conformational multistates within the hydrophobic core."
    Declercq J.-P., Evrard C., Lamzin V., Parello J.
    Protein Sci. 8:2194-2204(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (0.91 ANGSTROMS).

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.