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Protein

Parvalbumin beta

Gene
N/A
Organism
Cyprinus carpio (Common carp)
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 bindingi51 – 511Calcium 1By similarity
Metal bindingi53 – 531Calcium 1By similarity
Metal bindingi55 – 551Calcium 1By similarity
Metal bindingi57 – 571Calcium 1; via carbonyl oxygenBy similarity
Metal bindingi59 – 591Calcium 1By similarity
Metal bindingi62 – 621Calcium 1By similarity
Metal bindingi90 – 901Calcium 2By similarity
Metal bindingi92 – 921Calcium 2By similarity
Metal bindingi94 – 941Calcium 2By similarity
Metal bindingi101 – 1011Calcium 2By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi51 – 62121Add
BLAST
Calcium bindingi90 – 101122Add
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
OrganismiCyprinus carpio (Common carp)
Taxonomic identifieri7962 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeCyprinus

Pathology & Biotechi

Protein family/group databases

Allergomei263. Cyp c 1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 108108Parvalbumin betaPRO_0000073606Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylalanine1 Publication

Keywords - PTMi

Acetylation

Structurei

Secondary structure

1
108
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni3 – 53Combined sources
Helixi8 – 1710Combined sources
Helixi26 – 327Combined sources
Helixi35 – 373Combined sources
Helixi40 – 5011Combined sources
Beta strandi55 – 584Combined sources
Helixi60 – 645Combined sources
Helixi66 – 694Combined sources
Helixi79 – 8911Combined sources
Beta strandi94 – 974Combined sources
Helixi99 – 1079Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1B8CX-ray2.00A/B1-108[»]
1B8LX-ray1.70A1-108[»]
1B8RX-ray1.90A1-108[»]
1B9AX-ray2.00A1-108[»]
1CDPX-ray1.60A1-108[»]
4CPVX-ray1.50A1-108[»]
5CPVX-ray1.60A1-108[»]
ProteinModelPortaliP02618.
SMRiP02618. Positions 1-108.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02618.

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.

P02618-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
AFAGVLNDAD IAAALEACKA ADSFNHKAFF AKVGLTSKSA DDVKKAFAII
60 70 80 90 100
DQDKSGFIEE DELKLFLQNF KADARALTDG ETKTFLKAGD SDGDGKIGVD

EFTALVKA
Length:108
Mass (Da):11,436
Last modified:July 21, 1986 - v1
Checksum:iAB33129FC2D79E4D
GO

Sequence databases

PIRiA92133. PVCAB.

Cross-referencesi

Sequence databases

PIRiA92133. PVCAB.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1B8CX-ray2.00A/B1-108[»]
1B8LX-ray1.70A1-108[»]
1B8RX-ray1.90A1-108[»]
1B9AX-ray2.00A1-108[»]
1CDPX-ray1.60A1-108[»]
4CPVX-ray1.50A1-108[»]
5CPVX-ray1.60A1-108[»]
ProteinModelPortaliP02618.
SMRiP02618. Positions 1-108.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

Allergomei263. Cyp c 1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG107490.

Miscellaneous databases

EvolutionaryTraceiP02618.

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. "Carp muscle calcium-binding protein. I. Characterization of the tryptic peptides and the complete amino acid sequence of component B."
    Coffee C.J., Bradshaw R.A.
    J. Biol. Chem. 248:3305-3312(1973) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE, ACETYLATION AT ALA-1.
  2. Erratum
    Coffee C.J., Bradshaw R.A.
    J. Biol. Chem. 248:6576-6576(1973)
    Cited for: SEQUENCE REVISION.
  3. "Carp muscle calcium-binding protein. II. Structure determination and general description."
    Kretsinger R.H., Nockolds C.E.
    J. Biol. Chem. 248:3313-3326(1973) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS).
  4. "Terbium replacement of calcium in carp muscle calcium-binding parvalbumin: an X-ray crystallographic study."
    Moews P.C., Kretsinger R.H.
    J. Mol. Biol. 91:229-232(1975) [PubMed] [Europe PMC] [Abstract]
    Cited for: CRYSTALLIZATION.
  5. "Restrained least squares refinement of native (calcium) and cadmium-substituted carp parvalbumin using X-ray crystallographic data at 1.6-A resolution."
    Swain A.L., Kretsinger R.H., Amma E.L.
    J. Biol. Chem. 264:16620-16628(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
  6. "Refined crystal structure of calcium-liganded carp parvalbumin 4.25 at 1.5-A resolution."
    Kumar V.D., Lee L., Edwards B.F.P.
    Biochemistry 29:1404-1412(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).
  7. "Metal-ion affinity and specificity in EF-hand proteins: coordination geometry and domain plasticity in parvalbumin."
    Cates M.S., Berry M.B., Ho E.L., Li Q., Potter J.D., Phillips G.N. Jr.
    Structure 7:1269-1278(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).

Entry informationi

Entry nameiPRVB_CYPCA
AccessioniPrimary (citable) accession number: P02618
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: March 16, 2016
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

This parvalbumin has an isoelectric point of 4.25.

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.