Pvalb
entrez
25269
canonical
uniprot
P02625
canonical
ensembl
ENSRNOG00000006471
resolver
ensembl
ENSRNOG00055032164
resolver
ensembl
ENSRNOG00060027887
resolver
ensp
ENSRNOP00000106492
resolver
ensp
ENSRNOP00055045852
resolver
ensp
ENSRNOP00060040388
resolver
enst
ENSRNOT00000141011
resolver
enst
ENSRNOT00055055615
resolver
enst
ENSRNOT00060048473
resolver
genesymbol
Pvalb
resolver
genesymbol_syn
Pva
resolver
uniprot
A0JN21
resolver
uniprot_entry
PRVA_RAT
resolver
uniprot_sec
A0JN21
resolver
amino_acid_sequence
MSMTDLLSAEDIKKAIGAFTAADSFDHKKFFQMVGLKKKSADDVKKVFHILDKDKSGFIEEDELGSILKGFSSDARDLSAKETKTLMAAGDKDGDGKIGVEEFSTLVAES
uniprot
proteins
function
FUNCTION: In muscle, parvalbumin is thought to be involved in relaxation after contraction (By similarity). It binds two calcium ions (PubMed:19622856, PubMed:16101280, PubMed:15169955, PubMed:15287728, PubMed:11562941, PubMed:8289291). {ECO:0000250|UniProtKB:P02624, ECO:0000269|PubMed:11562941, ECO:0000269|PubMed:15169955, ECO:0000269|PubMed:15287728, ECO:0000269|PubMed:16101280, ECO:0000269|PubMed:19622856, ECO:0000269|PubMed:8289291}.
uniprot
proteins
mass_dalton
11926
uniprot
proteins
mutagenesis
MUTAGEN 1..37; /note="Missing: Deletion of both A and B helices results in loss of stable apo form, in lower Ca(+) ion-binding affinity compared to wild-type, and in inability to bind Mg(2+)."; /evidence="ECO:0000269|PubMed:11562941"; MUTAGEN 56; /note="S->D: Increased Ca(2+)-binding affinity in the EF-hand 1 domain probably due to the orientation of mutant D-60 side chain, which is predicted to stabilize helix D; when associated with D-60. Behaves as wild-type with identical Na(+)-binding stoichiometry and increased Ca(2+) and Mg(2+) ion-binding affinity in K(+)-containing solution; when associated with D-60."; /evidence="ECO:0000269|PubMed:15287728"; MUTAGEN 60; /note="E->D: Increased Ca(2+)-binding affinity in the EF-hand 1 domain probably due to the orientation of mutant D-60 side chain, which is predicted to stabilize helix D; when associated with D-56. Behaves as wild-type with identical Na(+)-binding stoichiometry and increased Ca(2+) and Mg(2+) ion-binding affinity in K(+)-containing solution; when associated with D-56."; /evidence="ECO:0000269|PubMed:15287728"; MUTAGEN 76; /note="R->A: Loss of salt bridge formation with E-81. No effect in the overall structure of the protein. However, more solvent-exposed AB loop, which consists of two antiparallel helices A and B, and higher flexibility of the AB loop compared to the wild-type structure. Lower thermal stability of the calcium-loaded form of the protein than that of the wild-type, but melting temperature (Tm) value still remains quite high. Unfolded apo form at room temperature. Weaker calcium- and, to a lesser extent, magnesium-binding affinities compared to the wild-type."; /evidence="ECO:0000269|PubMed:19622856"; MUTAGEN 95; /note="D->S: Reduced Ca(2+)-binding affinity in the EF-hand 2 domain due to a substantial enthalpic penalty, the source of which may be steric interference between F-58 and C alpha atom of mutant E-99; when associated with E-99. No effect on the Ca(2+) or Mg(2+) ion-binding properties in either Na(+)- or K(+)-containing buffers indicating that the reduced affinity for divalent ions is not a result of heightened monovalent ion competition; when associated with E-99."; /evidence="ECO:0000269|PubMed:16101280"; MUTAGEN 99; /note="G->E: Reduced Ca(2+)-binding affinity in the EF-hand 2 domain due to a substantial enthalpic penalty, the source of which may be steric interference between F-58 and C alpha atom of mutant E-99; when associated with S-95. No effect on the Ca(2+) or Mg(2+) ion-binding properties in either Na(+)- or K(+)-containing buffers indicating that the reduced affinity for divalent ions is not a result of heightened monovalent ion competition; when associated with S-95."; /evidence="ECO:0000269|PubMed:16101280
uniprot
proteins
protein_family
Parvalbumin family
uniprot
proteins
pubmed
10036163
uniprot
proteins
pubmed
11562941
uniprot
proteins
pubmed
15169955
uniprot
proteins
pubmed
15287728
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16101280
uniprot
proteins
pubmed
18218708
uniprot
proteins
pubmed
19622856
uniprot
proteins
pubmed
22673903
uniprot
proteins
pubmed
3009434
uniprot
proteins
pubmed
3036821
uniprot
proteins
pubmed
3707914
uniprot
proteins
pubmed
3856270
uniprot
proteins
pubmed
6754379
uniprot
proteins
pubmed
8289291
uniprot
proteins
sequence_length
110
uniprot
proteins