ID   PRVA_BOVIN              Reviewed;         110 AA.
AC   Q0VCG3;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Parvalbumin alpha;
GN   Name=PVALB;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal cerebellum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: In muscle, parvalbumin is thought to be involved in
CC       relaxation after contraction. It binds two calcium ions (By
CC       similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the parvalbumin family. {ECO:0000305}.
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DR   EMBL; BC120184; AAI20185.1; -; mRNA.
DR   RefSeq; NP_001069582.1; NM_001076114.2.
DR   RefSeq; XP_010803641.1; XM_010805339.2.
DR   AlphaFoldDB; Q0VCG3; -.
DR   SMR; Q0VCG3; -.
DR   STRING; 9913.ENSBTAP00000025499; -.
DR   PaxDb; Q0VCG3; -.
DR   PRIDE; Q0VCG3; -.
DR   Ensembl; ENSBTAT00000025499; ENSBTAP00000025499; ENSBTAG00000019159.
DR   GeneID; 538603; -.
DR   KEGG; bta:538603; -.
DR   CTD; 5816; -.
DR   VEuPathDB; HostDB:ENSBTAG00000019159; -.
DR   VGNC; VGNC:33579; PVALB.
DR   eggNOG; KOG0027; Eukaryota.
DR   GeneTree; ENSGT00940000159653; -.
DR   HOGENOM; CLU_157356_0_0_1; -.
DR   InParanoid; Q0VCG3; -.
DR   OMA; ETKRMMA; -.
DR   OrthoDB; 1435392at2759; -.
DR   TreeFam; TF332342; -.
DR   Proteomes; UP000009136; Chromosome 5.
DR   Bgee; ENSBTAG00000019159; Expressed in midbrain and 69 other tissues.
DR   GO; GO:0030424; C:axon; IEA:Ensembl.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0045202; C:synapse; IEA:GOC.
DR   GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR   GO; GO:0098976; P:excitatory chemical synaptic transmission; IEA:Ensembl.
DR   GO; GO:0010467; P:gene expression; IEA:Ensembl.
DR   GO; GO:0098977; P:inhibitory chemical synaptic transmission; IEA:Ensembl.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR002048; EF_hand_dom.
DR   InterPro; IPR008080; Parvalbumin.
DR   PANTHER; PTHR11653; PTHR11653; 1.
DR   Pfam; PF13499; EF-hand_7; 1.
DR   SMART; SM00054; EFh; 2.
DR   SUPFAM; SSF47473; SSF47473; 1.
DR   PROSITE; PS00018; EF_HAND_1; 2.
DR   PROSITE; PS50222; EF_HAND_2; 2.
PE   3: Inferred from homology;
KW   Acetylation; Calcium; Metal-binding; Muscle protein; Phosphoprotein;
KW   Reference proteome; Repeat.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P80079"
FT   CHAIN           2..110
FT                   /note="Parvalbumin alpha"
FT                   /id="PRO_0000260257"
FT   DOMAIN          39..74
FT                   /note="EF-hand 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          78..110
FT                   /note="EF-hand 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         52
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         54
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         56
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         63
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         91
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         93
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         95
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         97
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         102
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250|UniProtKB:P80079"
FT   MOD_RES         2
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P02625"
FT   MOD_RES         24
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P02625"
SQ   SEQUENCE   110 AA;  12082 MW;  B5240B6252E9B62C CRC64;
     MSMTDLLHAE DIKKAVGAFT AVDSFDHKKF FQMVGLKKKS PEDVKKVFHI LDKDKSGFIE
     EEELGFILKG FSPDARDLSV KETKTLLAAG DKDGDGKIGA DEFSTLVAES