ID   PRVB_MERME              Reviewed;         108 AA.
AC   P02620;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   27-NOV-2024, entry version 99.
DE   RecName: Full=Parvalbumin beta;
OS   Merluccius merluccius (European hake).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Zeiogadaria; Gadariae; Gadiformes; Gadoidei; Merlucciidae; Merluccius.
OX   NCBI_TaxID=8063;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=4569071; DOI=10.1111/j.1432-1033.1973.tb02584.x;
RA   Capony J.-P., Ryden L., Demaille J.G., Pechere J.-F.;
RT   "The primary structure of the major parvalbumin from hake muscle.
RT   Overlapping peptides obtained with chemical and enzymatic methods. The
RT   complete amino-acid sequence.";
RL   Eur. J. Biochem. 32:97-108(1973).
RN   [2]
RP   PROTEIN SEQUENCE, MASS SPECTROMETRY, AND ACETYLATION AT ALA-1.
RC   TISSUE=Muscle;
RX   PubMed=20586483; DOI=10.1021/pr100163e;
RA   Carrera M., Canas B., Vazquez J., Gallardo J.M.;
RT   "Extensive de novo sequencing of new parvalbumin isoforms using a novel
RT   combination of bottom-up proteomics, accurate molecular mass measurement by
RT   FTICR-MS, and selected MS/MS ion monitoring.";
RL   J. Proteome Res. 9:4393-4406(2010).
CC   -!- FUNCTION: In muscle, parvalbumin is thought to be involved in
CC       relaxation after contraction. It binds two calcium ions.
CC   -!- MASS SPECTROMETRY: Mass=11329.746; Mass_error=0.0013;
CC       Method=Electrospray; Evidence={ECO:0000269|PubMed:20586483};
CC   -!- MISCELLANEOUS: This is the major hake parvalbumin.
CC   -!- MISCELLANEOUS: This parvalbumin has an isoelectric point of 4.36.
CC   -!- MISCELLANEOUS: Is regarded as an important allergen.
CC   -!- SIMILARITY: Belongs to the parvalbumin family. {ECO:0000305}.
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DR   PIR; A03055; PVHK.
DR   AlphaFoldDB; P02620; -.
DR   SMR; P02620; -.
DR   Allergome; 7643; Mer mr 1.
DR   iPTMnet; P02620; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   CDD; cd16255; EFh_parvalbumin_beta; 1.
DR   FunFam; 1.10.238.10:FF:000060; Parvalbumin, thymic; 1.
DR   Gene3D; 1.10.238.10; EF-hand; 1.
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:SF12; PARVALBUMIN; 1.
DR   PANTHER; PTHR11653; PARVALBUMIN ALPHA; 1.
DR   Pfam; PF13499; EF-hand_7; 1.
DR   PRINTS; PR01697; PARVALBUMIN.
DR   SUPFAM; SSF47473; EF-hand; 1.
DR   PROSITE; PS00018; EF_HAND_1; 2.
DR   PROSITE; PS50222; EF_HAND_2; 2.
PE   1: Evidence at protein level;
KW   Acetylation; Allergen; Calcium; Direct protein sequencing; Metal-binding;
KW   Muscle protein; Repeat.
FT   CHAIN           1..108
FT                   /note="Parvalbumin beta"
FT                   /id="PRO_0000073614"
FT   DOMAIN          38..73
FT                   /note="EF-hand 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          77..108
FT                   /note="EF-hand 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         51
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         53
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         55
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         57
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P02621"
FT   BINDING         59
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P02621"
FT   BINDING         62
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         90
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         92
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         94
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         96
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         101
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   MOD_RES         1
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000269|PubMed:20586483,
FT                   ECO:0000269|PubMed:4569071"
SQ   SEQUENCE   108 AA;  11295 MW;  E5526ACBF3DC3B64 CRC64;
     AFAGILADAD ITAALAACKA EGSFKHGEFF TKIGLKGKSA ADIKKVFGII DQDKSDFVEE
     DELKLFLQNF SAGARALTDA ETATFLKAGD SDGDGKIGVE EFAAMVKG
//