ID   PRVB_OPSTA              Reviewed;         109 AA.
AC   P05941;
DT   01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 2.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Parvalbumin beta;
DE   AltName: Full=Parvalbumin IIIF;
OS   Opsanus tau (Oyster toadfish) (Gadus tau).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Batrachoidaria; Batrachoididae; Opsanus.
OX   NCBI_TaxID=8068;
RN   [1]
RP   PROTEIN SEQUENCE, AND ACETYLATION AT SER-1.
RC   TISSUE=Fast swimbladder muscle;
RX   PubMed=2752733; DOI=10.1016/0305-0491(89)90214-9;
RA   Gerday C., Collins S., Gerardin-Otthiers N.;
RT   "The amino acid sequence of the parvalbumin from the very fast swimbladder
RT   muscle of the toadfish (Opsanus tau).";
RL   Comp. Biochem. Physiol. 93B:49-55(1989).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RX   PubMed=3965297; DOI=10.1016/0014-5793(85)80207-6;
RA   Kahn R., Fourme R., Bosshard R., Chiadmi M., Risler J.-L., Dideberg O.,
RA   Wery J.P.;
RT   "Crystal structure study of Opsanus tau parvalbumin by multiwavelength
RT   anomalous diffraction.";
RL   FEBS Lett. 179:133-137(1985).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS).
RA   Wery J.P., Dideberg O., Charlier P., Gerday C.;
RT   "Crystallization and structure at 3.2-A resolution of a terbium
RT   parvalbumin.";
RL   FEBS Lett. 182:103-106(1985).
CC   -!- FUNCTION: In muscle, parvalbumin is thought to be involved in
CC       relaxation after contraction. It binds two calcium ions.
CC   -!- MISCELLANEOUS: Three parvalbumin isotypes, in nearly equal proportion,
CC       are found in toadfish white trunk muscle whereas only one main
CC       component (IIIF) is present in the swimbladder muscle of adult
CC       specimens.
CC   -!- SIMILARITY: Belongs to the parvalbumin family. {ECO:0000305}.
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DR   PIR; JL0094; PVTFB3.
DR   AlphaFoldDB; P05941; -.
DR   SMR; P05941; -.
DR   iPTMnet; P05941; -.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
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   1: Evidence at protein level;
KW   Acetylation; Calcium; Direct protein sequencing; Metal-binding;
KW   Muscle protein; Repeat.
FT   CHAIN           1..109
FT                   /note="Parvalbumin beta"
FT                   /id="PRO_0000073616"
FT   DOMAIN          38..73
FT                   /note="EF-hand 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          77..109
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-acetylserine"
FT                   /evidence="ECO:0000269|PubMed:2752733"
SQ   SEQUENCE   109 AA;  11757 MW;  2C90F7738AD4E542 CRC64;
     SFAGILSDAD IDAALAACQA AESFKHKEFF AKVGLSAKTP DVIKKAFYVI DQDKSGFIEE
     DELKLFLQNF ASSARALTDK ETETFLKAGD SDGDGKIGID EFADLVKEA