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 27-MAR-2024, entry version 98.
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 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 SMART; SM00054; EFh; 2.
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; 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
//
