PRVB_MERMR
ID PRVB_MERMR Reviewed; 108 AA.
AC P02621;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Parvalbumin beta;
OS Merlangius merlangus (Whiting) (Gadus merlangus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Zeiogadaria; Gadariae; Gadiformes; Gadoidei; Gadidae; Merlangius.
OX NCBI_TaxID=8058;
RN [1]
RP PROTEIN SEQUENCE, AND ACETYLATION AT ALA-1.
RC TISSUE=Muscle;
RX PubMed=318435; DOI=10.1016/0305-0491(77)90166-3;
RA Joassin L., Gerday C.;
RT "The amino acid sequence of the major parvalbumin of the whiting (Gadus
RT merlangus).";
RL Comp. Biochem. Physiol. 57B:159-161(1977).
RN [2]
RP CALCIUM-BINDING.
RX PubMed=6773772; DOI=10.1111/j.1432-1033.1980.tb04796.x;
RA Permyakov E.A., Yarmolenko V.V., Emelyanenko V.I., Burstein E.A.,
RA Closset J., Gerday C.;
RT "Fluorescence studies of the calcium binding to whiting (Gadus merlangus)
RT parvalbumin.";
RL Eur. J. Biochem. 109:307-315(1980).
RN [3]
RP CALCIUM-BINDING DATA.
RX PubMed=3390436; DOI=10.1021/bi00409a036;
RA White H.D.;
RT "Kinetic mechanism of calcium binding to whiting parvalbumin.";
RL Biochemistry 27:3357-3365(1988).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), AND SEQUENCE REVISION TO 11-12.
RC TISSUE=Muscle;
RA Declercq J.P., Baneres J.L., Rambaud J., Parello J.;
RL Submitted (MAR-1998) to the PDB data bank.
CC -!- FUNCTION: In muscle, parvalbumin is thought to be involved in
CC relaxation after contraction. It binds two calcium ions.
CC -!- MISCELLANEOUS: This parvalbumin has an isoelectric point of 4.50.
CC -!- SIMILARITY: Belongs to the parvalbumin family. {ECO:0000305}.
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DR PIR; A03056; PVWI.
DR PDB; 1A75; X-ray; 1.90 A; A/B=1-108.
DR PDBsum; 1A75; -.
DR AlphaFoldDB; P02621; -.
DR SMR; P02621; -.
DR iPTMnet; P02621; -.
DR EvolutionaryTrace; P02621; -.
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 3D-structure; Acetylation; Calcium; Direct protein sequencing;
KW Disulfide bond; Metal-binding; Muscle protein; Repeat.
FT CHAIN 1..108
FT /note="Parvalbumin beta"
FT /id="PRO_0000073615"
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 ECO:0000269|Ref.4, ECO:0007744|PDB:1A75"
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 ECO:0000269|Ref.4, ECO:0007744|PDB:1A75"
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 ECO:0000269|Ref.4, ECO:0007744|PDB:1A75"
FT BINDING 57
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|Ref.4, ECO:0007744|PDB:1A75"
FT BINDING 59
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|Ref.4, ECO:0007744|PDB:1A75"
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 ECO:0000269|Ref.4, ECO:0007744|PDB:1A75"
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 ECO:0000269|Ref.4, ECO:0007744|PDB:1A75"
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 ECO:0000269|Ref.4, ECO:0007744|PDB:1A75"
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 ECO:0000269|Ref.4, ECO:0007744|PDB:1A75"
FT BINDING 96
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|Ref.4, ECO:0007744|PDB:1A75"
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 ECO:0000269|Ref.4, ECO:0007744|PDB:1A75"
FT MOD_RES 1
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:318435"
FT DISULFID 11..33
FT /evidence="ECO:0000269|Ref.4, ECO:0007744|PDB:1A75"
FT TURN 3..6
FT /evidence="ECO:0007829|PDB:1A75"
FT HELIX 9..17
FT /evidence="ECO:0007829|PDB:1A75"
FT HELIX 26..32
FT /evidence="ECO:0007829|PDB:1A75"
FT HELIX 40..50
FT /evidence="ECO:0007829|PDB:1A75"
FT STRAND 55..59
FT /evidence="ECO:0007829|PDB:1A75"
FT HELIX 60..63
FT /evidence="ECO:0007829|PDB:1A75"
FT HELIX 66..70
FT /evidence="ECO:0007829|PDB:1A75"
FT HELIX 79..89
FT /evidence="ECO:0007829|PDB:1A75"
FT STRAND 94..97
FT /evidence="ECO:0007829|PDB:1A75"
FT HELIX 99..106
FT /evidence="ECO:0007829|PDB:1A75"
SQ SEQUENCE 108 AA; 11323 MW; 4AA2ACDD29334FB2 CRC64;
AFAGILADAD CAAAVKACEA ADSFSYKAFF AKCGLSGKSA DDIKKAFVFI DQDKSGFIEE
DELKLFLQVF KAGARALTDA ETKAFLKAGD SDGDGAIGVE EWVALVKA
