PRVB_MERBI
ID PRVB_MERBI Reviewed; 108 AA.
AC P56503;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Parvalbumin beta;
DE AltName: Full=Parvalbumin isoform B;
OS Merluccius bilinearis (Silver hake).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Zeiogadaria; Gadariae; Gadiformes; Gadoidei; Merlucciidae; Merluccius.
OX NCBI_TaxID=79698;
RN [1]
RP PROTEIN SEQUENCE, ACETYLATION AT ALA-1, AND MASS SPECTROMETRY.
RX PubMed=9385642; DOI=10.1002/pro.5560061113;
RA Revett S.P., King G., Shabanowitz J., Hunt D.F., Hartman T.M., Nelson D.J.;
RT "Characterization of a helix-loop-helix (EF hand) motif of silver hake
RT parvalbumin isoform B.";
RL Protein Sci. 6:2397-2408(1997).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS).
RX PubMed=10739249; DOI=10.1110/ps.9.1.73;
RA Richardson R.C., King N.M., Harrington D.J., Sun H., Royer W.E.,
RA Nelson D.J.;
RT "X-Ray crystal structure and molecular dynamics simulations of silver hake
RT parvalbumin (Isoform B).";
RL Protein Sci. 9:73-82(2000).
CC -!- FUNCTION: In muscle, parvalbumin is thought to be involved in
CC relaxation after contraction. It binds two calcium ions.
CC -!- MASS SPECTROMETRY: Mass=11357; Mass_error=3.5; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:9385642};
CC -!- MISCELLANEOUS: This parvalbumin has an isoelectric point of 4.2.
CC -!- SIMILARITY: Belongs to the parvalbumin family. {ECO:0000305}.
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DR PDB; 1BU3; X-ray; 1.65 A; A=1-108.
DR PDBsum; 1BU3; -.
DR AlphaFoldDB; P56503; -.
DR SMR; P56503; -.
DR iPTMnet; P56503; -.
DR EvolutionaryTrace; P56503; -.
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 Metal-binding; Muscle protein; Repeat.
FT CHAIN 1..108
FT /note="Parvalbumin beta"
FT /id="PRO_0000073613"
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:0000250|UniProtKB:P02621"
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:0000305|PubMed:9385642"
FT HELIX 8..17
FT /evidence="ECO:0007829|PDB:1BU3"
FT HELIX 26..33
FT /evidence="ECO:0007829|PDB:1BU3"
FT HELIX 35..37
FT /evidence="ECO:0007829|PDB:1BU3"
FT HELIX 40..50
FT /evidence="ECO:0007829|PDB:1BU3"
FT STRAND 55..59
FT /evidence="ECO:0007829|PDB:1BU3"
FT HELIX 60..64
FT /evidence="ECO:0007829|PDB:1BU3"
FT HELIX 66..70
FT /evidence="ECO:0007829|PDB:1BU3"
FT HELIX 79..89
FT /evidence="ECO:0007829|PDB:1BU3"
FT STRAND 94..97
FT /evidence="ECO:0007829|PDB:1BU3"
FT HELIX 99..106
FT /evidence="ECO:0007829|PDB:1BU3"
SQ SEQUENCE 108 AA; 11317 MW; 0B788EFC54002906 CRC64;
AFSGILADAD VAAALKACEA ADSFNYKAFF AKVGLTAKSA DDIKKAFFVI DQDKSGFIEE
DELKLFLQVF SAGARALTDA ETKAFLKAGD SDGDGAIGVD EWAALVKA
