PRVA_ESOLU
ID PRVA_ESOLU Reviewed; 108 AA.
AC P02628;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Parvalbumin alpha;
DE AltName: Full=Parvalbumin III;
DE AltName: Full=Parvalbumin pI 5.0;
DE AltName: Full=Parvalbumin-3;
OS Esox lucius (Northern pike).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Esociformes;
OC Esocidae; Esox.
OX NCBI_TaxID=8010;
RN [1]
RP PROTEIN SEQUENCE, AND ACETYLATION AT ALA-1.
RX PubMed=4751989; DOI=10.1016/0014-5793(73)80597-6;
RA Frankenne F., Joassin L., Gerday C.;
RT "The amino acid sequence of the pike (Esox lucius) parvalbumin 3.";
RL FEBS Lett. 35:145-147(1973).
RN [2]
RP SEQUENCE REVISION.
RA Gerday C.;
RL Submitted (JAN-1975) to the PIR data bank.
RN [3]
RP PROTEIN SEQUENCE, IDENTIFICATION BY MASS SPECTROMETRY, AND VARIANTS LEU-11
RP INS; ALA-27 AND LYS-31.
RC TISSUE=White muscle;
RX PubMed=18930845; DOI=10.1016/j.bbapap.2008.09.010;
RA Permyakov S.E., Karnoup A.S., Bakunts A.G., Permyakov E.A.;
RT "Sequence microheterogeneity of parvalbumin pI 5.0 of pike: a mass
RT spectrometric study.";
RL Biochim. Biophys. Acta 1794:129-136(2009).
RN [4]
RP STRUCTURE BY NMR.
RX PubMed=3221403; DOI=10.1016/0022-2836(88)90057-5;
RA Padilla A., Cave A., Parello J.;
RT "Two-dimensional 1H nuclear magnetic resonance study of pike pI 5.0
RT parvalbumin (Esox lucius). Sequential resonance assignments and folding of
RT the polypeptide chain.";
RL J. Mol. Biol. 204:995-1017(1988).
RN [5]
RP ERRATUM OF PUBMED:3221403.
RA Padilla A., Cave A., Parello J.;
RL J. Mol. Biol. 208:723-724(1989).
RN [6]
RP STRUCTURE BY NMR.
RX PubMed=8095405; DOI=10.1021/bi00056a015;
RA Blancuzzi Y., Padilla A., Parello J., Cave A.;
RT "Symmetrical rearrangement of the cation-binding sites of parvalbumin upon
RT Ca2+/Mg2+ exchange. A study by 1H 2D NMR.";
RL Biochemistry 32:1302-1309(1993).
RN [7]
RP STRUCTURE BY NMR.
RX PubMed=8647099; DOI=10.1111/j.1432-1033.1996.0561p.x;
RA Alattia T., Padilla A., Cave A.;
RT "Assignment of 13C resonances and analysis of relaxation properties and
RT internal dynamics of pike parvalbumin by 13C-NMR at natural abundance.";
RL Eur. J. Biochem. 237:561-574(1996).
CC -!- FUNCTION: In muscle, parvalbumin is thought to be involved in
CC relaxation after contraction. It binds two calcium ions.
CC -!- MISCELLANEOUS: This is the major component, having an isoelectric point
CC of 5.0.
CC -!- SIMILARITY: Belongs to the parvalbumin family. {ECO:0000305}.
CC -!- CAUTION: This protein is more closely related to beta-type parvalbumins
CC then to alpha-type. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR PIR; A67143; PVPK.
DR PDB; 1PVA; X-ray; 1.65 A; A/B=1-108.
DR PDB; 2PAS; NMR; -; A=1-108.
DR PDB; 3PAT; NMR; -; A=1-108.
DR PDBsum; 1PVA; -.
DR PDBsum; 2PAS; -.
DR PDBsum; 3PAT; -.
DR AlphaFoldDB; P02628; -.
DR BMRB; P02628; -.
DR SMR; P02628; -.
DR STRING; 8010.XP_010870996.1; -.
DR EvolutionaryTrace; P02628; -.
DR Proteomes; UP000265140; LG25.
DR GO; GO:0005509; F:calcium ion binding; IDA:CAFA.
DR DisProt; DP00550; -.
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; Reference proteome; Repeat.
FT CHAIN 1..108
FT /note="Parvalbumin alpha"
FT /id="PRO_0000073595"
FT DOMAIN 37..72
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 76..108
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 50
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 52
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 54
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 61
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 89
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 91
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 93
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 95
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 100
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 VARIANT 11
FT /note="K -> KL (in alpha-2)"
FT /evidence="ECO:0000269|PubMed:18930845"
FT VARIANT 27
FT /note="K -> A (in alpha-2)"
FT /evidence="ECO:0000269|PubMed:18930845"
FT VARIANT 31
FT /note="L -> K (in alpha-2)"
FT /evidence="ECO:0000269|PubMed:18930845"
FT HELIX 1..4
FT /evidence="ECO:0007829|PDB:1PVA"
FT HELIX 7..16
FT /evidence="ECO:0007829|PDB:1PVA"
FT TURN 18..21
FT /evidence="ECO:0007829|PDB:2PAS"
FT HELIX 25..31
FT /evidence="ECO:0007829|PDB:1PVA"
FT TURN 33..36
FT /evidence="ECO:0007829|PDB:2PAS"
FT HELIX 39..49
FT /evidence="ECO:0007829|PDB:1PVA"
FT STRAND 54..57
FT /evidence="ECO:0007829|PDB:1PVA"
FT HELIX 59..63
FT /evidence="ECO:0007829|PDB:1PVA"
FT HELIX 65..68
FT /evidence="ECO:0007829|PDB:1PVA"
FT HELIX 78..88
FT /evidence="ECO:0007829|PDB:1PVA"
FT STRAND 93..96
FT /evidence="ECO:0007829|PDB:1PVA"
FT HELIX 98..106
FT /evidence="ECO:0007829|PDB:1PVA"
SQ SEQUENCE 108 AA; 11707 MW; 8737BD351BA4ABC3 CRC64;
AKDLLKADDI KKALDAVKAE GSFNHKKFFA LVGLKAMSAN DVKKVFKAID ADASGFIEEE
ELKFVLKSFA ADGRDLTDAE TKAFLKAADK DGDGKIGIDE FETLVHEA
