PRVA_TRISE
ID PRVA_TRISE Reviewed; 109 AA.
AC P30563;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Parvalbumin alpha;
OS Triakis semifasciata (Leopard shark).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Elasmobranchii; Galeomorphii; Galeoidea; Carcharhiniformes; Triakidae;
OC Triakis.
OX NCBI_TaxID=30493;
RN [1]
RP X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS).
RC TISSUE=Muscle;
RX PubMed=1542115; DOI=10.1016/0022-2836(92)90985-s;
RA Roquet F., Declercq J.-P., Tinant B., Rambaud J., Parello J.;
RT "Crystal structure of the unique parvalbumin component from muscle of the
RT leopard shark (Triakis semifasciata). The first X-ray study of an alpha-
RT parvalbumin.";
RL J. Mol. Biol. 223:705-720(1992).
CC -!- FUNCTION: In muscle, parvalbumin is thought to be involved in
CC relaxation after contraction. It binds two calcium ions.
CC -!- SIMILARITY: Belongs to the parvalbumin family. {ECO:0000305}.
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DR PDB; 5PAL; X-ray; 1.54 A; A=1-109.
DR PDB; 5ZGM; X-ray; 1.40 A; A/B=1-109.
DR PDBsum; 5PAL; -.
DR PDBsum; 5ZGM; -.
DR AlphaFoldDB; P30563; -.
DR SMR; P30563; -.
DR EvolutionaryTrace; P30563; -.
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; Calcium; Metal-binding; Muscle protein; Repeat.
FT CHAIN 1..109
FT /note="Parvalbumin alpha"
FT /id="PRO_0000073601"
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 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 HELIX 2..4
FT /evidence="ECO:0007829|PDB:5ZGM"
FT HELIX 8..17
FT /evidence="ECO:0007829|PDB:5ZGM"
FT HELIX 26..32
FT /evidence="ECO:0007829|PDB:5ZGM"
FT HELIX 40..50
FT /evidence="ECO:0007829|PDB:5ZGM"
FT STRAND 55..58
FT /evidence="ECO:0007829|PDB:5ZGM"
FT HELIX 60..64
FT /evidence="ECO:0007829|PDB:5ZGM"
FT HELIX 66..70
FT /evidence="ECO:0007829|PDB:5ZGM"
FT HELIX 79..89
FT /evidence="ECO:0007829|PDB:5ZGM"
FT STRAND 94..97
FT /evidence="ECO:0007829|PDB:5ZGM"
FT HELIX 99..108
FT /evidence="ECO:0007829|PDB:5ZGM"
SQ SEQUENCE 109 AA; 11931 MW; AED1E240174CF80E CRC64;
PMTKVLKADD INKAISAFKD PGTFDYKRFF HLVGLKGKTD AQVKEVFEIL DKDQSGFIEE
EELKGVLKGF SAHGRDLNDT ETKALLAAGD SDHDGKIGAD EFAKMVAQA