PRVA_PELLE
ID PRVA_PELLE Reviewed; 109 AA.
AC P02627;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Parvalbumin alpha;
DE AltName: Full=Parvalbumin pI 4.88;
OS Pelophylax lessonae (Pool frog) (Rana lessonae).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Pelophylax.
OX NCBI_TaxID=45623;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=7042341; DOI=10.1111/j.1432-1033.1982.tb19773.x;
RA Jauregui-Adell J., Pechere J.-F., Briand G., Richet C., Demaille J.G.;
RT "Amino-acid sequence of an alpha-parvalbumin, pI = 4.88, from frog skeletal
RT muscle.";
RL Eur. J. Biochem. 123:337-345(1982).
RN [2]
RP CALCIUM-BINDING.
RX PubMed=3501318; DOI=10.1021/bi00398a020;
RA Tanokura M., Yamada K.;
RT "Heat capacity and entropy changes of the two major isotypes of bullfrog
RT (Rana catesbeiana) parvalbumins induced by calcium binding.";
RL Biochemistry 26:7668-7674(1987).
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 4.88.
CC -!- SIMILARITY: Belongs to the parvalbumin family. {ECO:0000305}.
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DR PIR; A03062; PVFGA.
DR AlphaFoldDB; P02627; -.
DR SMR; P02627; -.
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 Calcium; Direct protein sequencing; Metal-binding; Muscle protein; Repeat.
FT CHAIN 1..109
FT /note="Parvalbumin alpha"
FT /id="PRO_0000073599"
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"
SQ SEQUENCE 109 AA; 11797 MW; FD35BE18DDC76EC4 CRC64;
PMTDLLAAGD ISKAVSAFAA PESFNHKKFF ELCGLKSKSK EIMQKVFHVL DQDQSGFIEK
EELCLILKGF TPEGRSLSDK ETTALLAAGD KDGDGKIGVD EFVTLVSES
