PRVM_CHICK
ID PRVM_CHICK Reviewed; 109 AA.
AC P80026;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Parvalbumin, muscle;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP PROTEIN SEQUENCE, AND ACETYLATION AT ALA-1.
RX PubMed=1888741; DOI=10.1021/bi00100a012;
RA Kuster T., Staudenmann W., Hughes G.J., Heizmann C.W.;
RT "Parvalbumin isoforms in chicken muscle and thymus. Amino acid sequence
RT analysis of muscle parvalbumin by tandem mass spectrometry.";
RL Biochemistry 30:8812-8816(1991).
RN [2]
RP PROTEIN SEQUENCE.
RX PubMed=1958191; DOI=10.1016/s0006-291x(05)81406-8;
RA Brewer J.M., Arnold J., Beach G.G., Ragland W.L., Wunderlich J.K.;
RT "Comparison of the amino acid sequences of tissue-specific parvalbumins
RT from chicken muscle and thymus and possible evolutionary significance.";
RL Biochem. Biophys. Res. Commun. 181:226-231(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 57-101.
RX PubMed=1708248; DOI=10.1016/0006-291x(91)90928-z;
RA Palmisano W.A., Henzl M.T.;
RT "Avian thymic hormone and chicken (muscle) parvalbumin are distinct
RT proteins: isolation of a muscle parvalbumin cDNA fragment by PCR.";
RL Biochem. Biophys. Res. Commun. 176:328-334(1991).
CC -!- FUNCTION: In muscle, parvalbumin is thought to be involved in
CC relaxation after contraction. It binds two calcium ions (By
CC similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: This parvalbumin has an isoelectric point of 5.2.
CC -!- SIMILARITY: Belongs to the parvalbumin family. {ECO:0000305}.
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DR EMBL; M65068; AAA49004.1; -; mRNA.
DR PIR; JT0973; PVCHA.
DR AlphaFoldDB; P80026; -.
DR SMR; P80026; -.
DR BioGRID; 676708; 1.
DR IntAct; P80026; 1.
DR STRING; 9031.ENSGALP00000020426; -.
DR Allergome; 6107; Gal d 8.
DR iPTMnet; P80026; -.
DR PaxDb; P80026; -.
DR VEuPathDB; HostDB:geneid_396459; -.
DR eggNOG; KOG0027; Eukaryota.
DR HOGENOM; CLU_157356_0_0_1; -.
DR PRO; PR:P80026; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
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 Acetylation; Calcium; Direct protein sequencing; Metal-binding;
KW Muscle protein; Reference proteome; Repeat.
FT CHAIN 1..109
FT /note="Parvalbumin, muscle"
FT /id="PRO_0000073625"
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 MOD_RES 1
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:1888741"
FT CONFLICT 61
FT /note="E -> D (in Ref. 3; AAA49004)"
FT /evidence="ECO:0000305"
FT CONFLICT 99..101
FT /note="ADE -> VEK (in Ref. 3; AAA49004)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 109 AA; 11942 MW; 1226953FBA63E9CB CRC64;
AMTDVLSAED IKKAVGAFSA AESFNYKKFF EMVGLKKKSP EDVKKVFHIL DKDRSGFIEE
EELKFVLKGF TPDGRDLSDK ETKALLAAGD KDGDGKIGAD EFATMVAES
