PRVA_CYPCA
ID PRVA_CYPCA Reviewed; 109 AA.
AC P09227;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Parvalbumin alpha;
DE AltName: Full=A1;
OS Cyprinus carpio (Common carp).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Cyprininae; Cyprinus.
OX NCBI_TaxID=7962;
RN [1]
RP PROTEIN SEQUENCE OF 2-109, AND ACETYLATION AT ALA-2.
RX PubMed=4611157; DOI=10.1007/978-1-4684-0943-7_11;
RA Coffee C.J., Bradshaw R.A., Kretsinger R.H.;
RT "The coordination of calcium ions by carp muscle calcium binding proteins
RT A, B and C.";
RL Adv. Exp. Med. Biol. 48:211-233(1974).
RN [2]
RP CALCIUM-BINDING.
RX PubMed=6438069; DOI=10.1093/oxfordjournals.jbchem.a134841;
RA Iio T., Hoshihara Y.;
RT "Static and kinetic studies on carp muscle parvalbumins.";
RL J. Biochem. 96:321-328(1984).
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 4.47.
CC -!- SIMILARITY: Belongs to the parvalbumin family. {ECO:0000305}.
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DR Allergome; 263; Cyp c 1.
DR iPTMnet; P09227; -.
DR Proteomes; UP000694384; Unplaced.
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 Acetylation; Calcium; Direct protein sequencing; Metal-binding;
KW Muscle protein; Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:4611157"
FT CHAIN 2..109
FT /note="Parvalbumin alpha"
FT /id="PRO_0000073594"
FT DOMAIN 39..74
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 78..109
FT /note="EF-hand 2"
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 56
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 63
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
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 97
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 102
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:4611157"
SQ SEQUENCE 109 AA; 11451 MW; 1A06E77CB9AF7739 CRC64;
MAYGGILNDA DITAALEACX AXDSFNAKSF FAKVGLSAKT PDDIKKAFAV IDQDKSGFIE
EDELKLFLQN FSAGARALTD AETKAFLKAG DSDGDGKIGV DEFAALVKA
