PRVB_CYPCA
ID PRVB_CYPCA Reviewed; 108 AA.
AC P02618;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Parvalbumin beta;
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, AND ACETYLATION AT ALA-1.
RX PubMed=4700462; DOI=10.1016/s0021-9258(19)44042-8;
RA Coffee C.J., Bradshaw R.A.;
RT "Carp muscle calcium-binding protein. I. Characterization of the tryptic
RT peptides and the complete amino acid sequence of component B.";
RL J. Biol. Chem. 248:3305-3312(1973).
RN [2]
RP ERRATUM OF PUBMED:4700462, AND SEQUENCE REVISION.
RA Coffee C.J., Bradshaw R.A.;
RL J. Biol. Chem. 248:6576-6576(1973).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS).
RX PubMed=4700463; DOI=10.1016/s0021-9258(19)44043-x;
RA Kretsinger R.H., Nockolds C.E.;
RT "Carp muscle calcium-binding protein. II. Structure determination and
RT general description.";
RL J. Biol. Chem. 248:3313-3326(1973).
RN [4]
RP CRYSTALLIZATION.
RX PubMed=1237627; DOI=10.1016/0022-2836(75)90162-x;
RA Moews P.C., Kretsinger R.H.;
RT "Terbium replacement of calcium in carp muscle calcium-binding parvalbumin:
RT an X-ray crystallographic study.";
RL J. Mol. Biol. 91:229-232(1975).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
RX PubMed=2777802; DOI=10.1016/s0021-9258(19)84751-8;
RA Swain A.L., Kretsinger R.H., Amma E.L.;
RT "Restrained least squares refinement of native (calcium) and cadmium-
RT substituted carp parvalbumin using X-ray crystallographic data at 1.6-A
RT resolution.";
RL J. Biol. Chem. 264:16620-16628(1989).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).
RX PubMed=2334704; DOI=10.1021/bi00458a010;
RA Kumar V.D., Lee L., Edwards B.F.P.;
RT "Refined crystal structure of calcium-liganded carp parvalbumin 4.25 at
RT 1.5-A resolution.";
RL Biochemistry 29:1404-1412(1990).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=10545326; DOI=10.1016/s0969-2126(00)80060-x;
RA Cates M.S., Berry M.B., Ho E.L., Li Q., Potter J.D., Phillips G.N. Jr.;
RT "Metal-ion affinity and specificity in EF-hand proteins: coordination
RT geometry and domain plasticity in parvalbumin.";
RL Structure 7:1269-1278(1999).
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 4.25.
CC -!- SIMILARITY: Belongs to the parvalbumin family. {ECO:0000305}.
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DR PIR; A92133; PVCAB.
DR PDB; 1B8C; X-ray; 2.00 A; A/B=1-108.
DR PDB; 1B8L; X-ray; 1.70 A; A=1-108.
DR PDB; 1B8R; X-ray; 1.90 A; A=1-108.
DR PDB; 1B9A; X-ray; 2.00 A; A=1-108.
DR PDB; 1CDP; X-ray; 1.60 A; A=1-108.
DR PDB; 4CPV; X-ray; 1.50 A; A=1-108.
DR PDB; 5CPV; X-ray; 1.60 A; A=1-108.
DR PDBsum; 1B8C; -.
DR PDBsum; 1B8L; -.
DR PDBsum; 1B8R; -.
DR PDBsum; 1B9A; -.
DR PDBsum; 1CDP; -.
DR PDBsum; 4CPV; -.
DR PDBsum; 5CPV; -.
DR AlphaFoldDB; P02618; -.
DR SMR; P02618; -.
DR Allergome; 263; Cyp c 1.
DR iPTMnet; P02618; -.
DR EvolutionaryTrace; P02618; -.
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 3D-structure; Acetylation; Calcium; Direct protein sequencing;
KW Metal-binding; Muscle protein; Reference proteome; Repeat.
FT CHAIN 1..108
FT /note="Parvalbumin beta"
FT /id="PRO_0000073606"
FT DOMAIN 38..73
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 77..108
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 57
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P02621"
FT BINDING 59
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P02621"
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:4700462"
FT TURN 3..5
FT /evidence="ECO:0007829|PDB:4CPV"
FT HELIX 8..17
FT /evidence="ECO:0007829|PDB:4CPV"
FT HELIX 26..32
FT /evidence="ECO:0007829|PDB:4CPV"
FT HELIX 35..37
FT /evidence="ECO:0007829|PDB:4CPV"
FT HELIX 40..50
FT /evidence="ECO:0007829|PDB:4CPV"
FT STRAND 55..58
FT /evidence="ECO:0007829|PDB:4CPV"
FT HELIX 60..64
FT /evidence="ECO:0007829|PDB:4CPV"
FT HELIX 66..69
FT /evidence="ECO:0007829|PDB:4CPV"
FT HELIX 79..89
FT /evidence="ECO:0007829|PDB:4CPV"
FT STRAND 94..97
FT /evidence="ECO:0007829|PDB:4CPV"
FT HELIX 99..107
FT /evidence="ECO:0007829|PDB:4CPV"
SQ SEQUENCE 108 AA; 11436 MW; AB33129FC2D79E4D CRC64;
AFAGVLNDAD IAAALEACKA ADSFNHKAFF AKVGLTSKSA DDVKKAFAII DQDKSGFIEE
DELKLFLQNF KADARALTDG ETKTFLKAGD SDGDGKIGVD EFTALVKA
