PRVB_ESOLU
ID PRVB_ESOLU Reviewed; 107 AA.
AC P02619;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Parvalbumin beta;
DE AltName: Full=Parvalbumin II;
DE AltName: Full=Parvalbumin pI 4.10;
DE AltName: Full=Parvalbumin-2;
OS Esox lucius (Northern pike).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Esociformes;
OC Esocidae; Esox.
OX NCBI_TaxID=8010;
RN [1]
RP PROTEIN SEQUENCE, AND ACETYLATION AT SER-1.
RX PubMed=1009932; DOI=10.1111/j.1432-1033.1976.tb10982.x;
RA Gerday C.;
RT "The primary structure of the parvalbumin II of pike (Esox lucius).";
RL Eur. J. Biochem. 70:305-318(1976).
RN [2]
RP CALCIUM-BINDING.
RX PubMed=6639084; DOI=10.1016/0003-9861(83)90343-0;
RA Permyakov E.A., Medvedkin V.N., Kalinichenko L.P., Burstein E.A.;
RT "Comparative study of physiochemical properties of two pike parvalbumins by
RT means of their intrinsic tyrosyl and phenylalanyl fluorescence.";
RL Arch. Biochem. Biophys. 227:9-20(1983).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS).
RX PubMed=3172221; DOI=10.1016/0022-2836(88)90464-0;
RA Declercq J.-P., Tinant B., Parello J., Etienne G., Huber R.;
RT "Crystal structure determination and refinement of pike 4.10 parvalbumin
RT (minor component from Esox lucius).";
RL J. Mol. Biol. 202:349-353(1988).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS).
RX PubMed=1880797; DOI=10.1016/0022-2836(91)90369-h;
RA Declercq J.-P., Tinant B., Parello J., Rambaud J.;
RT "Ionic interactions with parvalbumins. Crystal structure determination of
RT pike 4.10 parvalbumin in four different ionic environments.";
RL J. Mol. Biol. 220:1017-1039(1991).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS).
RX PubMed=15299738; DOI=10.1107/s0907444995010006;
RA Declercq J.-P., Tinant B., Parello J.;
RT "X-ray structure of a new crystal form of pike 4.10 beta parvalbumin.";
RL Acta Crystallogr. D 52:165-169(1996).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (0.91 ANGSTROMS).
RX PubMed=10548066; DOI=10.1110/ps.8.10.2194;
RA Declercq J.-P., Evrard C., Lamzin V., Parello J.;
RT "Crystal structure of the EF-hand parvalbumin at atomic resolution (0.91 A)
RT and at low temperature (100 K). Evidence for conformational multistates
RT within the hydrophobic core.";
RL Protein Sci. 8:2194-2204(1999).
CC -!- FUNCTION: In muscle, parvalbumin is thought to be involved in
CC relaxation after contraction. It binds two calcium ions.
CC -!- MISCELLANEOUS: This is one of two major parvalbumins found in the white
CC muscle of pike.
CC -!- MISCELLANEOUS: This parvalbumin has an isoelectric point of 4.10.
CC -!- SIMILARITY: Belongs to the parvalbumin family. {ECO:0000305}.
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DR PIR; A03054; PVPK2.
DR PDB; 1PAL; X-ray; 1.65 A; A=1-107.
DR PDB; 1PVB; X-ray; 1.75 A; A=1-107.
DR PDB; 2PAL; X-ray; 1.80 A; A=1-107.
DR PDB; 2PVB; X-ray; 0.91 A; A=1-106.
DR PDB; 3PAL; X-ray; 2.40 A; A=1-107.
DR PDB; 4PAL; X-ray; 1.80 A; A=1-107.
DR PDBsum; 1PAL; -.
DR PDBsum; 1PVB; -.
DR PDBsum; 2PAL; -.
DR PDBsum; 2PVB; -.
DR PDBsum; 3PAL; -.
DR PDBsum; 4PAL; -.
DR AlphaFoldDB; P02619; -.
DR SMR; P02619; -.
DR STRING; 8010.XP_010862297.1; -.
DR iPTMnet; P02619; -.
DR OMA; ECEAGQC; -.
DR EvolutionaryTrace; P02619; -.
DR Proteomes; UP000265140; LG25.
DR GO; GO:0030424; C:axon; ISS:AgBase.
DR GO; GO:0043679; C:axon terminus; ISS:AgBase.
DR GO; GO:0030425; C:dendrite; ISS:AgBase.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR DisProt; DP01025; -.
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..107
FT /note="Parvalbumin beta"
FT /id="PRO_0000073607"
FT DOMAIN 37..72
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 76..107
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 50
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P02621,
FT 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:0000250|UniProtKB:P02621,
FT 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:0000250|UniProtKB:P02621,
FT 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:0000250|UniProtKB:P02621"
FT BINDING 58
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P02621"
FT BINDING 61
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P02621,
FT ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 89
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P02621,
FT 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:0000250|UniProtKB:P02621,
FT 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:0000250|UniProtKB:P02621,
FT 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 100
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P02621,
FT ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 1
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:1009932"
FT TURN 2..4
FT /evidence="ECO:0007829|PDB:4PAL"
FT HELIX 7..16
FT /evidence="ECO:0007829|PDB:2PVB"
FT HELIX 25..31
FT /evidence="ECO:0007829|PDB:2PVB"
FT HELIX 34..36
FT /evidence="ECO:0007829|PDB:2PVB"
FT HELIX 39..49
FT /evidence="ECO:0007829|PDB:2PVB"
FT STRAND 54..57
FT /evidence="ECO:0007829|PDB:2PVB"
FT HELIX 59..63
FT /evidence="ECO:0007829|PDB:2PVB"
FT HELIX 65..68
FT /evidence="ECO:0007829|PDB:2PVB"
FT HELIX 78..88
FT /evidence="ECO:0007829|PDB:2PVB"
FT STRAND 93..96
FT /evidence="ECO:0007829|PDB:2PVB"
FT HELIX 98..106
FT /evidence="ECO:0007829|PDB:2PVB"
SQ SEQUENCE 107 AA; 11390 MW; 100674BE1836D28F CRC64;
SFAGLKDADV AAALAACSAA DSFKHKEFFA KVGLASKSLD DVKKAFYVID QDKSGFIEED
ELKLFLQNFS PSARALTDAE TKAFLADGDK DGDGMIGVDE FAAMIKA
