PRVA_CAVPO
ID PRVA_CAVPO Reviewed; 95 AA.
AC P51434;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Parvalbumin alpha;
DE Flags: Fragment;
GN Name=PVALB;
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Cochlea;
RX PubMed=8750839; DOI=10.1016/0169-328x(95)00205-7;
RA Soto-Prior A., Cluzel M., Renard N., Ripoll C., Lavigne-Rebillard M.,
RA Eybalin M., Hamel C.P.;
RT "Molecular cloning and expression of alpha parvalbumin in the guinea pig
RT cochlea.";
RL Brain Res. Mol. Brain Res. 34:337-342(1995).
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 -!- SIMILARITY: Belongs to the parvalbumin family. {ECO:0000305}.
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DR EMBL; U26677; AAC52499.1; -; mRNA.
DR AlphaFoldDB; P51434; -.
DR SMR; P51434; -.
DR STRING; 10141.ENSCPOP00000019473; -.
DR eggNOG; KOG0027; Eukaryota.
DR InParanoid; P51434; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
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; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 2.
PE 2: Evidence at transcript level;
KW Calcium; Metal-binding; Muscle protein; Phosphoprotein; Reference proteome;
KW Repeat.
FT CHAIN <1..>95
FT /note="Parvalbumin alpha"
FT /id="PRO_0000073585"
FT DOMAIN 34..69
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 73..>95
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 47
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 49
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
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 58
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 86
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P20472"
FT BINDING 88
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P20472"
FT BINDING 90
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P20472"
FT BINDING 92
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P20472"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02625"
FT NON_TER 1
FT NON_TER 95
SQ SEQUENCE 95 AA; 10545 MW; 98C4740F9E76FE03 CRC64;
LLNAEDIKKA VGACAAAESF DHKKFFQMVG LKKKNREEVK MVFQILDKDK SGFIEEEELK
FILKGFSADA RDLSDTETKR MMAAGDKDGD GKIGA