PRV7_DANRE
ID PRV7_DANRE Reviewed; 109 AA.
AC Q804W2; Q6DGT3;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Parvalbumin-7;
DE AltName: Full=Parvalbumin alpha;
DE AltName: Full=Parvalbumin-4a;
GN Name=pvalb7; Synonyms=pvalb;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAO33398.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=AB;
RA Hsiao C.-D., Tsai W.-Y., Tsai H.-J.;
RT "Molecular cloning and developmental expression of parvalbumin genes in
RT zebrafish.";
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAO33398.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain {ECO:0000312|EMBL:AAH76256.1};
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
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:0000255}.
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DR EMBL; AF467912; AAO33398.1; -; mRNA.
DR EMBL; BC076256; AAH76256.1; -; mRNA.
DR RefSeq; NP_991137.2; NM_205574.2.
DR RefSeq; XP_005161849.1; XM_005161792.1.
DR RefSeq; XP_017208596.1; XM_017353107.1.
DR AlphaFoldDB; Q804W2; -.
DR SMR; Q804W2; -.
DR STRING; 7955.ENSDARP00000113048; -.
DR PaxDb; Q804W2; -.
DR Ensembl; ENSDART00000040761; ENSDARP00000040760; ENSDARG00000034705.
DR Ensembl; ENSDART00000129859; ENSDARP00000109181; ENSDARG00000109277.
DR Ensembl; ENSDART00000131386; ENSDARP00000113048; ENSDARG00000034705.
DR Ensembl; ENSDART00000132702; ENSDARP00000122628; ENSDARG00000034705.
DR Ensembl; ENSDART00000183161; ENSDARP00000147039; ENSDARG00000034705.
DR Ensembl; ENSDART00000189515; ENSDARP00000148703; ENSDARG00000034705.
DR GeneID; 402807; -.
DR KEGG; dre:402807; -.
DR CTD; 402807; -.
DR ZFIN; ZDB-GENE-040718-285; pvalb7.
DR eggNOG; KOG0027; Eukaryota.
DR GeneTree; ENSGT00940000159653; -.
DR HOGENOM; CLU_157356_0_0_1; -.
DR InParanoid; Q804W2; -.
DR OMA; HRKFFEM; -.
DR OrthoDB; 1435392at2759; -.
DR PhylomeDB; Q804W2; -.
DR TreeFam; TF332342; -.
DR PRO; PR:Q804W2; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 22.
DR Bgee; ENSDARG00000034705; Expressed in pharyngeal gill and 15 other tissues.
DR ExpressionAtlas; Q804W2; baseline and differential.
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 3: Inferred from homology;
KW Acetylation; Calcium; Metal-binding; Muscle protein; Reference proteome;
KW Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..109
FT /note="Parvalbumin-7"
FT /id="PRO_0000073593"
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:0000250"
FT CONFLICT 6
FT /note="L -> I (in Ref. 1; AAO33398)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 109 AA; 12029 MW; 239DBF5D98E74600 CRC64;
MAMKNLLKDD DIKKALDQFK AADSFDHKKF FDVVGLKALS ADNVKLVFKA LDVDASGFIE
EEELKFVLKG FSADGRDLTD KETKAFLAAA DKDGDGKIGI DEFEALVHE
