PRVA_MOUSE
ID PRVA_MOUSE Reviewed; 110 AA.
AC P32848;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Parvalbumin alpha;
GN Name=Pvalb; Synonyms=Pva;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2572511; DOI=10.1017/s0016672300028354;
RA Zuehlke C.H., Schoeffl F., Jockusch H., Simon D., Guenet J.-L.;
RT "cDNA sequence and chromosomal localization of the mouse parvalbumin gene,
RT Pva.";
RL Genet. Res. 54:37-43(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=A2G; TISSUE=Fast-twitch skeletal muscle;
RX PubMed=7522680; DOI=10.1016/0960-8966(94)90021-3;
RA Schleef M., Zuehlke C., Schoeffl F., Jockusch H.;
RT "Subtractive cDNA cloning as a tool to analyse secondary effects of a
RT muscle disease. Characterization of affected genes in the myotonic ADR
RT mouse.";
RL Neuromuscul. Disord. 4:205-217(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Salivary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-103.
RX PubMed=7818852; DOI=10.1139/o94-013;
RA Chatterjee A., Butler A.M., Blum M., Warner A.H.;
RT "Characterization of parvalbumin cDNA clones and gene expression in normal
RT and dystrophic mice of strain 129 ReJ.";
RL Biochem. Cell Biol. 72:70-77(1994).
RN [5]
RP SEQUENCE REVISION TO 110, ACETYLATION AT SER-2, AND MASS SPECTROMETRY.
RC TISSUE=Skeletal muscle;
RX PubMed=10036163; DOI=10.1006/abio.1998.3015;
RA Troxler H., Kuster T., Rhyner J.A., Gehrig P., Heizmann C.W.;
RT "Electrospray ionization mass spectrometry: analysis of the Ca2+-binding
RT properties of human recombinant alpha-parvalbumin and nine mutant
RT proteins.";
RL Anal. Biochem. 268:64-71(1999).
RN [6]
RP PARTIAL PROTEIN SEQUENCE, ACETYLATION, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RA Vilbois F.;
RL Submitted (SEP-1998) to UniProtKB.
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=17977745; DOI=10.1016/j.mcn.2007.09.006;
RA Saul S.M., Brzezinski J.A. IV, Altschuler R.A., Shore S.E., Rudolph D.D.,
RA Kabara L.L., Halsey K.E., Hufnagel R.B., Zhou J., Dolan D.F., Glaser T.;
RT "Math5 expression and function in the central auditory system.";
RL Mol. Cell. Neurosci. 37:153-169(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, and Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: In muscle, parvalbumin is thought to be involved in
CC relaxation after contraction. It binds two calcium ions.
CC -!- TISSUE SPECIFICITY: Expressed in the modiolar nerve root (at protein
CC level). {ECO:0000269|PubMed:17977745}.
CC -!- MASS SPECTROMETRY: Mass=11841.21; Mass_error=0.77; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:10036163};
CC -!- SIMILARITY: Belongs to the parvalbumin family. {ECO:0000305}.
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DR EMBL; X54613; CAA38434.1; -; mRNA.
DR EMBL; X59382; CAA42025.1; -; mRNA.
DR EMBL; BC027424; AAH27424.1; -; mRNA.
DR EMBL; S75909; AAB33066.1; -; mRNA.
DR EMBL; S75910; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS27609.1; -.
DR PIR; A37414; A37414.
DR PIR; I65238; I65238.
DR RefSeq; NP_001317615.1; NM_001330686.1.
DR RefSeq; NP_038673.2; NM_013645.4.
DR AlphaFoldDB; P32848; -.
DR SMR; P32848; -.
DR BioGRID; 202517; 3.
DR STRING; 10090.ENSMUSP00000112598; -.
DR iPTMnet; P32848; -.
DR PhosphoSitePlus; P32848; -.
DR SWISS-2DPAGE; P32848; -.
DR UCD-2DPAGE; P32848; -.
DR CPTAC; non-CPTAC-3996; -.
DR jPOST; P32848; -.
DR PaxDb; P32848; -.
DR PeptideAtlas; P32848; -.
DR PRIDE; P32848; -.
DR ProteomicsDB; 291827; -.
DR ABCD; P32848; 4 sequenced antibodies.
DR Antibodypedia; 3746; 369 antibodies from 42 providers.
DR DNASU; 19293; -.
DR Ensembl; ENSMUST00000005860; ENSMUSP00000005860; ENSMUSG00000005716.
DR Ensembl; ENSMUST00000120592; ENSMUSP00000112598; ENSMUSG00000005716.
DR GeneID; 19293; -.
DR KEGG; mmu:19293; -.
DR UCSC; uc007wot.2; mouse.
DR CTD; 5816; -.
DR MGI; MGI:97821; Pvalb.
DR VEuPathDB; HostDB:ENSMUSG00000005716; -.
DR eggNOG; KOG0027; Eukaryota.
DR GeneTree; ENSGT00940000159653; -.
DR HOGENOM; CLU_157356_0_0_1; -.
DR InParanoid; P32848; -.
DR OMA; VRKVFHI; -.
DR OrthoDB; 1435392at2759; -.
DR PhylomeDB; P32848; -.
DR TreeFam; TF332342; -.
DR BioGRID-ORCS; 19293; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Pvalb; mouse.
DR PRO; PR:P32848; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; P32848; protein.
DR Bgee; ENSMUSG00000005716; Expressed in triceps brachii and 145 other tissues.
DR ExpressionAtlas; P32848; baseline and differential.
DR Genevisible; P32848; MM.
DR GO; GO:0030424; C:axon; IDA:MGI.
DR GO; GO:0032437; C:cuticular plate; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0032420; C:stereocilium; ISO:MGI.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0005509; F:calcium ion binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0098976; P:excitatory chemical synaptic transmission; IMP:MGI.
DR GO; GO:0010467; P:gene expression; IMP:MGI.
DR GO; GO:0098977; P:inhibitory chemical synaptic transmission; IMP:MGI.
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; Phosphoprotein; Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:10036163"
FT CHAIN 2..110
FT /note="Parvalbumin alpha"
FT /id="PRO_0000073590"
FT DOMAIN 39..74
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 78..110
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-acetylserine"
FT /evidence="ECO:0000269|PubMed:10036163"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02625"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02625"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02625"
FT CONFLICT 110
FT /note="S -> T (in Ref. 1; CAA38434 and 2; CAA42025)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 110 AA; 11931 MW; C54FF4FDD935F51A CRC64;
MSMTDVLSAE DIKKAIGAFA AADSFDHKKF FQMVGLKKKN PDEVKKVFHI LDKDKSGFIE
EDELGSILKG FSSDARDLSA KETKTLLAAG DKDGDGKIGV EEFSTLVAES
