PRVA_RAT
ID PRVA_RAT Reviewed; 110 AA.
AC P02625; A0JN21;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Parvalbumin alpha;
GN Name=Pvalb; Synonyms=Pva;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3009434; DOI=10.1016/s0021-9258(17)38466-1;
RA Epstein P., Means A.R., Berchtold M.W.;
RT "Isolation of a rat parvalbumin gene and full length cDNA.";
RL J. Biol. Chem. 261:5886-5891(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3036821; DOI=10.1016/s0021-9258(18)47470-4;
RA Berchtold M.W., Epstein P., Beaudet A.L., Payne M.E., Heizmann C.W.,
RA Means A.R.;
RT "Structural organization and chromosomal assignment of the parvalbumin
RT gene.";
RL J. Biol. Chem. 262:8696-8701(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 PROTEIN SEQUENCE OF 2-110, AND ACETYLATION AT SER-2.
RX PubMed=6754379; DOI=10.1111/j.1432-1033.1982.tb06883.x;
RA Berchtold M.W., Heizmann C.W., Wilson K.J.;
RT "Primary structure of parvalbumin from rat skeletal muscle.";
RL Eur. J. Biochem. 127:381-389(1982).
RN [5]
RP PROTEIN SEQUENCE OF 15-29; 47-69 AND 98-110, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
RA Lubec G., Diao W.;
RL Submitted (APR-2007) to UniProtKB.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 35-55 AND 84-92.
RX PubMed=3856270; DOI=10.1073/pnas.82.5.1414;
RA Berchtold M.W., Means A.R.;
RT "The Ca2+-binding protein parvalbumin: molecular cloning and developmental
RT regulation of mRNA abundance.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:1414-1418(1985).
RN [7]
RP CALCIUM-BINDING.
RX PubMed=3707914; DOI=10.1021/bi00355a057;
RA Williams T.C., Corson D.C., Oikawa K., McCubbin W.D., Kay C.M., Sykes B.D.;
RT "1H NMR spectroscopic studies of calcium-binding proteins. 3. Solution
RT conformations of rat apo-alpha-parvalbumin and metal-bound rat alpha-
RT parvalbumin.";
RL Biochemistry 25:1835-1846(1986).
RN [8]
RP 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 [9]
RP ACETYLATION AT SER-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RA Lubec G., Chen W.-Q.;
RL Submitted (FEB-2007) to UniProtKB.
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-8; SER-24 AND SER-66,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=8289291; DOI=10.1006/jmbi.1994.1023;
RA McPhalen C.A., Sielecki A.R., Santarsiero B.D., James M.N.G.;
RT "Refined crystal structure of rat parvalbumin, a mammalian alpha-lineage
RT parvalbumin, at 2.0-A resolution.";
RL J. Mol. Biol. 235:718-732(1994).
CC -!- FUNCTION: In muscle, parvalbumin is thought to be involved in
CC relaxation after contraction. It binds two calcium ions.
CC -!- MASS SPECTROMETRY: Mass=11836.88; Mass_error=1.57; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:10036163};
CC -!- SIMILARITY: Belongs to the parvalbumin family. {ECO:0000305}.
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DR EMBL; M12725; AAA41799.1; -; mRNA.
DR EMBL; M15457; AAA41800.1; -; Genomic_DNA.
DR EMBL; M15453; AAA41800.1; JOINED; Genomic_DNA.
DR EMBL; M15454; AAA41800.1; JOINED; Genomic_DNA.
DR EMBL; M15455; AAA41800.1; JOINED; Genomic_DNA.
DR EMBL; BC126090; AAI26091.1; -; mRNA.
DR EMBL; M10764; AAA41797.1; -; mRNA.
DR EMBL; M10765; AAA41798.1; -; mRNA.
DR PIR; A29308; PVRTA.
DR RefSeq; NP_071944.1; NM_022499.2.
DR RefSeq; XP_006241991.1; XM_006241929.3.
DR PDB; 1G33; X-ray; 1.44 A; A=38-110.
DR PDB; 1RTP; X-ray; 2.00 A; 1/2/3=2-110.
DR PDB; 1RWY; X-ray; 1.05 A; A/B/C=2-110.
DR PDB; 1S3P; X-ray; 2.00 A; A=2-110.
DR PDB; 1XVJ; X-ray; 1.80 A; A/B=2-110.
DR PDB; 2JWW; NMR; -; A=2-110.
DR PDB; 3F45; X-ray; 2.00 A; A=2-110.
DR PDBsum; 1G33; -.
DR PDBsum; 1RTP; -.
DR PDBsum; 1RWY; -.
DR PDBsum; 1S3P; -.
DR PDBsum; 1XVJ; -.
DR PDBsum; 2JWW; -.
DR PDBsum; 3F45; -.
DR AlphaFoldDB; P02625; -.
DR BMRB; P02625; -.
DR SMR; P02625; -.
DR STRING; 10116.ENSRNOP00000058825; -.
DR iPTMnet; P02625; -.
DR PhosphoSitePlus; P02625; -.
DR PaxDb; P02625; -.
DR PRIDE; P02625; -.
DR ABCD; P02625; 4 sequenced antibodies.
DR GeneID; 25269; -.
DR KEGG; rno:25269; -.
DR UCSC; RGD:3457; rat.
DR CTD; 5816; -.
DR RGD; 3457; Pvalb.
DR VEuPathDB; HostDB:ENSRNOG00000006471; -.
DR eggNOG; KOG0027; Eukaryota.
DR HOGENOM; CLU_157356_0_0_1; -.
DR InParanoid; P02625; -.
DR OMA; ETKRMMA; -.
DR OrthoDB; 1435392at2759; -.
DR PhylomeDB; P02625; -.
DR TreeFam; TF332342; -.
DR EvolutionaryTrace; P02625; -.
DR PRO; PR:P02625; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000006471; Expressed in quadriceps femoris and 17 other tissues.
DR Genevisible; P02625; RN.
DR GO; GO:0030424; C:axon; ISO:RGD.
DR GO; GO:0032437; C:cuticular plate; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0032420; C:stereocilium; IDA:RGD.
DR GO; GO:0043195; C:terminal bouton; HDA:ParkinsonsUK-UCL.
DR GO; GO:0005509; F:calcium ion binding; IDA:RGD.
DR GO; GO:0042802; F:identical protein binding; IPI:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0090102; P:cochlea development; IEP:RGD.
DR GO; GO:0098976; P:excitatory chemical synaptic transmission; ISO:RGD.
DR GO; GO:0010467; P:gene expression; ISO:RGD.
DR GO; GO:0098977; P:inhibitory chemical synaptic transmission; ISO:RGD.
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; Phosphoprotein; Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:10036163,
FT ECO:0000269|PubMed:6754379, ECO:0000269|Ref.9"
FT CHAIN 2..110
FT /note="Parvalbumin alpha"
FT /id="PRO_0000073592"
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 ECO:0000269|PubMed:6754379, ECO:0000269|Ref.9"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 66
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT HELIX 3..6
FT /evidence="ECO:0007829|PDB:1RWY"
FT HELIX 9..17
FT /evidence="ECO:0007829|PDB:1RWY"
FT HELIX 22..25
FT /evidence="ECO:0007829|PDB:2JWW"
FT HELIX 27..33
FT /evidence="ECO:0007829|PDB:1RWY"
FT HELIX 36..38
FT /evidence="ECO:0007829|PDB:1RWY"
FT HELIX 41..51
FT /evidence="ECO:0007829|PDB:1RWY"
FT STRAND 52..55
FT /evidence="ECO:0007829|PDB:2JWW"
FT STRAND 56..59
FT /evidence="ECO:0007829|PDB:1RWY"
FT HELIX 61..65
FT /evidence="ECO:0007829|PDB:1RWY"
FT HELIX 67..71
FT /evidence="ECO:0007829|PDB:1RWY"
FT HELIX 80..90
FT /evidence="ECO:0007829|PDB:1RWY"
FT TURN 91..94
FT /evidence="ECO:0007829|PDB:2JWW"
FT STRAND 95..99
FT /evidence="ECO:0007829|PDB:1RWY"
FT HELIX 100..108
FT /evidence="ECO:0007829|PDB:1RWY"
SQ SEQUENCE 110 AA; 11926 MW; 6A1509AC8F012B3D CRC64;
MSMTDLLSAE DIKKAIGAFT AADSFDHKKF FQMVGLKKKS ADDVKKVFHI LDKDKSGFIE
EDELGSILKG FSSDARDLSA KETKTLMAAG DKDGDGKIGV EEFSTLVAES
