PRVA_HUMAN
ID PRVA_HUMAN Reviewed; 110 AA.
AC P20472; B2R4H7; P78378; Q4VB78; Q5R3Q9;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=Parvalbumin alpha;
GN Name=PVALB;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2614829; DOI=10.1016/0022-2836(89)90119-8;
RA Berchtold M.W.;
RT "Parvalbumin genes from human and rat are identical in intron/exon
RT organization and contain highly homologous regulatory elements and coding
RT sequences.";
RL J. Mol. Biol. 210:417-427(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 2-110.
RC TISSUE=Cerebellum;
RX PubMed=8354278; DOI=10.1111/j.1432-1033.1993.tb18084.x;
RA Foehr U.G., Weber B.R., Muentener M., Staudenmann W., Hughes G.J.,
RA Frutiger S., Banville D., Schaefer B.W., Heizmann C.W.;
RT "Human alpha and beta parvalbumins. Structure and tissue-specific
RT expression.";
RL Eur. J. Biochem. 215:719-727(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cerebellum;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [8]
RP MUTAGENESIS, ACETYLATION AT SER-2, AND MASS SPECTROMETRY.
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 STRUCTURE BY NMR.
RX PubMed=15122922; DOI=10.1021/bi035879k;
RA Baig I., Bertini I., Del Bianco C., Gupta Y.K., Lee Y.M., Luchinat C.,
RA Quattrone A.;
RT "Paramagnetism-based refinement strategy for the solution structure of
RT human alpha-parvalbumin.";
RL Biochemistry 43:5562-5573(2004).
CC -!- FUNCTION: In muscle, parvalbumin is thought to be involved in
CC relaxation after contraction. It binds two calcium ions.
CC -!- MASS SPECTROMETRY: Mass=11927; Mass_error=0.76; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:10036163};
CC -!- SIMILARITY: Belongs to the parvalbumin family. {ECO:0000305}.
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DR EMBL; X63578; CAA45134.1; -; Genomic_DNA.
DR EMBL; X52695; CAA36924.1; -; Genomic_DNA.
DR EMBL; X52696; CAA36924.1; JOINED; Genomic_DNA.
DR EMBL; X52697; CAA36924.1; JOINED; Genomic_DNA.
DR EMBL; X52698; CAA36924.1; JOINED; Genomic_DNA.
DR EMBL; X63070; CAA44792.1; -; mRNA.
DR EMBL; CR456552; CAG30438.1; -; mRNA.
DR EMBL; AK311832; BAG34774.1; -; mRNA.
DR EMBL; Z82184; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z82185; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471095; EAW60118.1; -; Genomic_DNA.
DR EMBL; BC069300; AAH69300.1; -; mRNA.
DR EMBL; BC096112; AAH96112.1; -; mRNA.
DR EMBL; BC096113; AAH96113.1; -; mRNA.
DR EMBL; BC096114; AAH96114.1; -; mRNA.
DR EMBL; BC096115; AAH96115.1; -; mRNA.
DR CCDS; CCDS13933.1; -.
DR PIR; S07531; S07531.
DR RefSeq; NP_001302461.1; NM_001315532.1.
DR RefSeq; NP_002845.1; NM_002854.2.
DR PDB; 1RJV; NMR; -; A=1-110.
DR PDB; 1RK9; NMR; -; A=2-110.
DR PDBsum; 1RJV; -.
DR PDBsum; 1RK9; -.
DR AlphaFoldDB; P20472; -.
DR BMRB; P20472; -.
DR SMR; P20472; -.
DR BioGRID; 111774; 2.
DR IntAct; P20472; 1.
DR STRING; 9606.ENSP00000216200; -.
DR DrugBank; DB01942; Formic acid.
DR iPTMnet; P20472; -.
DR PhosphoSitePlus; P20472; -.
DR BioMuta; PVALB; -.
DR DMDM; 131100; -.
DR EPD; P20472; -.
DR MassIVE; P20472; -.
DR PaxDb; P20472; -.
DR PeptideAtlas; P20472; -.
DR PRIDE; P20472; -.
DR ProteomicsDB; 53761; -.
DR Antibodypedia; 3746; 369 antibodies from 42 providers.
DR DNASU; 5816; -.
DR Ensembl; ENST00000216200.9; ENSP00000216200.5; ENSG00000100362.13.
DR Ensembl; ENST00000417718.7; ENSP00000400247.2; ENSG00000100362.13.
DR Ensembl; ENST00000620986.3; ENSP00000480913.1; ENSG00000274665.3.
DR Ensembl; ENST00000625893.2; ENSP00000486144.1; ENSG00000274665.3.
DR GeneID; 5816; -.
DR KEGG; hsa:5816; -.
DR MANE-Select; ENST00000417718.7; ENSP00000400247.2; NM_001315532.2; NP_001302461.1.
DR UCSC; uc003apx.4; human.
DR CTD; 5816; -.
DR DisGeNET; 5816; -.
DR GeneCards; PVALB; -.
DR HGNC; HGNC:9704; PVALB.
DR HPA; ENSG00000100362; Tissue enriched (parathyroid).
DR MIM; 168890; gene.
DR neXtProt; NX_P20472; -.
DR OpenTargets; ENSG00000100362; -.
DR PharmGKB; PA34049; -.
DR VEuPathDB; HostDB:ENSG00000100362; -.
DR eggNOG; KOG0027; Eukaryota.
DR GeneTree; ENSGT00940000159653; -.
DR InParanoid; P20472; -.
DR OMA; VRKVFHI; -.
DR OrthoDB; 1435392at2759; -.
DR PhylomeDB; P20472; -.
DR TreeFam; TF332342; -.
DR PathwayCommons; P20472; -.
DR Reactome; R-HSA-8986944; Transcriptional Regulation by MECP2.
DR SignaLink; P20472; -.
DR BioGRID-ORCS; 5816; 12 hits in 1070 CRISPR screens.
DR ChiTaRS; PVALB; human.
DR EvolutionaryTrace; P20472; -.
DR GenomeRNAi; 5816; -.
DR Pharos; P20472; Tbio.
DR PRO; PR:P20472; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; P20472; protein.
DR Bgee; ENSG00000100362; Expressed in right hemisphere of cerebellum and 93 other tissues.
DR ExpressionAtlas; P20472; baseline and differential.
DR Genevisible; P20472; HS.
DR GO; GO:0030424; C:axon; IEA:Ensembl.
DR GO; GO:0032437; C:cuticular plate; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR GO; GO:0032420; C:stereocilium; IEA:Ensembl.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR GO; GO:0090102; P:cochlea development; IEA:Ensembl.
DR GO; GO:0098976; P:excitatory chemical synaptic transmission; IEA:Ensembl.
DR GO; GO:0010467; P:gene expression; IEA:Ensembl.
DR GO; GO:0098977; P:inhibitory chemical synaptic transmission; IEA:Ensembl.
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:8354278"
FT CHAIN 2..110
FT /note="Parvalbumin alpha"
FT /id="PRO_0000073588"
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 24
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02625"
FT MUTAGEN 52
FT /note="D->A: Inactivation."
FT /evidence="ECO:0000269|PubMed:10036163"
FT MUTAGEN 63
FT /note="E->V: Inactivation."
FT /evidence="ECO:0000269|PubMed:10036163"
FT MUTAGEN 91
FT /note="D->A: Inactivation."
FT /evidence="ECO:0000269|PubMed:10036163"
FT MUTAGEN 102
FT /note="E->V: Inactivation."
FT /evidence="ECO:0000269|PubMed:10036163"
FT CONFLICT 4
FT /note="T -> N (in Ref. 7; AAH96113)"
FT /evidence="ECO:0000305"
FT CONFLICT 99..100
FT /note="Missing (in Ref. 1; CAA45134)"
FT /evidence="ECO:0000305"
FT TURN 3..8
FT /evidence="ECO:0007829|PDB:1RJV"
FT HELIX 9..18
FT /evidence="ECO:0007829|PDB:1RJV"
FT STRAND 21..23
FT /evidence="ECO:0007829|PDB:1RJV"
FT HELIX 27..33
FT /evidence="ECO:0007829|PDB:1RJV"
FT HELIX 36..38
FT /evidence="ECO:0007829|PDB:1RJV"
FT HELIX 41..51
FT /evidence="ECO:0007829|PDB:1RJV"
FT HELIX 61..64
FT /evidence="ECO:0007829|PDB:1RJV"
FT TURN 65..67
FT /evidence="ECO:0007829|PDB:1RK9"
FT HELIX 68..71
FT /evidence="ECO:0007829|PDB:1RJV"
FT HELIX 80..90
FT /evidence="ECO:0007829|PDB:1RJV"
FT STRAND 92..98
FT /evidence="ECO:0007829|PDB:1RJV"
FT HELIX 100..106
FT /evidence="ECO:0007829|PDB:1RJV"
FT TURN 107..109
FT /evidence="ECO:0007829|PDB:1RJV"
SQ SEQUENCE 110 AA; 12059 MW; 03ABDD22E24AEA11 CRC64;
MSMTDLLNAE DIKKAVGAFS ATDSFDHKKF FQMVGLKKKS ADDVKKVFHM LDKDKSGFIE
EDELGFILKG FSPDARDLSA KETKMLMAAG DKDGDGKIGV DEFSTLVAES
