PVALB
Available structures PDB Ortholog search:PDBeRCSB List of PDB id codes 1RJV,1RK9,%%s1RK9,1RJV
Identifiers
Aliases	PVALB, D22S749, parvalbumin
External IDs	OMIM:168890;MGI:97821;HomoloGene:2137;GeneCards:PVALB;OMA:PVALB - orthologs
Gene location (Human) Chr. Chromosome 22 (human)[1] Band 22q12.3 Start 36,800,684bp[1] End 36,819,479bp[1]
Gene location (Mouse) Chr. Chromosome 15 (mouse)[2] Band 15 E1|15 36.93 cM Start 78,075,314bp[2] End 78,090,600bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in right hemisphere of cerebellum primary visual cortex superior frontal gyrus dorsolateral prefrontal cortex right frontal lobe muscle of thigh human kidney substantia nigra Brodmann area 9 C1 segment Top expressed in triceps brachii muscle temporal muscle sternocleidomastoid muscle digastric muscle muscle of thigh medial head of gastrocnemius muscle vastus lateralis muscle tibialis anterior muscle ankle joint ankle More reference expression data BioGPS n/a
Gene ontology Molecular function calcium ion binding protein homodimerization activity metal ion binding protein heterodimerization activity Cellular component cytoplasm axon soma nucleus protein-containing complex stereocilium cuticular plate Biological process regulation of cytosolic calcium ion concentration cochlea development Sources:Amigo /QuickGO
Orthologs Species Human Mouse Entrez 5816 19293 Ensembl ENSG00000274665 ENSG00000100362 ENSMUSG00000005716 UniProt P20472 P32848 RefSeq (mRNA) NM_002854 NM_001315532 NM_013645 NM_001330686 RefSeq (protein) NP_001302461 NP_002845 NP_001302461.1 NP_002845.1 NP_001317615 NP_038673 Location (UCSC) Chr 22: 36.8 – 36.82 Mb Chr 15: 78.08 – 78.09 Mb PubMed search [3] [4]
Wikidata
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Parvalbumin (PV) is acalcium-binding protein with low molecular weight (typically 9–11kDa). In humans, it is encoded by thePVALB gene. It is a member of thealbumin family; it is named for its size (parv-, from Latinparvus which means "small") and its ability to coagulate.

It has threeEF hand motifs and is structurally related tocalmodulin andtroponin C. Parvalbumin is found in fast-contracting muscles, where its levels are highest, as well as in the brain and some endocrine tissues.

Parvalbumin is a small, stable protein containing EF-hand type calcium binding sites. It is involved incalcium signaling. Typically, this protein is broken into three domains, domains AB, CD and EF, each individually containing a helix-loop-helix motif.^[5] The AB domain houses a two amino-acid deletion in the loop region, whereas domains CD and EF contain the N-terminal and C-terminal, respectively.^[5]

Parvalbumin is present in someGABAergicinterneurons in the nervous system, especially the reticular thalamus,^[6] and expressed predominantly bychandelier andbasket cells in the cortex. In thecerebellum, PV is expressed inPurkinje cells and molecular layer interneurons.^[7] In thehippocampus, PV+ interneurons are subdivided into basket, axo-axonic, and bistratified cells, each subtype targeting distinct compartments ofpyramidal cells.^[8]

PV interneurons' connections are mostly perisomatic (around the cell body of neurons). Most of the PV interneurons are fast-spiking. They are also thought to give rise togamma waves recorded inEEG.

PV-expressing interneurons represent approximately 25% of GABAergic cells in theprimateDLPFC.^[9][10] Other calcium-binding protein markers arecalretinin (most abundant subtype in DLPFC, about 50%) andcalbindin. Interneurons are also divided into subgroups by the expression ofneuropeptides such assomatostatin,neuropeptide Y,cholecystokinin.

PV is known to be involved in relaxation offast-twitch muscle fibers.^[11][12] This function is associated with the PV role in calcium sequestration.

Calcium binding proteins like parvalbumin play a role in many physiological processes, namely cell-cycle regulation,second messenger production,muscle contraction, organization ofmicrotubules andphototransduction.^[13] Therefore, calcium-binding proteins must distinguish calcium in the presence of high concentrations of other metal ions. The mechanism for the calcium selectivity has been extensively studied.^[13][14]

Duringmuscle contraction, theaction potential stimulates voltage-sensitive proteins in theT-tubule membrane. These proteins stimulate the opening ofCa²⁺ channels in thesarcoplasmic reticulum, leading to release of Ca²⁺ in the sarcoplasm. The Ca²⁺ ions bind totroponin, which causes the displacement oftropomyosin, a protein that preventsmyosin walking alongactin. The displacement of tropomyosin exposes the myosin-binding sites on actin, permitting muscle contraction.^[15] This way, while muscle contraction is driven by Ca²⁺ release, muscle relaxation is driven by Ca²⁺ removal from sarcoplasm. Along with Ca²⁺ pumps, PV contributes to Ca²⁺ removal from cytoplasm: PV binds to Ca²⁺ ions in the sarcoplasm, and then shuttles it to the sarcoplasmic reticulum.^[16]

Decreased PV andGAD67 expression was found in PV+ GABAergic interneurons inschizophrenia.^[17][18]

Parvalbumin has been identified as the majorallergen causingfish meat allergy (but notshellfish allergy).^{[19][20][21][22]} Mostbony fishes manifest β-parvalbumins as major allergens andcartilaginous fishes such as sharks and rays manifest α-parvalbumins as major allergens; allergenicity to bony fishes has a lowcross-reactivity to cartilaginous fishes^[20] and also chicken meat.^[23]

Parvalbumins and their genes have only been found in jawed vertebrate species so far. From the evolutionary level of sharks, already three major lineages of parvalbumins can be distinguished:^[24] (1) α-parvalbumins, which include the above discussed human "parvalbumin"; (2) oncomodulins (sometimes called "β-1 parvalbumins"), which are also found in human and mouse; and (3) β-2 parvalbumins, which are the major allergens in most bony fish and were lost in human and mouse but conserved in some primitive mammals.

All parvalbumins share a highly conserved structure (see the figure),^[24] which explains their high level of sequence conservation, resulting in the above-mentioned cross-reactivity in allergenic reactions against different bony fish species and even species from other animal clades such as chicken.^[25]

Bony fishes have, depending on the species, combined for all three parvalbumin lineages between 7 and 22 genes.^[26][24] Although in most bony fishes the β-2 parvalbumins are the major allergens, in some bony fishes the α-parvalbumins are the highest expressed in muscle and were identified as the allergens.^[25] The allergen nomenclature is partly based on the order of allergen detection per species, and therefore identical allergen numbers in different fish species do not always refer to the same gene (see the table).^[25]

The protein was discovered in 1965 as a component of the fast-twitching white muscle of fish. It was described as a low molecular-weight "albumin".^[27] It is unknown who coined the termparvalbumin, but the word is already in use by 1967.^[28]

• Parvalbumins at the U.S. National Library of MedicineMedical Subject Headings (MeSH)
• Baig I, Bertini I, Del Bianco C, Gupta YK, Lee YM, Luchinat C, et al. (May 2004). "Paramagnetism-based refinement strategy for the solution structure of human alpha-parvalbumin".Biochemistry.43 (18):5562–5573.doi:10.1021/bi035879k.PMID 15122922.

• Genes on human chromosome 22
• Molecular neuroscience
• EF-hand-containing proteins

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