Filaggrin

FLG
Available structures
PDB	Human UniProt search: PDBe RCSB
List of PDB id codes
	4PCW
Identifiers
Aliases	FLG, ATOD2, filaggrin
External IDs	OMIM: 135940; HomoloGene: 136751; GeneCards: FLG; OMA:FLG - orthologs
Gene location (Human)
Chr.	Chromosome 1 (human)
End	152,325,239 bp
RNA expression pattern
	Top expressed in
	skin of thigh; ; skin of arm; ; skin of hip; ; human penis; ; vulva; ; nipple; ; skin of abdomen; ; epithelium of esophagus; ; oral cavity; ; amniotic fluid;
	n/a
	More reference expression data
	n/a
Gene ontology
Molecular function	calcium ion binding; protein binding; structural molecule activity; metal ion binding; transition metal ion binding; structural constituent of skin epidermis;
Cellular component	intermediate filament; keratohyalin granule; intracellular membrane-bounded organelle; nucleus; cytosol; cornified envelope; collagen-containing extracellular matrix;
Biological process	multicellular organism development; keratinocyte differentiation; establishment of skin barrier; cornification; peptide cross-linking;
	Sources:Amigo / QuickGO
Orthologs
	2312
	n/a
	ENSG00000143631
	n/a
	P20930
	n/a
	NM_002016
	n/a
	NP_002007
	n/a
	Wikidata
View/Edit Human

Filaggrin (filament aggregating protein) is a filament-associated protein that binds to keratin fibers in epithelial cells. Ten to twelve filaggrin units are post-translationally hydrolyzed from a large profilaggrin precursor protein during terminal differentiation of epidermal cells.^[3] In humans, profilaggrin is encoded by the FLG gene, which is part of the S100 fused-type protein (SFTP) family within the epidermal differentiation complex on chromosome 1q21.^[4] In cetaceans and sirenians, the FLG family has lost its function, with the curious exception of manatees in the latter clade: manatees still retain some functional FLG genes.^[5]

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000143631 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Markova NG, Marekov LN, Chipev CC, Gan SQ, Idler WW, Steinert PM (January 1993). "Profilaggrin is a major epidermal calcium-binding protein". Molecular and Cellular Biology. 13 (1): 613–25. doi:10.1128/MCB.13.1.613. PMC 358940. PMID 8417356.
^ Kypriotou M, Huber M, Hohl D (September 2012). "The human epidermal differentiation complex: cornified envelope precursors, S100 proteins and the 'fused genes' family". Experimental Dermatology. 21 (9): 643–9. doi:10.1111/j.1600-0625.2012.01472.x. PMID 22507538. S2CID 5435031.
^ Steinbinder, Julia; Sachslehner, Attila Placido; Holthaus, Karin Brigit; Eckhart, Leopold (2024-04-23). "Comparative genomics of sirenians reveals evolution of filaggrin and caspase-14 upon adaptation of the epidermis to aquatic life". Scientific Reports. 14 (1): 9278. doi:10.1038/s41598-024-60099-2. ISSN 2045-2322. PMC 11039687. PMID 38653760.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000143631 – Ensembl, May 2017

[2] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[3] Markova NG, Marekov LN, Chipev CC, Gan SQ, Idler WW, Steinert PM (January 1993). "Profilaggrin is a major epidermal calcium-binding protein". Molecular and Cellular Biology. 13 (1): 613–25. doi:10.1128/MCB.13.1.613. PMC 358940. PMID 8417356.

[4] Kypriotou M, Huber M, Hohl D (September 2012). "The human epidermal differentiation complex: cornified envelope precursors, S100 proteins and the 'fused genes' family". Experimental Dermatology. 21 (9): 643–9. doi:10.1111/j.1600-0625.2012.01472.x. PMID 22507538. S2CID 5435031.

[5] Steinbinder, Julia; Sachslehner, Attila Placido; Holthaus, Karin Brigit; Eckhart, Leopold (2024-04-23). "Comparative genomics of sirenians reveals evolution of filaggrin and caspase-14 upon adaptation of the epidermis to aquatic life". Scientific Reports. 14 (1): 9278. doi:10.1038/s41598-024-60099-2. ISSN 2045-2322. PMC 11039687. PMID 38653760.

[1]

[2]

[3]

[4]

[5]