ADAM20

ADAM20
Identifiers
Aliases	ADAM20, ADAM metallopeptidase domain 20
External IDs	OMIM: 603712; MGI: 3045694; HomoloGene: 128364; GeneCards: ADAM20; OMA:ADAM20 - orthologs
Gene location (Human)
Chr.	Chromosome 14 (human)
End	70,535,015 bp
Gene location (Mouse)
Chr.	Chromosome 8 (mouse)
End	41,280,074 bp
RNA expression pattern
	Top expressed in
	sperm; ; gonad; ; testicle; ; right testis; ; left testis; ; buccal mucosa cell; ; Achilles tendon; ; corpus callosum; ; muscle of thigh; ; cervix;
	Top expressed in
	spermatid; ; testicle; ; spermatocyte; ; pancreas; ; islet of Langerhans; ; primary visual cortex;
	More reference expression data
	n/a
Gene ontology
Molecular function	peptidase activity; metalloendopeptidase activity; hydrolase activity; metallopeptidase activity; metal ion binding;
Cellular component	integral component of membrane; plasma membrane; membrane;
Biological process	proteolysis; single fertilization; binding of sperm to zona pellucida;
	Sources:Amigo / QuickGO
Orthologs
	8748
	546055
	ENSG00000134007
	ENSMUSG00000054033
	O43506
	Q7M762
	NM_003814
	NM_001025380
	NP_003805
	NP_001020551
	Wikidata
View/Edit Human	View/Edit Mouse

Disintegrin and metalloproteinase domain-containing protein 20 is an enzyme that in humans is encoded by the ADAM20 gene. It is a membrane disintegrin-metalloprotease that belongs to the ADAM family. It is exclusively expressed in Testes and is similar to sperm cell-specific fertilins -alpha and -beta.

Its cDNA is tightly linked to marker SHGC-36001 on chromosome 14q24.1. ADAM20 is related to fertilin α (ADAM1A/B pseudogene), fertilin β (ADAM2), and fertilin γ (ADAM9). In humans, fertilin α has recently been deactivated so ADAM20 may be the functional equivalent fertilin α in humans.^[5]

Structure

Computed structure of the ADAM 20 protein.^[6] The signal and propeptide sites have been removed as they would be cleaved in the active form. Extracellular domains are highlighted in red, helical domains are highlighted in yellow, and cytoplasmic domains are highlighted in blue.

In common with other ADAM family members, ADAM20 contains a N-terminal reprolysin family propeptide (residues 57–159), reprolysin (M12B) family zinc metalloprotease domain (207–395), disintegrin domain (416–488), and a C-terminal ADAM cysteine-rich domain (493–605).^[7]

The propeptide acts both a signal peptide and an activator domain. This prodomain has a cysteine that interacts with a zinc in the catalytic domain, thereby preventing the catalytic activity of the protein.When the pro-protein domain is cleaved, this cysteine zinc bond is broken and the protein is activated.^[8] A notable variant showed an amino acid difference in the pro protein domain that prevented the cleavage of this domain which prevented the fusion of the sperm cell to an egg.^[9]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000134007 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000054033 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Hooft van Huijsduijnen R (January 1998). "ADAM 20 and 21; two novel human testis-specific membrane metalloproteases with similarity to fertilin-alpha". Gene. 206 (2): 273–82. doi:10.1016/s0378-1119(97)00597-0. PMID 9469942.
^ "Computed structure model of Disintegrin and metalloproteinase domain-containing protein 20". Research Collaboratory for Structural Bioinformatics (RCSB) Protein Data Bank.
^ "Disintegrin and metalloproteinase domain-containing protein 20". Pfam – via InterPro.
^ Van Wart HE, Birkedal-Hansen H (July 1990). "The cysteine switch: a principle of regulation of metalloproteinase activity with potential applicability to the entire matrix metalloproteinase gene family". Proceedings of the National Academy of Sciences of the United States of America. 87 (14): 5578–82. Bibcode:1990PNAS...87.5578V. doi:10.1073/pnas.87.14.5578. PMC 54368. PMID 2164689.
^ Sha YW, Xu X, Ji ZY, Mei LB, Qiu PP, Ji H, Li P, Li L, Liu WW (January 2018). "Sperm-egg fusion disorder in a Chinese male patient was associated with a rare ADAM20 variant". Oncotarget. 9 (2): 2086–2091. doi:10.18632/oncotarget.23331. PMC 5788623. PMID 29416755.

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[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000134007 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000054033 – Ensembl, May 2017

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

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

[5] Hooft van Huijsduijnen R (January 1998). "ADAM 20 and 21; two novel human testis-specific membrane metalloproteases with similarity to fertilin-alpha". Gene. 206 (2): 273–82. doi:10.1016/s0378-1119(97)00597-0. PMID 9469942.

[6] "Computed structure model of Disintegrin and metalloproteinase domain-containing protein 20". Research Collaboratory for Structural Bioinformatics (RCSB) Protein Data Bank.

[7] "Disintegrin and metalloproteinase domain-containing protein 20". Pfam – via InterPro.

[Van_Wart_1990-8] Van Wart HE, Birkedal-Hansen H (July 1990). "The cysteine switch: a principle of regulation of metalloproteinase activity with potential applicability to the entire matrix metalloproteinase gene family". Proceedings of the National Academy of Sciences of the United States of America. 87 (14): 5578–82. Bibcode:1990PNAS...87.5578V. doi:10.1073/pnas.87.14.5578. PMC 54368. PMID 2164689.

[Sha_2018-9] Sha YW, Xu X, Ji ZY, Mei LB, Qiu PP, Ji H, Li P, Li L, Liu WW (January 2018). "Sperm-egg fusion disorder in a Chinese male patient was associated with a rare ADAM20 variant". Oncotarget. 9 (2): 2086–2091. doi:10.18632/oncotarget.23331. PMC 5788623. PMID 29416755.

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