ADAM2

Disintegrin and metalloproteinase domain-containing protein 2 or Beta-fertilin[5] is an enzyme that in humans is encoded by the ADAM2 gene.[6][7][8]

ADAM2
Identifiers
Aliases	ADAM2, CRYN1, CRYN2, CT15, FTNB, PH-30b, PH30, PH30-beta, ADAM metallopeptidase domain 2
External IDs	OMIM: 601533 MGI: 1340894 HomoloGene: 1127 GeneCards: ADAM2
Gene location (Human) Chr. Chromosome 8 (human)[1] Band 8p11.22 Start 39,743,735 bp[1] End 39,838,289 bp[1]
Gene location (Mouse) Chr. Chromosome 14 (mouse)[2] Band 14 D1|14 34.36 cM Start 66,027,329 bp[2] End 66,077,733 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • integrin binding • metalloendopeptidase activity • metallopeptidase activity Cellular component • integral component of membrane • cell surface • cell membrane • integral component of plasma membrane • membrane • macromolecular complex Biological process • visual learning • fusion of sperm to egg plasma membrane involved in single fertilization • cell adhesion • adult behavior • proteolysis • binding of sperm to zona pellucida • single fertilization • positive regulation of gene expression Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	2515	11495
Ensembl	ENSG00000104755 ENSG00000276286	ENSMUSG00000022039
UniProt	Q99965	Q60718
RefSeq (mRNA)	NM_001278113 NM_001278114 NM_001464	NM_009618
RefSeq (protein)	NP_001265042 NP_001265043 NP_001455	NP_033748
Location (UCSC)	Chr 8: 39.74 – 39.84 Mb	Chr 14: 66.03 – 66.08 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Function

This gene encodes a member of the ADAM (a disintegrin and metalloprotease domain) family. Members of this family are membrane-anchored proteins structurally related to snake venom disintegrins, and have been implicated in a variety of biological processes involving cell–cell and cell–matrix interactions, including fertilization, muscle development, and neurogenesis. This member is a subunit of an integral sperm membrane heterodimer glycoprotein called fertilin, which plays an important role in sperm-egg interactions.[8] The other subunit is ADAM1 or alpha-fertilin.[5]

References

1. ENSG00000276286 GRCh38: Ensembl release 89: ENSG00000104755, ENSG00000276286 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000022039 - 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. Fàbrega A, Guyonnet B, Dacheux JL, Gatti JL, Puigmulé M, Bonet S, Pinart E (June 2011). "Expression, immunolocalization and processing of fertilins ADAM-1 and ADAM-2 in the boar (Sus domesticus) spermatozoa during epididymal maturation". Reproductive Biology and Endocrinology. 9: 96. doi:10.1186/1477-7827-9-96. PMC 3141649. PMID 21718510.
6. Gupta SK, Alves K, Palladino LO, Mark GE, Hollis GF (July 1996). "Molecular cloning of the human fertilin beta subunit". Biochemical and Biophysical Research Communications. 224 (2): 318–26. doi:10.1006/bbrc.1996.1027. PMID 8702389.
7. Burkin HR, Burkin DJ, Davey PM, Griffin DK, Affara NA (February 1997). "Mapping, sequence, and expression analysis of the human fertilin beta gene (FTNB)". Genomics. 40 (1): 190–2. doi:10.1006/geno.1996.4531. PMID 9070941.
8. "Entrez Gene: ADAM2 ADAM metallopeptidase domain 2 (fertilin beta)".

Further reading

• Eto K, Huet C, Tarui T, Kupriyanov S, Liu HZ, Puzon-McLaughlin W, Zhang XP, Sheppard D, Engvall E, Takada Y (May 2002). "Functional classification of ADAMs based on a conserved motif for binding to integrin alpha 9beta 1: implications for sperm-egg binding and other cell interactions". The Journal of Biological Chemistry. 277 (20): 17804–10. doi:10.1074/jbc.M200086200. PMID 11882657.
• Ikawa M, Nakanishi T, Yamada S, Wada I, Kominami K, Tanaka H, Nozaki M, Nishimune Y, Okabe M (December 2001). "Calmegin is required for fertilin alpha/beta heterodimerization and sperm fertility". Developmental Biology. 240 (1): 254–61. doi:10.1006/dbio.2001.0462. PMID 11784061.
• Cho C, Ge H, Branciforte D, Primakoff P, Myles DG (June 2000). "Analysis of mouse fertilin in wild-type and fertilin beta(-/-) sperm: evidence for C-terminal modification, alpha/beta dimerization, and lack of essential role of fertilin alpha in sperm-egg fusion". Developmental Biology. 222 (2): 289–95. doi:10.1006/dbio.2000.9703. PMID 10837118.
• Chen MS, Tung KS, Coonrod SA, Takahashi Y, Bigler D, Chang A, Yamashita Y, Kincade PW, Herr JC, White JM (October 1999). "Role of the integrin-associated protein CD9 in binding between sperm ADAM 2 and the egg integrin alpha6beta1: implications for murine fertilization". Proceedings of the National Academy of Sciences of the United States of America. 96 (21): 11830–5. doi:10.1073/pnas.96.21.11830. PMC 18372. PMID 10518536.
• Chen H, Sampson NS (January 1999). "Mediation of sperm-egg fusion: evidence that mouse egg alpha6beta1 integrin is the receptor for sperm fertilinbeta". Chemistry & Biology. 6 (1): 1–10. doi:10.1016/S1074-5521(99)80015-5. PMID 9889149.
• Vidaeus CM, von Kapp-Herr C, Golden WL, Eddy RL, Shows TB, Herr JC (March 1997). "Human fertilin beta: identification, characterization, and chromosomal mapping of an ADAM gene family member". Molecular Reproduction and Development. 46 (3): 363–9. doi:10.1002/(SICI)1098-2795(199703)46:3<363::AID-MRD15>3.0.CO;2-#. PMID 9041139.
• Dawson SJ, White LA (May 1992). "Treatment of Haemophilus aphrophilus endocarditis with ciprofloxacin". The Journal of Infection. 24 (3): 317–20. doi:10.1016/S0163-4453(05)80037-4. PMID 1602151.

External links

• The MEROPS online database for peptidases and their inhibitors: M12.950
• Human ADAM2 genome location and ADAM2 gene details page in the UCSC Genome Browser.