ADAM28

ADAM28
Identifiers
Aliases	ADAM28, ADAM 28, ADAM23, MDC-L, MDC-Lm, MDC-Ls, MDCL, eMDC II, eMDCII, ADAM metallopeptidase domain 28
External IDs	OMIM: 606188 MGI: 105988 HomoloGene: 40705 GeneCards: ADAM28
Gene location (Human)
Chr.	Chromosome 8 (human)[1]
End	24,359,014 bp[1]
Gene location (Mouse)
Chr.	Chromosome 14 (mouse)[2]
End	68,655,842 bp[2]
RNA expression pattern
	; ;
	More reference expression data
Gene ontology
Molecular function	• peptidase activity; • metalloendopeptidase activity; • hydrolase activity; • metallopeptidase activity; • metal ion binding;
Cellular component	• integral component of membrane; • extracellular region; • membrane; • mitochondrion; • cell membrane;
Biological process	• spermatogenesis; • proteolysis;
	Sources:Amigo / QuickGO
Orthologs
	10863
	13522
	ENSG00000042980
	ENSMUSG00000014725
	Q9UKQ2
	Q9JLN6
	NM_001304351; NM_014265; NM_021777
	NM_001048175; NM_010082; NM_176991; NM_183366
	NP_001291280; NP_055080; NP_068547
	NP_001041640; NP_034212; NP_899222
	Wikidata
View/Edit Human	View/Edit Mouse

Disintegrin and metalloproteinase domain-containing protein 28 is an enzyme that in humans is encoded by the ADAM28 gene.[5]

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. The protein encoded by this gene is a lymphocyte-expressed ADAM protein. Alternative splicing results in two transcript variants. The shorter version encodes a secreted isoform, while the longer version encodes a transmembrane isoform.[5]

References

GRCh38: Ensembl release 89: ENSG00000042980 - Ensembl, May 2017
GRCm38: Ensembl release 89: ENSMUSG00000014725 - 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.
"Entrez Gene: ADAM28 ADAM metallopeptidase domain 28".

Roberts CM, Tani PH, Bridges LC, et al. (1999). "MDC-L, a novel metalloprotease disintegrin cysteine-rich protein family member expressed by human lymphocytes". J. Biol. Chem. 274 (41): 29251–29259. doi:10.1074/jbc.274.41.29251. PMID 10506182.
Jury JA, Perry AC, Hall L (2000). "Identification, sequence analysis and expression of transcripts encoding a putative metalloproteinase, eMDC II, in human and macaque epididymis". Mol. Hum. Reprod. 5 (12): 1127–1134. doi:10.1093/molehr/5.12.1127. PMID 10587367.
Howard L, Maciewicz RA, Blobel CP (2000). "Cloning and characterization of ADAM28: evidence for autocatalytic pro-domain removal and for cell surface localization of mature ADAM28". Biochem. J. 348 Pt 1 (Pt 1): 21–27. doi:10.1042/0264-6021:3480021. PMC 1221031. PMID 10794709.
Bridges LC, Tani PH, Hanson KR, et al. (2002). "The lymphocyte metalloprotease MDC-L (ADAM 28) is a ligand for the integrin alpha4beta1". J. Biol. Chem. 277 (5): 3784–3792. doi:10.1074/jbc.M109538200. PMID 11724793.
Bridges LC, Hanson KR, Tani PH, et al. (2003). "Integrin alpha4beta1-dependent adhesion to ADAM 28 (MDC-L) requires an extended surface of the disintegrin domain". Biochemistry. 42 (13): 3734–3741. doi:10.1021/bi026871y. PMID 12667064.
Fourie AM, Coles F, Moreno V, Karlsson L (2003). "Catalytic activity of ADAM8, ADAM15, and MDC-L (ADAM28) on synthetic peptide substrates and in ectodomain cleavage of CD23". J. Biol. Chem. 278 (33): 30469–30477. doi:10.1074/jbc.M213157200. PMID 12777399.
Mochizuki S, Shimoda M, Shiomi T, et al. (2004). "ADAM28 is activated by MMP-7 (matrilysin-1) and cleaves insulin-like growth factor binding protein-3". Biochem. Biophys. Res. Commun. 315 (1): 79–84. doi:10.1016/j.bbrc.2004.01.022. PMID 15013428.
Ohtsuka T, Shiomi T, Shimoda M, et al. (2006). "ADAM28 is overexpressed in human non-small cell lung carcinomas and correlates with cell proliferation and lymph node metastasis". Int. J. Cancer. 118 (2): 263–273. doi:10.1002/ijc.21324. PMID 16052521. S2CID 19344958.
Mitsui Y, Mochizuki S, Kodama T, et al. (2006). "ADAM28 is overexpressed in human breast carcinomas: implications for carcinoma cell proliferation through cleavage of insulin-like growth factor binding protein-3". Cancer Res. 66 (20): 9913–9920. doi:10.1158/0008-5472.CAN-06-0377. PMID 17047053.
Shimoda M, Hashimoto G, Mochizuki S, et al. (2007). "Binding of ADAM28 to P-selectin glycoprotein ligand-1 enhances P-selectin-mediated leukocyte adhesion to endothelial cells". J. Biol. Chem. 282 (35): 25864–25874. doi:10.1074/jbc.M702414200. PMID 17597069.

External links

The MEROPS online database for peptidases and their inhibitors: M12.224
Human ADAM28 genome location and ADAM28 gene details page in the UCSC Genome Browser.

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[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000042980 - Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000014725 - 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.

[entrez-5] "Entrez Gene: ADAM28 ADAM metallopeptidase domain 28".

Proteases: metalloendopeptidases (EC 3.4.24)
ADAM proteins	Alpha secretases ADAM9 ADAM10 ADAM17 ADAM19 ADAM2 ADAM7 ADAM8 ADAM11 ADAM12 ADAM15 ADAM18 ADAM22 ADAM23 ADAM28 ADAM33 ADAMTS1 ADAMTS2 ADAMTS3 ADAMTS4 ADAMTS5 ADAMTS8 ADAMTS9 ADAMTS10 ADAMTS12 ADAMTS13
Matrix metalloproteinases	Collagenases MMP1 MMP8 Gelatinases MMP2 MMP9 MMP3 MMP7 MMP10 MMP11 MMP12 MMP13 MMP14 MMP15 MMP16 MMP17 MMP19 MMP20 MMP21 MMP23A MMP23B MMP24 MMP25 MMP26 MMP27 MMP28
Other	Neprilysin Procollagen peptidase Thermolysin Pregnancy-associated plasma protein A Bone morphogenetic protein 1 Lysostaphin Insulin-degrading enzyme ZMPSTE24

Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

ADAM28

References

Further reading

External links