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; OMA:ADAM28 - orthologs
Gene location (Human) Chr. Chromosome 8 (human) [1] Band 8p21.2 Start 24,294,069 bp [1] End 24,359,014 bp [1]
Gene location (Mouse) Chr. Chromosome 14 (mouse) [2] Band 14|14 D1 Start 68,843,476 bp [2] End 68,893,291 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in corpus epididymis nasal epithelium olfactory zone of nasal mucosa gallbladder pancreatic ductal cell right uterine tube epithelium of nasopharynx mucosa of paranasal sinus bronchial epithelial cell appendix Top expressed in superior surface of tongue gallbladder Ileal epithelium nasal epithelium olfactory epithelium transitional epithelium of urinary bladder corneal stroma plantaris muscle extensor digitorum longus muscle interventricular septum More reference expression data BioGPS 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 plasma membrane Biological process spermatogenesis proteolysis Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 10863 13522 Ensembl ENSG00000042980 ENSMUSG00000014725 UniProt Q9UKQ2 Q9JLN6 RefSeq (mRNA) NM_001304351 NM_014265 NM_021777 NM_001048175 NM_010082 NM_176991 NM_183366 RefSeq (protein) NP_001291280 NP_055080 NP_068547 NP_001041640 NP_034212 NP_899222 Location (UCSC) Chr 8: 24.29 – 24.36 Mb Chr 14: 68.84 – 68.89 Mb PubMed search [3] [4]
Wikidata
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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

1. GRCh38: Ensembl release 89: ENSG00000042980 – Ensembl, May 2017
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.
5. "Entrez Gene: ADAM28 ADAM metallopeptidase domain 28".

Further reading

• 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 .