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ADAM28

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

ADAM28

Identifiers

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]
Band	8p21.2	End	24,359,014 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 14 (mouse)^[2]

Band	14\|14 D1	Start	68,843,476 bp^[2]
Band	14\|14 D1	End	68,893,291 bp^[2]

RNA expression pattern

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


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

Species

Human

Mouse


10863


13522


ENSG00000042980


ENSMUSG00000014725


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]

View/Edit Human

View/Edit Mouse

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

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000042980 – Ensembl, May 2017

^ ^a ^b ^c 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.

^ ^a ^b "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.

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Retrieved from "https://en.wikipedia.org/w/index.php?title=ADAM28&oldid=1166576816" Last edited on 22 July 2023, at 13:22

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