ADAM33

Last updated
ADAM33
Protein ADAM33 PDB 1r54.png
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases ADAM33 , C20orf153, DJ964F7.1, ADAM metallopeptidase domain 33
External IDs OMIM: 607114 MGI: 1341813 HomoloGene: 11881 GeneCards: ADAM33
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001282447
NM_025220
NM_153202

NM_001163529
NM_033615

RefSeq (protein)

NP_001269376
NP_079496
NP_694882

NP_001157001
NP_291093

Location (UCSC) Chr 20: 3.67 – 3.68 Mb Chr 2: 130.89 – 130.91 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Disintegrin and metalloproteinase domain-containing protein 33 is an enzyme that in humans is encoded by the ADAM33 gene. [5] [6]

Contents

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 protein is a type I transmembrane protein implicated in asthma and bronchial hyperresponsiveness. [7] Alternative splicing of this gene results in two transcript variants encoding different isoforms. [6]

Related Research Articles

<span class="mw-page-title-main">ADAM (protein)</span>

ADAMs are a family of single-pass transmembrane and secreted metalloendopeptidases. All ADAMs are characterized by a particular domain organization featuring a pro-domain, a metalloprotease, a disintegrin, a cysteine-rich, an epidermal-growth factor like and a transmembrane domain, as well as a C-terminal cytoplasmic tail. Nonetheless, not all human ADAMs have a functional protease domain, which indicates that their biological function mainly depends on protein–protein interactions. Those ADAMs which are active proteases are classified as sheddases because they cut off or shed extracellular portions of transmembrane proteins. For example, ADAM10 can cut off part of the HER2 receptor, thereby activating it. ADAM genes are found in animals, choanoflagellates, fungi and some groups of green algae. Most green algae and all land plants likely lost ADAM proteins.

<span class="mw-page-title-main">ADAMTS4</span> Protein-coding gene in the species Homo sapiens

A disintegrin and metalloproteinase with thrombospondin motifs 4 is an enzyme that in humans is encoded by the ADAMTS4 gene.

<span class="mw-page-title-main">ADAM12</span> Human protein-coding gene

Disintegrin and metalloproteinase domain-containing protein 12 is an enzyme that in humans is encoded by the ADAM12 gene. ADAM12 has two splice variants: ADAM12-L, the long form, has a transmembrane region and ADAM12-S, a shorter variant, is soluble and lacks the transmembrane and cytoplasmic domains.

<span class="mw-page-title-main">ADAM15</span> Protein-coding gene in the species Homo sapiens

Disintegrin and metalloproteinase domain-containing protein 15 is an enzyme that in humans is encoded by the ADAM15 gene.

<span class="mw-page-title-main">ADAM10</span> Protein-coding gene in the species Homo sapiens

A Disintegrin and metalloproteinase domain-containing protein 10, also known as ADAM10 or CDw156 or CD156c is a protein that in humans is encoded by the ADAM10 gene.

<span class="mw-page-title-main">ADAM9</span> Protein-coding gene in the species Homo sapiens

Disintegrin and metalloproteinase domain-containing protein 9 is an enzyme that in humans is encoded by the ADAM9 gene.

<span class="mw-page-title-main">ADAM19</span> Protein-coding gene in the species Homo sapiens

ADAM19 , is a human gene.

<span class="mw-page-title-main">MAD2L2</span> Protein-coding gene in the species Homo sapiens

Mitotic spindle assembly checkpoint protein MAD2B is a protein that in humans is encoded by the MAD2L2 gene.

<span class="mw-page-title-main">ADAM22</span> Enzyme found in humans

Disintegrin and metalloproteinase domain-containing protein 22, also known as ADAM22, is an enzyme that in humans is encoded by the ADAM22 gene.

<span class="mw-page-title-main">ADAMTS8</span> Protein-coding gene in the species Homo sapiens

A disintegrin and metalloproteinase with thrombospondin motifs 8 is an enzyme that in humans is encoded by the ADAMTS8 gene.

<span class="mw-page-title-main">ADAM23</span> Protein-coding gene in the species Homo sapiens

Disintegrin and metalloproteinase domain-containing protein 23 is a non-catalytic protein that in humans is encoded by the ADAM23 gene. It is a member of the ADAM family of extracellular matrix metalloproteinases.

<span class="mw-page-title-main">ADAM8</span> Protein-coding gene in the species Homo sapiens

A Disintegrin and metalloproteinase domain-containing protein 8 is an enzyme that in humans is encoded by the ADAM8 gene.

<span class="mw-page-title-main">ADAM28</span> Protein-coding gene in the species Homo sapiens

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

<span class="mw-page-title-main">ADAM11</span> Protein-coding gene in the species Homo sapiens

Disintegrin and metalloproteinase domain-containing protein 11 is an enzyme that in humans is encoded by the ADAM11 gene.

<span class="mw-page-title-main">ADAMTS3</span> Protein-coding gene in the species Homo sapiens

A disintegrin and metalloproteinase with thrombospondin motifs 3 is an enzyme that in humans is encoded by the ADAMTS3 gene. The protein encoded by this gene is the major procollagen II N-propeptidase.

<span class="mw-page-title-main">ADAM18</span> Protein-coding gene in the species Homo sapiens

Disintegrin and metalloproteinase domain-containing protein 18 is an enzyme that in humans is encoded by the ADAM18 gene.

<span class="mw-page-title-main">ADAM20</span> Protein-coding gene in the species Homo sapiens

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.

Sir Stephen Townley Holgate, is a British physician who specializes in immunopharmacology, respiratory medicine and allergies, and asthma and air pollution, based at the University of Southampton and University Hospital Southampton NHS Foundation Trust, UK.

Donna Elizabeth Davies is a British biochemist and professor of respiratory cell and molecular biology at the University of Southampton. In 2003, Davies was the co-founder of Synairgen, an interferon-beta drug designed to treat patients with asthma and chronic obstructive pulmonary disease.

John William Holloway is a geneticist based at the University of Southampton, where he is professor of allergy and respiratory genetics, and was appointed associate vice-president interdisciplinary research in 2021. He leads a research team based within the human genetics and medical genomics theme of the School of Human Development & Health, Faculty of Medicine. Holloway is a Fellow of the Higher Education Academy.

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000149451 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000027318 - 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. Yoshinaka T, Nishii K, Yamada K, Sawada H, Nishiwaki E, Smith K, Yoshino K, Ishiguro H, Higashiyama S (January 2002). "Identification and characterization of novel mouse and human ADAM33s with potential metalloprotease activity". Gene. 282 (1–2): 227–36. doi:10.1016/S0378-1119(01)00818-6. PMID   11814695.
  6. 1 2 "Entrez Gene: ADAM33 ADAM metallopeptidase domain 33".
  7. Davies ER, Kelly JF, Howarth PH, Wilson DI, Holgate ST, Davies DE, Whitsett JA, Haitchi HM (2016-07-21). "Soluble ADAM33 initiates airway remodeling to promote susceptibility for allergic asthma in early life". JCI Insight. 1 (11). doi:10.1172/jci.insight.87632. ISSN   0021-9738. PMC   4968941 . PMID   27489884.

Further reading