XB-FEAT-29085838: Difference between revisions
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Following a review by Xenbase and the NCBIref seq team, the ''Xenopus'' gene name has changed from ''LOC101732075, disintegrin and metalloproteinase domain-containing protein 12' to ''adam33, ADAM metallopeptidase domain 33'' | Following a review by Xenbase and the NCBIref seq team, the ''Xenopus'' gene name has changed from ''LOC101732075, disintegrin and metalloproteinase domain-containing protein 12'' to ''adam33, ADAM metallopeptidase domain 33'' | ||
By synteny, the true Xtropicalis ortholog of human ADAM33 is ''Xenopus'' GeneID: 101732075 (XB-GENE-29085839) along with ''X. laevis.L'' GeneID: 108697349 & ''X. laevis.S'' & GeneID: 108704093. | By synteny, the true Xtropicalis ortholog of human ADAM33 is ''Xenopus'' GeneID: 101732075 (XB-GENE-29085839) along with ''X. laevis.L'' GeneID: 108697349 & ''X. laevis.S'' & GeneID: 108704093. | ||
=background to resolution of adam13 v adam33 names in ''Xenopus''= | |||
July2023: Xenbase (cuz_) submitted request for review to NCBO RefSeq team, as follows: | |||
In summary this is what we know/hypothesize: | |||
*The protein ADAM13 (Alfandari et al., 1997 [1] is related to human ADAM33 but the sequences have diverged sufficiently that the two proteins cannot functionally replace each other. | |||
*Alfandari et al considers ADAM13 and ADAM33 as different proteins with different the functionality due to a recombination of the cytoplasmic domain in placental mammals, and notes that ADAM13 architecture is conserved from worm to marsupial. | |||
*We can see this in architecture of the ADAM33 proteins as shown on NCBI (see screen shots) | |||
*see: https://www.ncbi.nlm.nih.gov/gene/80332/ortholog/?scope=1338369&term=ADAM33 | |||
'''Background on ADAM13:''' | |||
Much of the of the primary researcher on this gene is a from Xenopus researchers Dom Alfandari, Helene Cousins and colleagues, who published extensively on Xenopus adam13 in the early 2000s. | |||
Functionally, adam13 is a cell surface metalloprotease that binds to its substrate via its cystein rich domain ([Gaultier et al., 2002][2]; [Smith et al., 2002][3]). adam3 binds and cleave fibronectin (Alfandari et al., 2001[4]), Cadherin-11 (McCusker et al., 2009[5]), PAPC (Cousin et al., 2011[6]) and ephrinB (Wei et al., 2011[7]). | |||
adam13 also cleaves itself within its cystein rich domain (Gaultier et al., 2002[2]). This cleavage can be followed by a cleavage by gama-secretase that release the cytoplasmic domain. The ADAM13 cytoplasmic domain translocates into the nucleus where it regulates gene expression to promote cranial neural crest cell migration (Cousin et al., 2011[6]). | |||
The cytoplasmic domain of adam13 interacts with multiple SH# containing proteins including PACSIN-2 which negatively regulates its proteolytic activity (Cousin et al., 2000 [8]). | |||
References: | |||
1. PMID: 9070330 DOI: 10.1006/dbio.1996.8458 | |||
2. PMID: 11967265 DOI: 10.1074/jbc.M201792200 | |||
3. PMID: 12460986 PMCID: PMC2173380 DOI: 10.1083/jcb.200206023 | |||
4. PMID: 11448768 DOI: 10.1016/s0960-9822(01)00263-9 | |||
5. PMID: 18946084 PMCID: PMC2613130 DOI: 10.1091/mbc.e08-05-0535 | |||
6. PMID: 21316592 PMCID: PMC3074609 DOI: 10.1016/j.devcel.2010.12.009 | |||
7. PMID: 20708595 PMCID: PMC2951023 DOI: 10.1016/j.devcel.2010.07.012 | |||
8. PMID: 11076687 DOI: 10.1006/dbio.2000.9871 | |||
'''David Webb of NCBI refSeq Team wrote:''' | |||
Aug/25/23 06:20 PM | |||
''Hi XenBase Team | |||
I agree that GeneID: 677728 (XB-GENE-988107) should be named ADAM13 rather than ADAM33 along with X. laevis L & S Gene ID: 386623 & Gene ID: 373720. | |||
By synteny, the true Xtr ortholog of human ADAM33 is GeneID: 101732075 (XB-GENE-29085839) along with X. laevis L & S GeneID: 108697349 & GeneID: 108704093. The nomenclature error occurred because NCBI had a setting that prohibited the ADAM33 symbol from being applied to GeneID: 101732075. | |||
It appears that ADAM13 was lost in amniotes. The ADAM13 gene region in lower gnathostomes is quite variable so it's difficult to determine synteny outside of amphibia but I suspect the gene is present in most teleosts and sarcopterygian fish.'' | |||
=summary for HUMAN ADAM33 from NCBI= | =summary for HUMAN ADAM33 from NCBI= |
Latest revision as of 12:55, 2 October 2023
adam33
This is the community wiki page for the gene adam33 please feel free to add any information that is relevant to this gene that is not already captured elsewhere in Xenbase.
nomenclature changes
13SEPT2023
Following a review by Xenbase and the NCBIref seq team, the Xenopus gene name has changed from LOC101732075, disintegrin and metalloproteinase domain-containing protein 12 to adam33, ADAM metallopeptidase domain 33
By synteny, the true Xtropicalis ortholog of human ADAM33 is Xenopus GeneID: 101732075 (XB-GENE-29085839) along with X. laevis.L GeneID: 108697349 & X. laevis.S & GeneID: 108704093.
background to resolution of adam13 v adam33 names in Xenopus
July2023: Xenbase (cuz_) submitted request for review to NCBO RefSeq team, as follows:
In summary this is what we know/hypothesize:
- The protein ADAM13 (Alfandari et al., 1997 [1] is related to human ADAM33 but the sequences have diverged sufficiently that the two proteins cannot functionally replace each other.
- Alfandari et al considers ADAM13 and ADAM33 as different proteins with different the functionality due to a recombination of the cytoplasmic domain in placental mammals, and notes that ADAM13 architecture is conserved from worm to marsupial.
- We can see this in architecture of the ADAM33 proteins as shown on NCBI (see screen shots)
Background on ADAM13:
Much of the of the primary researcher on this gene is a from Xenopus researchers Dom Alfandari, Helene Cousins and colleagues, who published extensively on Xenopus adam13 in the early 2000s.
Functionally, adam13 is a cell surface metalloprotease that binds to its substrate via its cystein rich domain ([Gaultier et al., 2002][2]; [Smith et al., 2002][3]). adam3 binds and cleave fibronectin (Alfandari et al., 2001[4]), Cadherin-11 (McCusker et al., 2009[5]), PAPC (Cousin et al., 2011[6]) and ephrinB (Wei et al., 2011[7]).
adam13 also cleaves itself within its cystein rich domain (Gaultier et al., 2002[2]). This cleavage can be followed by a cleavage by gama-secretase that release the cytoplasmic domain. The ADAM13 cytoplasmic domain translocates into the nucleus where it regulates gene expression to promote cranial neural crest cell migration (Cousin et al., 2011[6]).
The cytoplasmic domain of adam13 interacts with multiple SH# containing proteins including PACSIN-2 which negatively regulates its proteolytic activity (Cousin et al., 2000 [8]).
References:
1. PMID: 9070330 DOI: 10.1006/dbio.1996.8458
2. PMID: 11967265 DOI: 10.1074/jbc.M201792200
3. PMID: 12460986 PMCID: PMC2173380 DOI: 10.1083/jcb.200206023
4. PMID: 11448768 DOI: 10.1016/s0960-9822(01)00263-9
5. PMID: 18946084 PMCID: PMC2613130 DOI: 10.1091/mbc.e08-05-0535
6. PMID: 21316592 PMCID: PMC3074609 DOI: 10.1016/j.devcel.2010.12.009
7. PMID: 20708595 PMCID: PMC2951023 DOI: 10.1016/j.devcel.2010.07.012
8. PMID: 11076687 DOI: 10.1006/dbio.2000.9871
David Webb of NCBI refSeq Team wrote:
Aug/25/23 06:20 PM
Hi XenBase Team
I agree that GeneID: 677728 (XB-GENE-988107) should be named ADAM13 rather than ADAM33 along with X. laevis L & S Gene ID: 386623 & Gene ID: 373720.
By synteny, the true Xtr ortholog of human ADAM33 is GeneID: 101732075 (XB-GENE-29085839) along with X. laevis L & S GeneID: 108697349 & GeneID: 108704093. The nomenclature error occurred because NCBI had a setting that prohibited the ADAM33 symbol from being applied to GeneID: 101732075.
It appears that ADAM13 was lost in amniotes. The ADAM13 gene region in lower gnathostomes is quite variable so it's difficult to determine synteny outside of amphibia but I suspect the gene is present in most teleosts and sarcopterygian fish.
summary for HUMAN ADAM33 from NCBI
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. Alternative splicing results in multiple transcript variants encoding different isoforms. [provided by RefSeq, Sep 2013]
synteny
Xtr.adam33 chr1: lyrm2 hspa12b c20orf27 spef1 GeneID:101732075/LOC101732075 cdc25b znf638 loc100488564 cyp26b1 exoc6b
Xla.adam33.L chr1L: LOC121401575 LOC108697270 znf638.L LOC108697345 cdc25b.L GeneID:108697349/LOC108697349 spef1.L LOC108719387 hspa12b.L lyrm2.L LOC108719395
Xla.adam33.S chr1S: vax2.S exoc6b.S cyp26b1.S znf638.S cdc25b.S GeneID:108704093/LOC108704093 spef1.S c20orf27.S lyrm2.S LOC121399259 XB22166511.S