XB-FEAT-29098062: Difference between revisions
Created page with "=''ovos5d''= This is the Xenbase community page for ''Xenopus ovos5d''. Please feel free to record here anything relevant to these genes/proteins that is not found elsewhere on Xenbase. =nomenclature updates= 18DEC2025 ''Xenopus'' Gene Name and symbol was changed from ''LOC116412135, ovostatin-like and ovos2(LOC431886), alpha-2-macroglobulin like 1'', to ''ovos5d, ovostatin 5D'' following phylogenetic analysis of the vertebrate ovostatin and A2M protein/gene family by..." |
|||
| Line 9: | Line 9: | ||
LOC116412135 is recorded as Synonym. | LOC116412135 is recorded as Synonym. | ||
=OVOS protein background= | |||
Ovostatins (OVOS gene /protein family) were originally called “ovomacroglobulins”, and were first identified in the 1960's as an abundant proteins from the 'whites' of chicken eggs [1]. Ovostatins were subsequently shown to be active enzymes that inhibited the peptidases trypsin, papain and thermolysin [2]. | |||
References: | |||
1. Miller et al 1966. Biochemistry. 1966;5:952–8. | |||
2. Nielsen et al 1994. DNA Seq. 1994;5:111–9 | |||
Latest revision as of 17:46, 19 December 2025
ovos5d
This is the Xenbase community page for Xenopus ovos5d. Please feel free to record here anything relevant to these genes/proteins that is not found elsewhere on Xenbase.
nomenclature updates
18DEC2025 Xenopus Gene Name and symbol was changed from LOC116412135, ovostatin-like and ovos2(LOC431886), alpha-2-macroglobulin like 1, to ovos5d, ovostatin 5D following phylogenetic analysis of the vertebrate ovostatin and A2M protein/gene family by Xenbase and the HGNC.
The X. laevis gene was moved from XB-GENE-6251755 to XB-GENE-29098064.
LOC116412135 is recorded as Synonym.
OVOS protein background
Ovostatins (OVOS gene /protein family) were originally called “ovomacroglobulins”, and were first identified in the 1960's as an abundant proteins from the 'whites' of chicken eggs [1]. Ovostatins were subsequently shown to be active enzymes that inhibited the peptidases trypsin, papain and thermolysin [2].
References: 1. Miller et al 1966. Biochemistry. 1966;5:952–8. 2. Nielsen et al 1994. DNA Seq. 1994;5:111–9