XB-FEAT-29079474: Difference between revisions
Created page with "=''ovos5c''= This is the Xenbase community page for ''Xenopus ovos5c''. Please feel free to record here anything relevant to these genes/proteins that is not found elsewhere on Xenbase. =nomenclature updates= 18DEC2025 ''Xenopus'' Gene Symbol nad gene names were changed from ''LOC100488897 ovostatin, , LOC108695708, alpha-2-macroglobulin, and LOC100036845, ovostatin-like precursor'' to ''ovos5c/5c.L/5c.S, ovostatin 5C/L/S homeolog'' following phylogenetic analysis o..." |
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LOC100488897, LOC108695708, LOC100036845 are recorded as Synonyms. | LOC100488897, LOC108695708, LOC100036845 are recorded as Synonyms. | ||
=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
ovos5c
This is the Xenbase community page for Xenopus ovos5c. Please feel free to record here anything relevant to these genes/proteins that is not found elsewhere on Xenbase.
nomenclature updates
18DEC2025 Xenopus Gene Symbol nad gene names were changed from LOC100488897 ovostatin, , LOC108695708, alpha-2-macroglobulin, and LOC100036845, ovostatin-like precursor to ovos5c/5c.L/5c.S, ovostatin 5C/L/S homeolog following phylogenetic analysis of the vertebrate ovostatin and A2M protein/gene family by Xenbase and the HGNC.
LOC100488897, LOC108695708, LOC100036845 are recorded as Synonyms.
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