Abstract:
:The urine of bank voles (Myodes glareolus) contains substantial quantities of a small protein that is expressed at much higher levels in males than females, and at higher levels in males in the breeding season. This protein was purified and completely sequenced at the protein level by mass spectrometry. Leucine/isoleucine ambiguity was completely resolved by metabolic labelling, monitoring the incorporation of dietary deuterated leucine into specific sites in the protein. The predicted mass of the sequenced protein was exactly consonant with the mass of the protein measured in bank vole urine samples, correcting for the formation of two disulfide bonds. The sequence of the protein revealed that it was a lipocalin related to aphrodisin and other odorant-binding proteins (OBPs), but differed from all OBPs previously described. The pattern of secretion in urine used for scent marking by male bank voles, and the similarity to other lipocalins used as chemical signals in rodents, suggest that this protein plays a role in male sexual and/or competitive communication. We propose the name glareosin for this novel protein to reflect the origin of the protein and to emphasize the distinction from known OBPs.
journal_name
Open Bioljournal_title
Open biologyauthors
Loxley GM,Unsworth J,Turton MJ,Jebb A,Lilley KS,Simpson DM,Rigden DJ,Hurst JL,Beynon RJdoi
10.1098/rsob.170135subject
Has Abstractpub_date
2017-09-01 00:00:00issue
9issn
2046-2441pii
rsob.170135journal_volume
7pub_type
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