Mol. Reprod. Dev.

The sperm surface fertilin complex was first described in the guinea pig where it was found as a heterodimer of alpha and beta subunits, both of which were proposed to play a role in sperm-oolemma recognition and plasma membrane fusion during fertilisation. Whilst the beta subunit is apparently testis-specific, the finding of low levels of fertilin alpha in nonreproductive tissues has cast some doubt on a unique role in fertilisation. Moreover, the absence of a functional fertilin alpha gene in the human would imply that this gene product is not absolutely essential for fertilisation, although it could play a facilitatory role. We now describe the organisation and sequence of the fertilin alpha genes in a range of primates, including the great apes, and find that the gorilla gene, like that of the human, is non-functional.

Source:http://purl.uniprot.org/citations/9712322

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The sperm surface fertilin complex was first described in the guinea pig where it was found as a heterodimer of alpha and beta subunits, both of which were proposed to play a role in sperm-oolemma recognition and plasma membrane fusion during fertilisation. Whilst the beta subunit is apparently testis-specific, the finding of low levels of fertilin alpha in nonreproductive tissues has cast some doubt on a unique role in fertilisation. Moreover, the absence of a functional fertilin alpha gene in the human would imply that this gene product is not absolutely essential for fertilisation, although it could play a facilitatory role. We now describe the organisation and sequence of the fertilin alpha genes in a range of primates, including the great apes, and find that the gorilla gene, like that of the human, is non-functional.
skos:exactMatch
uniprot:name
Mol. Reprod. Dev.
uniprot:author
Frayne J., Hall L., Jury J.A.
uniprot:date
1998
uniprot:pages
92-97
uniprot:title
Sequence analysis of a variety of primate fertilin alpha genes: evidence for non-functional genes in the gorilla and man.
uniprot:volume
51
dc-term:identifier
doi:10.1002/(SICI)1098-2795(199809)51:1<92::AID-MRD11>3.0.CO;2-W