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.
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rdfs:comment |
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.
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skos:exactMatch | |
uniprot:name |
Mol. Reprod. Dev.
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uniprot:author |
Frayne J.,
Hall L.,
Jury J.A.
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uniprot:date |
1998
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uniprot:pages |
92-97
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uniprot:title |
Sequence analysis of a variety of primate fertilin alpha genes: evidence for non-functional genes in the gorilla and man.
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uniprot:volume |
51
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dc-term:identifier |
doi:10.1002/(SICI)1098-2795(199809)51:1<92::AID-MRD11>3.0.CO;2-W
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