Identification, sequence analysis and expression of transcripts encoding a putative metalloproteinase, eMDC II, in human and macaque epididymis.
The metalloproteinase-like, disintegrin-like, cysteine-rich (MDC) family is a large group of sequence-related proteins, first characterized in the male reproductive tract, but subsequently also identified in non-reproductive tissues. Their primary translation products are of approximately 90 kDa and each can be divided into distinct domains which show remarkable homology to reprolysins; snake venom haemorrhagic components possessing metalloproteinase and/or disintegrin domains. Several MDC proteins are abundantly-expressed in the male reproductive tract, suggesting functions in fertility. We now describe the cloning, sequence determination and characterization of transcripts encoding the human and macaque (Macaca fascicularis) orthologues of a novel member of the MDC family (eMDC II) which is abundantly-expressed in the epididymis. Unlike many MDC proteins expressed in the reproductive tract, eMDC II possesses the extended 'catalytic centre' consensus sequence characteristic of a reprolysin-like metalloproteinase. This suggests that eMDC II has proteolytic activity.
Jury
J A
JA
Department of Biochemistry, University of Bristol, School of Medical Sciences, Bristol, BS8 1TD, UK.
Perry
A C
AC
Hall
L
L
D051722:ADAM Proteins; D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D001665:Binding Sites; D020134:Catalytic Domain; D003001:Cloning, Molecular; D004822:Epididymis / Q000201:enzymology*; D005260:Female; D020869:Gene Expression Profiling; D006801:Humans; D008252:Macaca fascicularis; D008297:Male; D008666:Metalloendopeptidases / Q000235:genetics* / Q000378:metabolism*; D008969:Molecular Sequence Data; D017421:Sequence Analysis; D014158:Transcription, Genetic; D015032:Zinc / Q000378:metabolism
D051722:ADAM Proteins; C410224:ADAM28 protein, human; D008666:Metalloendopeptidases; D015032:Zinc