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The precursor region of a protein active in sperm-egg fusion contains a metalloprotease and a disintegrin domain: structural, functional, and evolutionary implications
PH-30, a sperm surface protein involved in sperm-egg fusion, is composed of two subunits, alpha and beta, which are synthesized as precursors and processed, during sperm development, to yield the mature forms. The mature PH-30 alpha/beta complex resembles certain viral fusion proteins in membrane to...
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Published in: | Proceedings of the National Academy of Sciences - PNAS 1993-11, Vol.90 (22), p.10783-10787 |
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container_title | Proceedings of the National Academy of Sciences - PNAS |
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creator | WOLFSBERG, T. G BAZAN, J. F BLOBEL, C. P MYLES, D. G PRIMAKOFF, P WHITE, J. M |
description | PH-30, a sperm surface protein involved in sperm-egg fusion, is composed of two subunits, alpha and beta, which are synthesized as precursors and processed, during sperm development, to yield the mature forms. The mature PH-30 alpha/beta complex resembles certain viral fusion proteins in membrane topology and predicted binding and fusion functions. Furthermore, the mature subunits are similar in sequence to each other and to a family of disintegrin domain-containing snake venom proteins. We report here the sequences of the PH-30 alpha and beta precursor regions. Their domain organizations are similar to each other and to precursors of snake venom metalloproteases and disintegrins. The alpha precursor region contains, from amino to carboxyl terminus, pro, metalloprotease, and disintegrin domains. The beta precursor region contains pro and metalloprotease domains. Residues diagnostic of a catalytically active metalloprotease are present in the alpha, but not the beta, precursor region. We propose that the active sites of the PH-30 alpha and snake venom metalloproteases are structurally similar to that of astacin. PH-30, acting through its metalloprotease and/or disintegrin domains, could be involved in sperm development as well as sperm-egg binding and fusion. Phylogenetic analysis indicates that PH-30 stems from a multidomain ancestral protein. |
doi_str_mv | 10.1073/pnas.90.22.10783 |
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G ; BAZAN, J. F ; BLOBEL, C. P ; MYLES, D. G ; PRIMAKOFF, P ; WHITE, J. M</creator><creatorcontrib>WOLFSBERG, T. G ; BAZAN, J. F ; BLOBEL, C. P ; MYLES, D. G ; PRIMAKOFF, P ; WHITE, J. M</creatorcontrib><description>PH-30, a sperm surface protein involved in sperm-egg fusion, is composed of two subunits, alpha and beta, which are synthesized as precursors and processed, during sperm development, to yield the mature forms. The mature PH-30 alpha/beta complex resembles certain viral fusion proteins in membrane topology and predicted binding and fusion functions. Furthermore, the mature subunits are similar in sequence to each other and to a family of disintegrin domain-containing snake venom proteins. We report here the sequences of the PH-30 alpha and beta precursor regions. Their domain organizations are similar to each other and to precursors of snake venom metalloproteases and disintegrins. The alpha precursor region contains, from amino to carboxyl terminus, pro, metalloprotease, and disintegrin domains. The beta precursor region contains pro and metalloprotease domains. Residues diagnostic of a catalytically active metalloprotease are present in the alpha, but not the beta, precursor region. We propose that the active sites of the PH-30 alpha and snake venom metalloproteases are structurally similar to that of astacin. PH-30, acting through its metalloprotease and/or disintegrin domains, could be involved in sperm development as well as sperm-egg binding and fusion. Phylogenetic analysis indicates that PH-30 stems from a multidomain ancestral protein.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.90.22.10783</identifier><identifier>PMID: 8248170</identifier><identifier>CODEN: PNASA6</identifier><language>eng</language><publisher>Washington, DC: National Acad Sciences</publisher><subject>ADAM Proteins ; Amino Acid Sequence ; Analytical, structural and metabolic biochemistry ; Animals ; Biological and medical sciences ; Cloning, Molecular ; Cricetinae ; Disintegrins ; Female ; Fertilins ; Fundamental and applied biological sciences. Psychology ; Gene Expression ; Male ; Membrane Glycoproteins - chemistry ; Membrane Glycoproteins - genetics ; Membrane Proteins - metabolism ; Metalloendopeptidases - chemistry ; Metalloendopeptidases - metabolism ; Miscellaneous ; Molecular Sequence Data ; Peptides - metabolism ; Phylogeny ; Protein Precursors - metabolism ; Proteins ; Proteins - metabolism ; RNA, Messenger - genetics ; Sequence Alignment ; Sequence Homology, Amino Acid ; Sperm-Ovum Interactions ; Spermatozoa - ultrastructure ; Venoms - metabolism</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 1993-11, Vol.90 (22), p.10783-10787</ispartof><rights>1994 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c572t-dafb1729294db16f7861db1595e20848fb5753627d1a4870b133e422cf91644c3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/90/22.cover.gif</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC47862/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC47862/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,727,780,784,885,27924,27925,53791,53793</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=3850514$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8248170$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>WOLFSBERG, T. G</creatorcontrib><creatorcontrib>BAZAN, J. F</creatorcontrib><creatorcontrib>BLOBEL, C. P</creatorcontrib><creatorcontrib>MYLES, D. G</creatorcontrib><creatorcontrib>PRIMAKOFF, P</creatorcontrib><creatorcontrib>WHITE, J. M</creatorcontrib><title>The precursor region of a protein active in sperm-egg fusion contains a metalloprotease and a disintegrin domain: structural, functional, and evolutionary implications</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>PH-30, a sperm surface protein involved in sperm-egg fusion, is composed of two subunits, alpha and beta, which are synthesized as precursors and processed, during sperm development, to yield the mature forms. The mature PH-30 alpha/beta complex resembles certain viral fusion proteins in membrane topology and predicted binding and fusion functions. Furthermore, the mature subunits are similar in sequence to each other and to a family of disintegrin domain-containing snake venom proteins. We report here the sequences of the PH-30 alpha and beta precursor regions. Their domain organizations are similar to each other and to precursors of snake venom metalloproteases and disintegrins. The alpha precursor region contains, from amino to carboxyl terminus, pro, metalloprotease, and disintegrin domains. The beta precursor region contains pro and metalloprotease domains. Residues diagnostic of a catalytically active metalloprotease are present in the alpha, but not the beta, precursor region. We propose that the active sites of the PH-30 alpha and snake venom metalloproteases are structurally similar to that of astacin. PH-30, acting through its metalloprotease and/or disintegrin domains, could be involved in sperm development as well as sperm-egg binding and fusion. Phylogenetic analysis indicates that PH-30 stems from a multidomain ancestral protein.</description><subject>ADAM Proteins</subject><subject>Amino Acid Sequence</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Cloning, Molecular</subject><subject>Cricetinae</subject><subject>Disintegrins</subject><subject>Female</subject><subject>Fertilins</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gene Expression</subject><subject>Male</subject><subject>Membrane Glycoproteins - chemistry</subject><subject>Membrane Glycoproteins - genetics</subject><subject>Membrane Proteins - metabolism</subject><subject>Metalloendopeptidases - chemistry</subject><subject>Metalloendopeptidases - metabolism</subject><subject>Miscellaneous</subject><subject>Molecular Sequence Data</subject><subject>Peptides - metabolism</subject><subject>Phylogeny</subject><subject>Protein Precursors - metabolism</subject><subject>Proteins</subject><subject>Proteins - metabolism</subject><subject>RNA, Messenger - genetics</subject><subject>Sequence Alignment</subject><subject>Sequence Homology, Amino Acid</subject><subject>Sperm-Ovum Interactions</subject><subject>Spermatozoa - ultrastructure</subject><subject>Venoms - metabolism</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1993</creationdate><recordtype>article</recordtype><recordid>eNp9kU9v1DAQxS0EKkvhzgWRA6o4kMV2nNhBXKqKf1IlLuVsOc4kNXLsYDsr-ER8TZxtWJULJ4_n_d68kQah5wTvCebV29mpuG_xntL1L6oHaEdwS8qGtfgh2mFMeSkYZY_Rkxi_Y4zbWuAzdCYoE4TjHfp9cwvFHEAvIfpQBBiNd4UfCpW7PoFxhdLJHKDIVZwhTCWMYzEsceW0d0kZFzM9QVLW-qNJRSiU63O3N9G4BGPI7t5PmX1XxBQWnZag7Js8x-Xp3q316oCDt8uxEX4VZpqt0Wr9xqfo0aBshGfbe46-ffxwc_W5vP766cvV5XWpa05T2auhI5y2tGV9R5qBi4bkom5roFgwMXQ1r6uG8p4oJjjuSFUBo1QPLWkY09U5en83d166CXoNLuVF5RzMlFeSXhn5r-LMrRz9QbIcRbP9YrMH_2OBmORkogZrlQO_REkaXnFCRAbxHaiDjzHAcIogWK6nletpZYslpfJ42mx5cX-1k2G7ZdZfbbqKWtkhKKdNPGGVqHFNWMZeb9ga8Fe9FySHxdoEP1NGX_4frf4AC1_KDA</recordid><startdate>19931115</startdate><enddate>19931115</enddate><creator>WOLFSBERG, T. 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M</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c572t-dafb1729294db16f7861db1595e20848fb5753627d1a4870b133e422cf91644c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1993</creationdate><topic>ADAM Proteins</topic><topic>Amino Acid Sequence</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Cloning, Molecular</topic><topic>Cricetinae</topic><topic>Disintegrins</topic><topic>Female</topic><topic>Fertilins</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gene Expression</topic><topic>Male</topic><topic>Membrane Glycoproteins - chemistry</topic><topic>Membrane Glycoproteins - genetics</topic><topic>Membrane Proteins - metabolism</topic><topic>Metalloendopeptidases - chemistry</topic><topic>Metalloendopeptidases - metabolism</topic><topic>Miscellaneous</topic><topic>Molecular Sequence Data</topic><topic>Peptides - metabolism</topic><topic>Phylogeny</topic><topic>Protein Precursors - metabolism</topic><topic>Proteins</topic><topic>Proteins - metabolism</topic><topic>RNA, Messenger - genetics</topic><topic>Sequence Alignment</topic><topic>Sequence Homology, Amino Acid</topic><topic>Sperm-Ovum Interactions</topic><topic>Spermatozoa - ultrastructure</topic><topic>Venoms - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>WOLFSBERG, T. G</creatorcontrib><creatorcontrib>BAZAN, J. F</creatorcontrib><creatorcontrib>BLOBEL, C. P</creatorcontrib><creatorcontrib>MYLES, D. G</creatorcontrib><creatorcontrib>PRIMAKOFF, P</creatorcontrib><creatorcontrib>WHITE, J. M</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>WOLFSBERG, T. G</au><au>BAZAN, J. F</au><au>BLOBEL, C. P</au><au>MYLES, D. G</au><au>PRIMAKOFF, P</au><au>WHITE, J. M</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The precursor region of a protein active in sperm-egg fusion contains a metalloprotease and a disintegrin domain: structural, functional, and evolutionary implications</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>1993-11-15</date><risdate>1993</risdate><volume>90</volume><issue>22</issue><spage>10783</spage><epage>10787</epage><pages>10783-10787</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><coden>PNASA6</coden><abstract>PH-30, a sperm surface protein involved in sperm-egg fusion, is composed of two subunits, alpha and beta, which are synthesized as precursors and processed, during sperm development, to yield the mature forms. The mature PH-30 alpha/beta complex resembles certain viral fusion proteins in membrane topology and predicted binding and fusion functions. Furthermore, the mature subunits are similar in sequence to each other and to a family of disintegrin domain-containing snake venom proteins. We report here the sequences of the PH-30 alpha and beta precursor regions. Their domain organizations are similar to each other and to precursors of snake venom metalloproteases and disintegrins. The alpha precursor region contains, from amino to carboxyl terminus, pro, metalloprotease, and disintegrin domains. The beta precursor region contains pro and metalloprotease domains. Residues diagnostic of a catalytically active metalloprotease are present in the alpha, but not the beta, precursor region. We propose that the active sites of the PH-30 alpha and snake venom metalloproteases are structurally similar to that of astacin. PH-30, acting through its metalloprotease and/or disintegrin domains, could be involved in sperm development as well as sperm-egg binding and fusion. Phylogenetic analysis indicates that PH-30 stems from a multidomain ancestral protein.</abstract><cop>Washington, DC</cop><pub>National Acad Sciences</pub><pmid>8248170</pmid><doi>10.1073/pnas.90.22.10783</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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subjects | ADAM Proteins Amino Acid Sequence Analytical, structural and metabolic biochemistry Animals Biological and medical sciences Cloning, Molecular Cricetinae Disintegrins Female Fertilins Fundamental and applied biological sciences. Psychology Gene Expression Male Membrane Glycoproteins - chemistry Membrane Glycoproteins - genetics Membrane Proteins - metabolism Metalloendopeptidases - chemistry Metalloendopeptidases - metabolism Miscellaneous Molecular Sequence Data Peptides - metabolism Phylogeny Protein Precursors - metabolism Proteins Proteins - metabolism RNA, Messenger - genetics Sequence Alignment Sequence Homology, Amino Acid Sperm-Ovum Interactions Spermatozoa - ultrastructure Venoms - metabolism |
title | The precursor region of a protein active in sperm-egg fusion contains a metalloprotease and a disintegrin domain: structural, functional, and evolutionary implications |
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