The complete primary structure of the spermadhesin AWN, a zona pellucida-binding protein isolated from boar spermatozoa
AWN is a boar protein which originates in secretions of the male accessory glands and which becomes sperm surface-associated upon ejaculation. It is one of the components thought to mediate sperm adhesion to the egg's zona pellucida through a carbohydrate-recognition mechanism. AWN may, thus, p...
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| Veröffentlicht in: | FEBS letters 1992-04, Vol.300 (3), p.213-218 |
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| creator | Sanz, Libia Calvete, Juan José Mann, Karlheinz Schäfer, Wolfram Schmid, Erich R. Amselgruber, Werner Sinowatz, Fred Ehrhard, Michael Töpfer-Petersen, Edda |
| description | AWN is a boar protein which originates in secretions of the male accessory glands and which becomes sperm surface-associated upon ejaculation. It is one of the components thought to mediate sperm adhesion to the egg's zona pellucida through a carbohydrate-recognition mechanism. AWN may, thus, participate in the initial events of fertilization in the pig. In this report we describe its complete primary structure by combination of protein-chemical and mass spectrometric methods. AWN exists as two isoforms, AWN-1 and AWN-2, which differ in that AWN-2 is N-terminally acetylated. The amino acid sequence of AWN contains 133 amino acid residues and two disulphide bridges between nearest-neighbour cysteine residues. Analysis of the amino acid sequence of the AWN proteins showed significant similarity only to AQN-1 and AQN-3, two other boar spermadhesins. |
| doi_str_mv | 10.1016/0014-5793(92)80848-B |
| format | Article |
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It is one of the components thought to mediate sperm adhesion to the egg's zona pellucida through a carbohydrate-recognition mechanism. AWN may, thus, participate in the initial events of fertilization in the pig. In this report we describe its complete primary structure by combination of protein-chemical and mass spectrometric methods. AWN exists as two isoforms, AWN-1 and AWN-2, which differ in that AWN-2 is N-terminally acetylated. The amino acid sequence of AWN contains 133 amino acid residues and two disulphide bridges between nearest-neighbour cysteine residues. Analysis of the amino acid sequence of the AWN proteins showed significant similarity only to AQN-1 and AQN-3, two other boar spermadhesins.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/0014-5793(92)80848-B</identifier><identifier>PMID: 1555646</identifier><identifier>CODEN: FEBLAL</identifier><language>eng</language><publisher>Amsterdam: Elsevier B.V</publisher><subject>Amino Acid Sequence ; Animals ; AWN ; AWN protein ; Biological and medical sciences ; Boar sperm protein ; Carrier Proteins - chemistry ; Carrier Proteins - isolation & purification ; Carrier Proteins - pharmacology ; Female ; Fundamental and applied biological sciences. Psychology ; Hormone metabolism and regulation ; Male ; Mammalian male genital system ; Molecular Sequence Data ; pigs ; Primary structure ; Protein Binding ; Seminal Plasma Proteins ; Sperm-Ovum Interactions - drug effects ; Spermadhesin ; spermatozoa ; Spermatozoa - chemistry ; Structure-Activity Relationship ; Swine ; Vertebrates: reproduction ; Zona Pellucida - chemistry ; zona pellucida-binding protein</subject><ispartof>FEBS letters, 1992-04, Vol.300 (3), p.213-218</ispartof><rights>1992</rights><rights>FEBS Letters 300 (1992) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><rights>1992 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c546B-8ad950a82b66e4dd542ea0a14f1f9ba525003b380c2e6a328f99362192bed34a3</citedby><cites>FETCH-LOGICAL-c546B-8ad950a82b66e4dd542ea0a14f1f9ba525003b380c2e6a328f99362192bed34a3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0014-5793(92)80848-B$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=5153700$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1555646$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Sanz, Libia</creatorcontrib><creatorcontrib>Calvete, Juan José</creatorcontrib><creatorcontrib>Mann, Karlheinz</creatorcontrib><creatorcontrib>Schäfer, Wolfram</creatorcontrib><creatorcontrib>Schmid, Erich R.</creatorcontrib><creatorcontrib>Amselgruber, Werner</creatorcontrib><creatorcontrib>Sinowatz, Fred</creatorcontrib><creatorcontrib>Ehrhard, Michael</creatorcontrib><creatorcontrib>Töpfer-Petersen, Edda</creatorcontrib><title>The complete primary structure of the spermadhesin AWN, a zona pellucida-binding protein isolated from boar spermatozoa</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>AWN is a boar protein which originates in secretions of the male accessory glands and which becomes sperm surface-associated upon ejaculation. It is one of the components thought to mediate sperm adhesion to the egg's zona pellucida through a carbohydrate-recognition mechanism. AWN may, thus, participate in the initial events of fertilization in the pig. In this report we describe its complete primary structure by combination of protein-chemical and mass spectrometric methods. AWN exists as two isoforms, AWN-1 and AWN-2, which differ in that AWN-2 is N-terminally acetylated. The amino acid sequence of AWN contains 133 amino acid residues and two disulphide bridges between nearest-neighbour cysteine residues. Analysis of the amino acid sequence of the AWN proteins showed significant similarity only to AQN-1 and AQN-3, two other boar spermadhesins.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>AWN</subject><subject>AWN protein</subject><subject>Biological and medical sciences</subject><subject>Boar sperm protein</subject><subject>Carrier Proteins - chemistry</subject><subject>Carrier Proteins - isolation & purification</subject><subject>Carrier Proteins - pharmacology</subject><subject>Female</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Hormone metabolism and regulation</subject><subject>Male</subject><subject>Mammalian male genital system</subject><subject>Molecular Sequence Data</subject><subject>pigs</subject><subject>Primary structure</subject><subject>Protein Binding</subject><subject>Seminal Plasma Proteins</subject><subject>Sperm-Ovum Interactions - drug effects</subject><subject>Spermadhesin</subject><subject>spermatozoa</subject><subject>Spermatozoa - chemistry</subject><subject>Structure-Activity Relationship</subject><subject>Swine</subject><subject>Vertebrates: reproduction</subject><subject>Zona Pellucida - chemistry</subject><subject>zona pellucida-binding protein</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1992</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkU1v1DAQhi0EKtuFfwCSDwiBRMAfseNckLpVF5AquBRxtBx7Qo2SeGsnVO2vr9NE5QacLM88887MOwi9oOQ9JVR-IISWhahq_qZmbxVRpSp2j9CGqooXvJTqMdo8IE_RcUq_SP4rWh-hIyqEkKXcoOuLS8A29IcORsCH6HsTb3Aa42THKQIOLR4zkQ4Qe-MuIfkBn_z4-g4bfBsGgw_QdZP1zhSNH5wffmaNMEKmfAqdGcHhNoYeN8HEVWUMt8E8Q09a0yV4vr5b9H1_dnH6uTj_9unL6cl5YUUpd4UyrhbEKNZICaVzomRgiKFlS9u6MYIJQnjDFbEMpOFMtXXNJaM1a8Dx0vAter3o5rGuJkij7n2yeWgzQJiSrpiSTOWif4FUcsZEVWWwXEAbQ0oRWr26pinR82H07LqeXdc10_eH0btc9nLVn5oe3J-i5RI5_2rNm2RN10YzWJ8eMEEFr_KuW7RfsGvfwc1_tdb7sx2bE3O8ZvfReZ6PixBk9397iDpZD4MF5yPYUbvg_77QHTirvhM</recordid><startdate>19920406</startdate><enddate>19920406</enddate><creator>Sanz, Libia</creator><creator>Calvete, Juan José</creator><creator>Mann, Karlheinz</creator><creator>Schäfer, Wolfram</creator><creator>Schmid, Erich R.</creator><creator>Amselgruber, Werner</creator><creator>Sinowatz, Fred</creator><creator>Ehrhard, Michael</creator><creator>Töpfer-Petersen, Edda</creator><general>Elsevier B.V</general><general>Elsevier</general><scope>6I.</scope><scope>AAFTH</scope><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>M81</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>19920406</creationdate><title>The complete primary structure of the spermadhesin AWN, a zona pellucida-binding protein isolated from boar spermatozoa</title><author>Sanz, Libia ; Calvete, Juan José ; Mann, Karlheinz ; Schäfer, Wolfram ; Schmid, Erich R. ; Amselgruber, Werner ; Sinowatz, Fred ; Ehrhard, Michael ; Töpfer-Petersen, Edda</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c546B-8ad950a82b66e4dd542ea0a14f1f9ba525003b380c2e6a328f99362192bed34a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1992</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>AWN</topic><topic>AWN protein</topic><topic>Biological and medical sciences</topic><topic>Boar sperm protein</topic><topic>Carrier Proteins - chemistry</topic><topic>Carrier Proteins - isolation & purification</topic><topic>Carrier Proteins - pharmacology</topic><topic>Female</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Hormone metabolism and regulation</topic><topic>Male</topic><topic>Mammalian male genital system</topic><topic>Molecular Sequence Data</topic><topic>pigs</topic><topic>Primary structure</topic><topic>Protein Binding</topic><topic>Seminal Plasma Proteins</topic><topic>Sperm-Ovum Interactions - drug effects</topic><topic>Spermadhesin</topic><topic>spermatozoa</topic><topic>Spermatozoa - chemistry</topic><topic>Structure-Activity Relationship</topic><topic>Swine</topic><topic>Vertebrates: reproduction</topic><topic>Zona Pellucida - chemistry</topic><topic>zona pellucida-binding protein</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Sanz, Libia</creatorcontrib><creatorcontrib>Calvete, Juan José</creatorcontrib><creatorcontrib>Mann, Karlheinz</creatorcontrib><creatorcontrib>Schäfer, Wolfram</creatorcontrib><creatorcontrib>Schmid, Erich R.</creatorcontrib><creatorcontrib>Amselgruber, Werner</creatorcontrib><creatorcontrib>Sinowatz, Fred</creatorcontrib><creatorcontrib>Ehrhard, Michael</creatorcontrib><creatorcontrib>Töpfer-Petersen, Edda</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><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>Bacteriology Abstracts (Microbiology B)</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biochemistry Abstracts 3</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Sanz, Libia</au><au>Calvete, Juan José</au><au>Mann, Karlheinz</au><au>Schäfer, Wolfram</au><au>Schmid, Erich R.</au><au>Amselgruber, Werner</au><au>Sinowatz, Fred</au><au>Ehrhard, Michael</au><au>Töpfer-Petersen, Edda</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The complete primary structure of the spermadhesin AWN, a zona pellucida-binding protein isolated from boar spermatozoa</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>1992-04-06</date><risdate>1992</risdate><volume>300</volume><issue>3</issue><spage>213</spage><epage>218</epage><pages>213-218</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><coden>FEBLAL</coden><abstract>AWN is a boar protein which originates in secretions of the male accessory glands and which becomes sperm surface-associated upon ejaculation. It is one of the components thought to mediate sperm adhesion to the egg's zona pellucida through a carbohydrate-recognition mechanism. AWN may, thus, participate in the initial events of fertilization in the pig. In this report we describe its complete primary structure by combination of protein-chemical and mass spectrometric methods. AWN exists as two isoforms, AWN-1 and AWN-2, which differ in that AWN-2 is N-terminally acetylated. The amino acid sequence of AWN contains 133 amino acid residues and two disulphide bridges between nearest-neighbour cysteine residues. Analysis of the amino acid sequence of the AWN proteins showed significant similarity only to AQN-1 and AQN-3, two other boar spermadhesins.</abstract><cop>Amsterdam</cop><pub>Elsevier B.V</pub><pmid>1555646</pmid><doi>10.1016/0014-5793(92)80848-B</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| identifier | ISSN: 0014-5793 |
| ispartof | FEBS letters, 1992-04, Vol.300 (3), p.213-218 |
| issn | 0014-5793 1873-3468 |
| language | eng |
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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; ScienceDirect Journals (5 years ago - present); Alma/SFX Local Collection |
| subjects | Amino Acid Sequence Animals AWN AWN protein Biological and medical sciences Boar sperm protein Carrier Proteins - chemistry Carrier Proteins - isolation & purification Carrier Proteins - pharmacology Female Fundamental and applied biological sciences. Psychology Hormone metabolism and regulation Male Mammalian male genital system Molecular Sequence Data pigs Primary structure Protein Binding Seminal Plasma Proteins Sperm-Ovum Interactions - drug effects Spermadhesin spermatozoa Spermatozoa - chemistry Structure-Activity Relationship Swine Vertebrates: reproduction Zona Pellucida - chemistry zona pellucida-binding protein |
| title | The complete primary structure of the spermadhesin AWN, a zona pellucida-binding protein isolated from boar spermatozoa |
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