Splicing in murine CABYR and its genomic structure
Human calcium-binding tyrosine-phosphorylation regulated protein (CABYR) is a polymorphic, testis-specific, calcium binding protein that undergoes tyrosine phosphorylation during in vitro capacitation. A protein kinase A (PKA) regulatory subunit type II alpha (RII-alpha) homologous domain in the N-t...
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| Veröffentlicht in: | Gene 2003-05, Vol.310, p.67-78 |
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| creator | Sen, Buer Mandal, Arabinda Wolkowicz, Michael J. Kim, Young-Hwan Reddi, P.Prabhakara Shetty, Jagathpala Bush, Leigh Ann Flickinger, Charles J. Herr, John C. |
| description | Human calcium-binding tyrosine-phosphorylation regulated protein (CABYR) is a polymorphic, testis-specific, calcium binding protein that undergoes tyrosine phosphorylation during in vitro capacitation. A protein kinase A (PKA) regulatory subunit type II alpha (RII-alpha) homologous domain in the N-terminus, phosphorylation dependent Ca
++ binding isoforms, and localization to the principal piece of the human sperm tail suggest that CABYR may be involved in sperm motility. In this paper, four mouse orthologous cDNAs and the genomic DNA of
CABYR were cloned, nucleotide and protein sequences of mouse and humans were compared, and the genomic organization of the m
CABYR gene was analyzed. Human and mouse CABYR conserve potential functional motifs including a domain homologous to the dimerization interface of cyclic adenosine monophosphate dependent PKA RII-alpha, 14 PXXP motifs, and regions of homology with extensins and src homology-3-binding protein 1. m
CABYR is arranged into six exons spanning about 14 kb of DNA. Mouse
CABYR showed several similarities with human
CABYR: (1) the protein was localized to the principal piece of mouse epididymal spermatozoa; (2) mouse CABYR has two coding regions (CR-A and CR-B), with 66 and 82% identity, respectively to human; and (3) m
CABYR showed the presence of two testis-specific transcripts of ∼1.4 and ∼2.4 kb. Three murine splice variants were identified, two of which spliced into CR-B. Exon 4, present in all human and mouse variants and comprising 85% of CR-A appears suitable for targeted deletion. The overall 81% nucleotide identity between mouse and human
CABYR, the common genomic organization, presence of similar testis-specific transcripts, localization in the principal piece of tail and occurrence of homologous splice variants indicate an authentic murine orthologue of
CABYR has been identified. |
| doi_str_mv | 10.1016/S0378-1119(03)00495-5 |
| format | Article |
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++ binding isoforms, and localization to the principal piece of the human sperm tail suggest that CABYR may be involved in sperm motility. In this paper, four mouse orthologous cDNAs and the genomic DNA of
CABYR were cloned, nucleotide and protein sequences of mouse and humans were compared, and the genomic organization of the m
CABYR gene was analyzed. Human and mouse CABYR conserve potential functional motifs including a domain homologous to the dimerization interface of cyclic adenosine monophosphate dependent PKA RII-alpha, 14 PXXP motifs, and regions of homology with extensins and src homology-3-binding protein 1. m
CABYR is arranged into six exons spanning about 14 kb of DNA. Mouse
CABYR showed several similarities with human
CABYR: (1) the protein was localized to the principal piece of mouse epididymal spermatozoa; (2) mouse CABYR has two coding regions (CR-A and CR-B), with 66 and 82% identity, respectively to human; and (3) m
CABYR showed the presence of two testis-specific transcripts of ∼1.4 and ∼2.4 kb. Three murine splice variants were identified, two of which spliced into CR-B. Exon 4, present in all human and mouse variants and comprising 85% of CR-A appears suitable for targeted deletion. The overall 81% nucleotide identity between mouse and human
CABYR, the common genomic organization, presence of similar testis-specific transcripts, localization in the principal piece of tail and occurrence of homologous splice variants indicate an authentic murine orthologue of
CABYR has been identified.</description><identifier>ISSN: 0378-1119</identifier><identifier>EISSN: 1879-0038</identifier><identifier>DOI: 10.1016/S0378-1119(03)00495-5</identifier><identifier>PMID: 12801634</identifier><language>eng</language><publisher>Netherlands: Elsevier B.V</publisher><subject>Alternative Splicing ; Amino Acid Sequence ; Animals ; Antibody Specificity ; Base Sequence ; Blotting, Northern ; Blotting, Western ; Calcium binding ; Calcium-Binding Proteins - genetics ; Calcium-Binding Proteins - immunology ; Calcium-Binding Proteins - metabolism ; Capacitation ; Exons ; Female ; Fibrousheathin 2 ; Gene Expression Profiling ; Genes - genetics ; Introns ; Male ; Mice ; Molecular Sequence Data ; Phosphoproteins ; Principal piece ; RNA, Messenger - genetics ; RNA, Messenger - metabolism ; Sequence Homology, Amino Acid ; Sperm ; Spermatozoa - immunology ; Spermatozoa - metabolism ; Tyrosine phosphorylation</subject><ispartof>Gene, 2003-05, Vol.310, p.67-78</ispartof><rights>2003 Elsevier Science B.V.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c458t-b99afd663450a87b2489f2f32db8458069b5bb9c0f0c499c2148835860d829c33</citedby><cites>FETCH-LOGICAL-c458t-b99afd663450a87b2489f2f32db8458069b5bb9c0f0c499c2148835860d829c33</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0378111903004955$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27903,27904,65309</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12801634$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Sen, Buer</creatorcontrib><creatorcontrib>Mandal, Arabinda</creatorcontrib><creatorcontrib>Wolkowicz, Michael J.</creatorcontrib><creatorcontrib>Kim, Young-Hwan</creatorcontrib><creatorcontrib>Reddi, P.Prabhakara</creatorcontrib><creatorcontrib>Shetty, Jagathpala</creatorcontrib><creatorcontrib>Bush, Leigh Ann</creatorcontrib><creatorcontrib>Flickinger, Charles J.</creatorcontrib><creatorcontrib>Herr, John C.</creatorcontrib><title>Splicing in murine CABYR and its genomic structure</title><title>Gene</title><addtitle>Gene</addtitle><description>Human calcium-binding tyrosine-phosphorylation regulated protein (CABYR) is a polymorphic, testis-specific, calcium binding protein that undergoes tyrosine phosphorylation during in vitro capacitation. A protein kinase A (PKA) regulatory subunit type II alpha (RII-alpha) homologous domain in the N-terminus, phosphorylation dependent Ca
++ binding isoforms, and localization to the principal piece of the human sperm tail suggest that CABYR may be involved in sperm motility. In this paper, four mouse orthologous cDNAs and the genomic DNA of
CABYR were cloned, nucleotide and protein sequences of mouse and humans were compared, and the genomic organization of the m
CABYR gene was analyzed. Human and mouse CABYR conserve potential functional motifs including a domain homologous to the dimerization interface of cyclic adenosine monophosphate dependent PKA RII-alpha, 14 PXXP motifs, and regions of homology with extensins and src homology-3-binding protein 1. m
CABYR is arranged into six exons spanning about 14 kb of DNA. Mouse
CABYR showed several similarities with human
CABYR: (1) the protein was localized to the principal piece of mouse epididymal spermatozoa; (2) mouse CABYR has two coding regions (CR-A and CR-B), with 66 and 82% identity, respectively to human; and (3) m
CABYR showed the presence of two testis-specific transcripts of ∼1.4 and ∼2.4 kb. Three murine splice variants were identified, two of which spliced into CR-B. Exon 4, present in all human and mouse variants and comprising 85% of CR-A appears suitable for targeted deletion. The overall 81% nucleotide identity between mouse and human
CABYR, the common genomic organization, presence of similar testis-specific transcripts, localization in the principal piece of tail and occurrence of homologous splice variants indicate an authentic murine orthologue of
CABYR has been identified.</description><subject>Alternative Splicing</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Antibody Specificity</subject><subject>Base Sequence</subject><subject>Blotting, Northern</subject><subject>Blotting, Western</subject><subject>Calcium binding</subject><subject>Calcium-Binding Proteins - genetics</subject><subject>Calcium-Binding Proteins - immunology</subject><subject>Calcium-Binding Proteins - metabolism</subject><subject>Capacitation</subject><subject>Exons</subject><subject>Female</subject><subject>Fibrousheathin 2</subject><subject>Gene Expression Profiling</subject><subject>Genes - genetics</subject><subject>Introns</subject><subject>Male</subject><subject>Mice</subject><subject>Molecular Sequence Data</subject><subject>Phosphoproteins</subject><subject>Principal piece</subject><subject>RNA, Messenger - genetics</subject><subject>RNA, Messenger - metabolism</subject><subject>Sequence Homology, Amino Acid</subject><subject>Sperm</subject><subject>Spermatozoa - immunology</subject><subject>Spermatozoa - metabolism</subject><subject>Tyrosine phosphorylation</subject><issn>0378-1119</issn><issn>1879-0038</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkMtKxDAUhoMozjj6CEpWoovqSdK0yUrGwRsMCI4uXIUmTYdIL2PSCr69mQu69GzO5vvPz_kQOiVwRYBk1wtguUgIIfIC2CVAKnnC99CYiFwmAEzso_EvMkJHIXxAHM7pIRoRKuINlo4RXaxqZ1y7xK7FzeBda_Fsevv-gou2xK4PeGnbrnEGh94Pph-8PUYHVVEHe7LbE_R2f_c6e0zmzw9Ps-k8MSkXfaKlLKoyiy0cCpFrmgpZ0YrRUosIQCY111oaqMCkUhpKUiEYFxmUgkrD2ASdb--ufPc52NCrxgVj67pobTcElTMWv4mZ_0AiBNCM8gjyLWh8F4K3lVp51xT-WxFQa6tqY1WtlSlgamNVrXNnu4JBN7b8S-00RuBmC9jo48tZr4JxtjW2dN6aXpWd-6fiBxvgg_4</recordid><startdate>20030522</startdate><enddate>20030522</enddate><creator>Sen, Buer</creator><creator>Mandal, Arabinda</creator><creator>Wolkowicz, Michael J.</creator><creator>Kim, Young-Hwan</creator><creator>Reddi, P.Prabhakara</creator><creator>Shetty, Jagathpala</creator><creator>Bush, Leigh Ann</creator><creator>Flickinger, Charles J.</creator><creator>Herr, John C.</creator><general>Elsevier B.V</general><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>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>20030522</creationdate><title>Splicing in murine CABYR and its genomic structure</title><author>Sen, Buer ; Mandal, Arabinda ; Wolkowicz, Michael J. ; Kim, Young-Hwan ; Reddi, P.Prabhakara ; Shetty, Jagathpala ; Bush, Leigh Ann ; Flickinger, Charles J. ; Herr, John C.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c458t-b99afd663450a87b2489f2f32db8458069b5bb9c0f0c499c2148835860d829c33</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2003</creationdate><topic>Alternative Splicing</topic><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Antibody Specificity</topic><topic>Base Sequence</topic><topic>Blotting, Northern</topic><topic>Blotting, Western</topic><topic>Calcium binding</topic><topic>Calcium-Binding Proteins - genetics</topic><topic>Calcium-Binding Proteins - immunology</topic><topic>Calcium-Binding Proteins - metabolism</topic><topic>Capacitation</topic><topic>Exons</topic><topic>Female</topic><topic>Fibrousheathin 2</topic><topic>Gene Expression Profiling</topic><topic>Genes - genetics</topic><topic>Introns</topic><topic>Male</topic><topic>Mice</topic><topic>Molecular Sequence Data</topic><topic>Phosphoproteins</topic><topic>Principal piece</topic><topic>RNA, Messenger - genetics</topic><topic>RNA, Messenger - metabolism</topic><topic>Sequence Homology, Amino Acid</topic><topic>Sperm</topic><topic>Spermatozoa - immunology</topic><topic>Spermatozoa - metabolism</topic><topic>Tyrosine phosphorylation</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Sen, Buer</creatorcontrib><creatorcontrib>Mandal, Arabinda</creatorcontrib><creatorcontrib>Wolkowicz, Michael J.</creatorcontrib><creatorcontrib>Kim, Young-Hwan</creatorcontrib><creatorcontrib>Reddi, P.Prabhakara</creatorcontrib><creatorcontrib>Shetty, Jagathpala</creatorcontrib><creatorcontrib>Bush, Leigh Ann</creatorcontrib><creatorcontrib>Flickinger, Charles J.</creatorcontrib><creatorcontrib>Herr, John C.</creatorcontrib><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>MEDLINE - Academic</collection><jtitle>Gene</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Sen, Buer</au><au>Mandal, Arabinda</au><au>Wolkowicz, Michael J.</au><au>Kim, Young-Hwan</au><au>Reddi, P.Prabhakara</au><au>Shetty, Jagathpala</au><au>Bush, Leigh Ann</au><au>Flickinger, Charles J.</au><au>Herr, John C.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Splicing in murine CABYR and its genomic structure</atitle><jtitle>Gene</jtitle><addtitle>Gene</addtitle><date>2003-05-22</date><risdate>2003</risdate><volume>310</volume><spage>67</spage><epage>78</epage><pages>67-78</pages><issn>0378-1119</issn><eissn>1879-0038</eissn><abstract>Human calcium-binding tyrosine-phosphorylation regulated protein (CABYR) is a polymorphic, testis-specific, calcium binding protein that undergoes tyrosine phosphorylation during in vitro capacitation. A protein kinase A (PKA) regulatory subunit type II alpha (RII-alpha) homologous domain in the N-terminus, phosphorylation dependent Ca
++ binding isoforms, and localization to the principal piece of the human sperm tail suggest that CABYR may be involved in sperm motility. In this paper, four mouse orthologous cDNAs and the genomic DNA of
CABYR were cloned, nucleotide and protein sequences of mouse and humans were compared, and the genomic organization of the m
CABYR gene was analyzed. Human and mouse CABYR conserve potential functional motifs including a domain homologous to the dimerization interface of cyclic adenosine monophosphate dependent PKA RII-alpha, 14 PXXP motifs, and regions of homology with extensins and src homology-3-binding protein 1. m
CABYR is arranged into six exons spanning about 14 kb of DNA. Mouse
CABYR showed several similarities with human
CABYR: (1) the protein was localized to the principal piece of mouse epididymal spermatozoa; (2) mouse CABYR has two coding regions (CR-A and CR-B), with 66 and 82% identity, respectively to human; and (3) m
CABYR showed the presence of two testis-specific transcripts of ∼1.4 and ∼2.4 kb. Three murine splice variants were identified, two of which spliced into CR-B. Exon 4, present in all human and mouse variants and comprising 85% of CR-A appears suitable for targeted deletion. The overall 81% nucleotide identity between mouse and human
CABYR, the common genomic organization, presence of similar testis-specific transcripts, localization in the principal piece of tail and occurrence of homologous splice variants indicate an authentic murine orthologue of
CABYR has been identified.</abstract><cop>Netherlands</cop><pub>Elsevier B.V</pub><pmid>12801634</pmid><doi>10.1016/S0378-1119(03)00495-5</doi><tpages>12</tpages></addata></record> |
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| subjects | Alternative Splicing Amino Acid Sequence Animals Antibody Specificity Base Sequence Blotting, Northern Blotting, Western Calcium binding Calcium-Binding Proteins - genetics Calcium-Binding Proteins - immunology Calcium-Binding Proteins - metabolism Capacitation Exons Female Fibrousheathin 2 Gene Expression Profiling Genes - genetics Introns Male Mice Molecular Sequence Data Phosphoproteins Principal piece RNA, Messenger - genetics RNA, Messenger - metabolism Sequence Homology, Amino Acid Sperm Spermatozoa - immunology Spermatozoa - metabolism Tyrosine phosphorylation |
| title | Splicing in murine CABYR and its genomic structure |
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