GG: A domain involved in phage LTF apparatus and implicated in human MEB and non-syndromic hearing loss diseases
Here, we report the identification of a novel domain – GG (domain in KIAA1199, FAM3, POMGnT1 and Tmem2 proteins, with two well-conserved glycine residues), present in eukaryotic FAM3 superfamily (FAM3A, FAM3B, FAM3C and FAM3D), POMGnT1 (protein O-linked mannose β-1,2- N-acetylglucosaminyltransferase...
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Veröffentlicht in: | FEBS letters 2006-01, Vol.580 (2), p.581-584 |
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description | Here, we report the identification of a novel domain – GG (domain in KIAA1199, FAM3, POMGnT1 and Tmem2 proteins, with two well-conserved glycine residues), present in eukaryotic FAM3 superfamily (FAM3A, FAM3B, FAM3C and FAM3D), POMGnT1 (protein O-linked mannose β-1,2-
N-acetylglucosaminyltransferase), TEM2 proteins as well as phage gp35 proteins. GG domain has been revealed to be implicated in muscle–eye–brain disease and non-syndromic hearing loss. The presence of GG domain in Bacteriophage gp35 hinge connector of long tail fiber might reflect the horizontal gene transfer from organisms. And we proposed that GG domain might function as important structural element in phage LTF. |
doi_str_mv | 10.1016/j.febslet.2005.12.076 |
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N-acetylglucosaminyltransferase), TEM2 proteins as well as phage gp35 proteins. GG domain has been revealed to be implicated in muscle–eye–brain disease and non-syndromic hearing loss. The presence of GG domain in Bacteriophage gp35 hinge connector of long tail fiber might reflect the horizontal gene transfer from organisms. And we proposed that GG domain might function as important structural element in phage LTF.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/j.febslet.2005.12.076</identifier><identifier>PMID: 16406369</identifier><language>eng</language><publisher>England: Elsevier B.V</publisher><subject>Amino Acid Sequence ; Animals ; Bacteriophage T4 - metabolism ; Bacteriophage T4 - ultrastructure ; FAM3 superfamily ; GG domain ; Gp35 ; Hearing Loss - physiopathology ; Humans ; KIAA1199 ; LTF apparatus ; Molecular Sequence Data ; Muscle–eye–brain disease ; Muscular Dystrophies - physiopathology ; Non-syndromic hearing loss ; Phylogeny ; POMGnT1 ; Protein Structure, Tertiary ; Sequence Alignment ; Sequence Homology, Amino Acid ; Viral Tail Proteins - classification ; Viral Tail Proteins - genetics ; Viral Tail Proteins - metabolism</subject><ispartof>FEBS letters, 2006-01, Vol.580 (2), p.581-584</ispartof><rights>2005 Federation of European Biochemical Societies</rights><rights>FEBS Letters 580 (2006) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5727-6a4949906b8db3d94df1606ebcbd0725757656644682b6a7fd8f40d95226c3fb3</citedby><cites>FETCH-LOGICAL-c5727-6a4949906b8db3d94df1606ebcbd0725757656644682b6a7fd8f40d95226c3fb3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1016%2Fj.febslet.2005.12.076$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0014579305015577$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,776,780,1411,1427,3537,27901,27902,45550,45551,46384,46808,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16406369$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Guo, Jinhu</creatorcontrib><creatorcontrib>Cheng, Haipeng</creatorcontrib><creatorcontrib>Zhao, Shouyuan</creatorcontrib><creatorcontrib>Yu, Long</creatorcontrib><title>GG: A domain involved in phage LTF apparatus and implicated in human MEB and non-syndromic hearing loss diseases</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>Here, we report the identification of a novel domain – GG (domain in KIAA1199, FAM3, POMGnT1 and Tmem2 proteins, with two well-conserved glycine residues), present in eukaryotic FAM3 superfamily (FAM3A, FAM3B, FAM3C and FAM3D), POMGnT1 (protein O-linked mannose β-1,2-
N-acetylglucosaminyltransferase), TEM2 proteins as well as phage gp35 proteins. GG domain has been revealed to be implicated in muscle–eye–brain disease and non-syndromic hearing loss. The presence of GG domain in Bacteriophage gp35 hinge connector of long tail fiber might reflect the horizontal gene transfer from organisms. And we proposed that GG domain might function as important structural element in phage LTF.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Bacteriophage T4 - metabolism</subject><subject>Bacteriophage T4 - ultrastructure</subject><subject>FAM3 superfamily</subject><subject>GG domain</subject><subject>Gp35</subject><subject>Hearing Loss - physiopathology</subject><subject>Humans</subject><subject>KIAA1199</subject><subject>LTF apparatus</subject><subject>Molecular Sequence Data</subject><subject>Muscle–eye–brain disease</subject><subject>Muscular Dystrophies - physiopathology</subject><subject>Non-syndromic hearing loss</subject><subject>Phylogeny</subject><subject>POMGnT1</subject><subject>Protein Structure, Tertiary</subject><subject>Sequence Alignment</subject><subject>Sequence Homology, Amino Acid</subject><subject>Viral Tail Proteins - classification</subject><subject>Viral Tail Proteins - genetics</subject><subject>Viral Tail Proteins - metabolism</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkUFv2yAUx9G0ac26fYRNnHazC9iA2WVqqySdlGmHdWeE4bkhsrFn7Ez59iNzpB67E6D3e394_BD6SElOCRU3h7yBOrYw5YwQnlOWEyleoRWtZJEVpaheoxUhtMy4VMUVehfjgaRzRdVbdEVFSUQh1AoN2-0XfItd3xkfsA_Hvj2CSxs87M0T4N3jBpthMKOZ5ohNSKVuaL0100Lt584E_H19968W-pDFU3Bj33mL92BGH55w28eInY9gIsT36E1j2ggfLus1-rVZP94_ZLsf22_3t7vMcslkJkypSqWIqCtXF06VrqGCCKht7YhkXHIpuBBlGpTVwsjGVU1JnOKMCVs0dXGNPi-5w9j_niFOuvPRQtuaAP0ctSSpk5HyRTAxistCJZAvoB3TQCM0ehh9Z8aTpkSfneiDvjjRZyeaMp2cpL5PlwvmugP33HWRkICHBfjjWzj9X6rerO_Yz7Pgs1_CCeVcyhT1dYmC9LVHD6OO1kOw4PwIdtKu9y-89i9X2bRo</recordid><startdate>20060123</startdate><enddate>20060123</enddate><creator>Guo, Jinhu</creator><creator>Cheng, Haipeng</creator><creator>Zhao, Shouyuan</creator><creator>Yu, Long</creator><general>Elsevier B.V</general><scope>6I.</scope><scope>AAFTH</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>7TK</scope><scope>7U9</scope><scope>H94</scope><scope>7X8</scope></search><sort><creationdate>20060123</creationdate><title>GG: A domain involved in phage LTF apparatus and implicated in human MEB and non-syndromic hearing loss diseases</title><author>Guo, Jinhu ; Cheng, Haipeng ; Zhao, Shouyuan ; Yu, Long</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5727-6a4949906b8db3d94df1606ebcbd0725757656644682b6a7fd8f40d95226c3fb3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Bacteriophage T4 - metabolism</topic><topic>Bacteriophage T4 - ultrastructure</topic><topic>FAM3 superfamily</topic><topic>GG domain</topic><topic>Gp35</topic><topic>Hearing Loss - physiopathology</topic><topic>Humans</topic><topic>KIAA1199</topic><topic>LTF apparatus</topic><topic>Molecular Sequence Data</topic><topic>Muscle–eye–brain disease</topic><topic>Muscular Dystrophies - physiopathology</topic><topic>Non-syndromic hearing loss</topic><topic>Phylogeny</topic><topic>POMGnT1</topic><topic>Protein Structure, Tertiary</topic><topic>Sequence Alignment</topic><topic>Sequence Homology, Amino Acid</topic><topic>Viral Tail Proteins - classification</topic><topic>Viral Tail Proteins - genetics</topic><topic>Viral Tail Proteins - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Guo, Jinhu</creatorcontrib><creatorcontrib>Cheng, Haipeng</creatorcontrib><creatorcontrib>Zhao, Shouyuan</creatorcontrib><creatorcontrib>Yu, Long</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Neurosciences Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Guo, Jinhu</au><au>Cheng, Haipeng</au><au>Zhao, Shouyuan</au><au>Yu, Long</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>GG: A domain involved in phage LTF apparatus and implicated in human MEB and non-syndromic hearing loss diseases</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>2006-01-23</date><risdate>2006</risdate><volume>580</volume><issue>2</issue><spage>581</spage><epage>584</epage><pages>581-584</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>Here, we report the identification of a novel domain – GG (domain in KIAA1199, FAM3, POMGnT1 and Tmem2 proteins, with two well-conserved glycine residues), present in eukaryotic FAM3 superfamily (FAM3A, FAM3B, FAM3C and FAM3D), POMGnT1 (protein O-linked mannose β-1,2-
N-acetylglucosaminyltransferase), TEM2 proteins as well as phage gp35 proteins. GG domain has been revealed to be implicated in muscle–eye–brain disease and non-syndromic hearing loss. The presence of GG domain in Bacteriophage gp35 hinge connector of long tail fiber might reflect the horizontal gene transfer from organisms. And we proposed that GG domain might function as important structural element in phage LTF.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>16406369</pmid><doi>10.1016/j.febslet.2005.12.076</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Amino Acid Sequence Animals Bacteriophage T4 - metabolism Bacteriophage T4 - ultrastructure FAM3 superfamily GG domain Gp35 Hearing Loss - physiopathology Humans KIAA1199 LTF apparatus Molecular Sequence Data Muscle–eye–brain disease Muscular Dystrophies - physiopathology Non-syndromic hearing loss Phylogeny POMGnT1 Protein Structure, Tertiary Sequence Alignment Sequence Homology, Amino Acid Viral Tail Proteins - classification Viral Tail Proteins - genetics Viral Tail Proteins - metabolism |
title | GG: A domain involved in phage LTF apparatus and implicated in human MEB and non-syndromic hearing loss diseases |
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