Analysis of the human hephaestin gene and protein: comparative modelling of the N-terminus ecto-domain based upon ceruloplasmin
Hephaestin was implicated in mammalian iron homeostasis following its identification as the defective gene in murine sex-linked anaemia. It is a member of the family of copper oxidases that includes mammalian ceruloplasmin, factors V and VIII, yeast fet3 and fet5 and bacterial ascorbate oxidase. Hep...
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| Veröffentlicht in: | Protein engineering 2002-03, Vol.15 (3), p.205-214 |
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| creator | Syed, Basharut A. Beaumont, Nick J. Patel, Alpesh Naylor, Claire E. Bayele, Henry K. Joannou, Christopher L. Rowe, Peter S.N. Evans, Robert W. Srai, S. Kaila S. |
| description | Hephaestin was implicated in mammalian iron homeostasis following its identification as the defective gene in murine sex-linked anaemia. It is a member of the family of copper oxidases that includes mammalian ceruloplasmin, factors V and VIII, yeast fet3 and fet5 and bacterial ascorbate oxidase. Hephaestin is different from ceruloplasmin, a soluble ferroxidase, in having a membrane-spanning region towards the C-terminus. Here we report the gene structure, spanning ~100 kb, of the human homologue of mouse hephaestin. The sequence was assembled from the cDNA clones and the chromosome X genomic sequence data available at the Sanger Centre. It has an open reading frame that encodes a protein of 1158 residues, 85% identical with the murine homologue. A model of the N-terminal ecto-domain has been built based on the known three-dimensional structure of human ceruloplasmin. The overall tertiary structure for the hephaestin and the putative residues involved in binding copper and iron appear to be highly conserved between these proteins, which suggests they share the same fold and a conserved function. |
| doi_str_mv | 10.1093/protein/15.3.205 |
| format | Article |
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Kaila S.</creator><creatorcontrib>Syed, Basharut A. ; Beaumont, Nick J. ; Patel, Alpesh ; Naylor, Claire E. ; Bayele, Henry K. ; Joannou, Christopher L. ; Rowe, Peter S.N. ; Evans, Robert W. ; Srai, S. Kaila S.</creatorcontrib><description>Hephaestin was implicated in mammalian iron homeostasis following its identification as the defective gene in murine sex-linked anaemia. It is a member of the family of copper oxidases that includes mammalian ceruloplasmin, factors V and VIII, yeast fet3 and fet5 and bacterial ascorbate oxidase. Hephaestin is different from ceruloplasmin, a soluble ferroxidase, in having a membrane-spanning region towards the C-terminus. Here we report the gene structure, spanning ~100 kb, of the human homologue of mouse hephaestin. The sequence was assembled from the cDNA clones and the chromosome X genomic sequence data available at the Sanger Centre. It has an open reading frame that encodes a protein of 1158 residues, 85% identical with the murine homologue. A model of the N-terminal ecto-domain has been built based on the known three-dimensional structure of human ceruloplasmin. The overall tertiary structure for the hephaestin and the putative residues involved in binding copper and iron appear to be highly conserved between these proteins, which suggests they share the same fold and a conserved function.</description><identifier>ISSN: 0269-2139</identifier><identifier>ISSN: 1741-0126</identifier><identifier>EISSN: 1460-213X</identifier><identifier>EISSN: 1741-0134</identifier><identifier>DOI: 10.1093/protein/15.3.205</identifier><identifier>PMID: 11932491</identifier><language>eng</language><publisher>England: Oxford University Press</publisher><subject>Base Sequence ; Binding Sites ; ceruloplasmin ; Ceruloplasmin - chemistry ; Copper - chemistry ; Copper - metabolism ; ferroxidase ; hephaestin ; homology modelling ; Humans ; Iron - chemistry ; Iron - metabolism ; Membrane Proteins - chemistry ; Membrane Proteins - genetics ; Models, Molecular ; Molecular Sequence Data ; Protein Structure, Tertiary ; Sequence Alignment ; Structure-Activity Relationship</subject><ispartof>Protein engineering, 2002-03, Vol.15 (3), p.205-214</ispartof><rights>Oxford University Press 2002</rights><rights>Copyright Oxford University Press(England) Mar 2002</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c500t-1bd85641b7fbebefa5b7b72b932a4be0faf7ad901f62129ed0f30f30018b38bf3</citedby><cites>FETCH-LOGICAL-c500t-1bd85641b7fbebefa5b7b72b932a4be0faf7ad901f62129ed0f30f30018b38bf3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>315,782,786,1586,27933,27934</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11932491$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Syed, Basharut A.</creatorcontrib><creatorcontrib>Beaumont, Nick J.</creatorcontrib><creatorcontrib>Patel, Alpesh</creatorcontrib><creatorcontrib>Naylor, Claire E.</creatorcontrib><creatorcontrib>Bayele, Henry K.</creatorcontrib><creatorcontrib>Joannou, Christopher L.</creatorcontrib><creatorcontrib>Rowe, Peter S.N.</creatorcontrib><creatorcontrib>Evans, Robert W.</creatorcontrib><creatorcontrib>Srai, S. Kaila S.</creatorcontrib><title>Analysis of the human hephaestin gene and protein: comparative modelling of the N-terminus ecto-domain based upon ceruloplasmin</title><title>Protein engineering</title><addtitle>Protein Eng</addtitle><addtitle>Protein Eng</addtitle><description>Hephaestin was implicated in mammalian iron homeostasis following its identification as the defective gene in murine sex-linked anaemia. It is a member of the family of copper oxidases that includes mammalian ceruloplasmin, factors V and VIII, yeast fet3 and fet5 and bacterial ascorbate oxidase. Hephaestin is different from ceruloplasmin, a soluble ferroxidase, in having a membrane-spanning region towards the C-terminus. Here we report the gene structure, spanning ~100 kb, of the human homologue of mouse hephaestin. The sequence was assembled from the cDNA clones and the chromosome X genomic sequence data available at the Sanger Centre. It has an open reading frame that encodes a protein of 1158 residues, 85% identical with the murine homologue. A model of the N-terminal ecto-domain has been built based on the known three-dimensional structure of human ceruloplasmin. The overall tertiary structure for the hephaestin and the putative residues involved in binding copper and iron appear to be highly conserved between these proteins, which suggests they share the same fold and a conserved function.</description><subject>Base Sequence</subject><subject>Binding Sites</subject><subject>ceruloplasmin</subject><subject>Ceruloplasmin - chemistry</subject><subject>Copper - chemistry</subject><subject>Copper - metabolism</subject><subject>ferroxidase</subject><subject>hephaestin</subject><subject>homology modelling</subject><subject>Humans</subject><subject>Iron - chemistry</subject><subject>Iron - metabolism</subject><subject>Membrane Proteins - chemistry</subject><subject>Membrane Proteins - genetics</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>Protein Structure, Tertiary</subject><subject>Sequence Alignment</subject><subject>Structure-Activity Relationship</subject><issn>0269-2139</issn><issn>1741-0126</issn><issn>1460-213X</issn><issn>1741-0134</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2002</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkc1v1DAQxS0EokvhzglZHLhU2XrsOB_cqopS0AJCArTiYtnJuJuS2KmdIHriX8erDSBxKZIl-_B7b_zmEfIU2BpYLU7H4Cfs3CnItVhzJu-RFeQFyziI7X2yYryo9-_6iDyK8ZoxVrGaPyRHALXgeQ0r8vPM6f42dpF6S6cd0t08aEd3OO40xqlz9AodUu1augx7SRs_jDroqfuOdPAt9n3nrn7r32cThqFzc6TYTD5r_aCTi9ERWzqP3tEGw9z7sdcxYY_JA6v7iE-W-5h8vnj16fwy23x4_eb8bJM1krEpA9NWssjBlNagQaulKU3JTYqhc4PMalvqtmZgCw68xpZZsT8MKiMqY8UxeXHwTSlu5pRMDV1s0te1Qz9HVYIsIS_ZnSDUVVVxye8GKyFyzosEPv8HvPZzSGuPinMpmaj4fiw7QE3wMQa0agzdoMOtAqb2Xatl_QqkEip1nSTPFt_ZDNj-FSzlJuDkAPh5_B-77EB3ccIff3gdvqmiFKVUl9uv6h1svmzeyq36KH4B_KvGcw</recordid><startdate>20020301</startdate><enddate>20020301</enddate><creator>Syed, Basharut A.</creator><creator>Beaumont, Nick J.</creator><creator>Patel, Alpesh</creator><creator>Naylor, Claire E.</creator><creator>Bayele, Henry K.</creator><creator>Joannou, Christopher L.</creator><creator>Rowe, Peter S.N.</creator><creator>Evans, Robert W.</creator><creator>Srai, S. Kaila S.</creator><general>Oxford University Press</general><general>Oxford Publishing Limited (England)</general><scope>BSCLL</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>7QO</scope><scope>7QP</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>K9.</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>20020301</creationdate><title>Analysis of the human hephaestin gene and protein: comparative modelling of the N-terminus ecto-domain based upon ceruloplasmin</title><author>Syed, Basharut A. ; Beaumont, Nick J. ; Patel, Alpesh ; Naylor, Claire E. ; Bayele, Henry K. ; Joannou, Christopher L. ; Rowe, Peter S.N. ; Evans, Robert W. ; Srai, S. 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Kaila S.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Analysis of the human hephaestin gene and protein: comparative modelling of the N-terminus ecto-domain based upon ceruloplasmin</atitle><jtitle>Protein engineering</jtitle><stitle>Protein Eng</stitle><addtitle>Protein Eng</addtitle><date>2002-03-01</date><risdate>2002</risdate><volume>15</volume><issue>3</issue><spage>205</spage><epage>214</epage><pages>205-214</pages><issn>0269-2139</issn><issn>1741-0126</issn><eissn>1460-213X</eissn><eissn>1741-0134</eissn><abstract>Hephaestin was implicated in mammalian iron homeostasis following its identification as the defective gene in murine sex-linked anaemia. It is a member of the family of copper oxidases that includes mammalian ceruloplasmin, factors V and VIII, yeast fet3 and fet5 and bacterial ascorbate oxidase. Hephaestin is different from ceruloplasmin, a soluble ferroxidase, in having a membrane-spanning region towards the C-terminus. Here we report the gene structure, spanning ~100 kb, of the human homologue of mouse hephaestin. The sequence was assembled from the cDNA clones and the chromosome X genomic sequence data available at the Sanger Centre. It has an open reading frame that encodes a protein of 1158 residues, 85% identical with the murine homologue. A model of the N-terminal ecto-domain has been built based on the known three-dimensional structure of human ceruloplasmin. The overall tertiary structure for the hephaestin and the putative residues involved in binding copper and iron appear to be highly conserved between these proteins, which suggests they share the same fold and a conserved function.</abstract><cop>England</cop><pub>Oxford University Press</pub><pmid>11932491</pmid><doi>10.1093/protein/15.3.205</doi><tpages>10</tpages><oa>free_for_read</oa></addata></record> |
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| identifier | ISSN: 0269-2139 |
| ispartof | Protein engineering, 2002-03, Vol.15 (3), p.205-214 |
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| language | eng |
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| source | MEDLINE; Oxford University Press Journals All Titles (1996-Current); EZB-FREE-00999 freely available EZB journals |
| subjects | Base Sequence Binding Sites ceruloplasmin Ceruloplasmin - chemistry Copper - chemistry Copper - metabolism ferroxidase hephaestin homology modelling Humans Iron - chemistry Iron - metabolism Membrane Proteins - chemistry Membrane Proteins - genetics Models, Molecular Molecular Sequence Data Protein Structure, Tertiary Sequence Alignment Structure-Activity Relationship |
| title | Analysis of the human hephaestin gene and protein: comparative modelling of the N-terminus ecto-domain based upon ceruloplasmin |
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