Cloning and characterization of a novel, human cellular retinaldehyde-binding protein CRALBP-like (CRALBPL) gene
Cellular retinaldehyde-binding protein (CRALBP) plays a role in the vertebrate visual process as a substrate-routing protein. It belongs to a widespread lipid-binding SEC14-like protein family. All the members of the family have the lipid-binding domain called CRAL-TRIO. Here we have isolated a new...
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| Veröffentlicht in: | Biotechnology letters 2006-09, Vol.28 (17), p.1327-1333 |
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| creator | KONG, Ya-Hui YE, Guang-Ming KAI QU PAN, Wen-Qi LIU, Xiang-Hua BO WAN GUO, Jin-Hu LONG YU |
| description | Cellular retinaldehyde-binding protein (CRALBP) plays a role in the vertebrate visual process as a substrate-routing protein. It belongs to a widespread lipid-binding SEC14-like protein family. All the members of the family have the lipid-binding domain called CRAL-TRIO. Here we have isolated a new human CRAL-TRIO domain containing a CRALBP-like (CRALBPL) gene from the cDNA library of human adult brain. The CRALBPL gene consisted of 1,694 bp and had an ORF encoding putatively 354 amino acids with a CRAL-TRIO domain from 118 to 279 aa. The expression pattern in 18 human tissues indicated that CRALBPL gene was mainly expressed in brain. The alignment of CRAL-TRIO domain showed that CRALBPL had 45% identity with human CRALBP. Subcellular location revealed that CRALBPL protein was located in the cytoplasm of HeLa cells. Western blotting indicated that the CRALBPL had a molecular weight of about 40 kDa. |
| doi_str_mv | 10.1007/s10529-006-9096-5 |
| format | Article |
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It belongs to a widespread lipid-binding SEC14-like protein family. All the members of the family have the lipid-binding domain called CRAL-TRIO. Here we have isolated a new human CRAL-TRIO domain containing a CRALBP-like (CRALBPL) gene from the cDNA library of human adult brain. The CRALBPL gene consisted of 1,694 bp and had an ORF encoding putatively 354 amino acids with a CRAL-TRIO domain from 118 to 279 aa. The expression pattern in 18 human tissues indicated that CRALBPL gene was mainly expressed in brain. The alignment of CRAL-TRIO domain showed that CRALBPL had 45% identity with human CRALBP. Subcellular location revealed that CRALBPL protein was located in the cytoplasm of HeLa cells. Western blotting indicated that the CRALBPL had a molecular weight of about 40 kDa.</description><identifier>ISSN: 0141-5492</identifier><identifier>EISSN: 1573-6776</identifier><identifier>DOI: 10.1007/s10529-006-9096-5</identifier><identifier>PMID: 16802092</identifier><identifier>CODEN: BILED3</identifier><language>eng</language><publisher>Dordrecht: Springer</publisher><subject>Amino Acid Sequence ; Amino acids ; Base Sequence ; Biological and medical sciences ; Biotechnology ; Brain - metabolism ; Carrier Proteins - biosynthesis ; Carrier Proteins - chemistry ; Carrier Proteins - genetics ; Chromosome Mapping ; Cloning ; Cloning, Molecular ; Fundamental and applied biological sciences. Psychology ; HeLa Cells ; Humans ; Molecular Sequence Data ; Proteins ; Recombinant Proteins - biosynthesis ; RNA, Messenger - analysis</subject><ispartof>Biotechnology letters, 2006-09, Vol.28 (17), p.1327-1333</ispartof><rights>2006 INIST-CNRS</rights><rights>Springer Science+Business Media, Inc. 2006</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c419t-ae2edc68b2df4cb9bc9fb62d1ddc0ebc430faeda79eb5d328244ec482d45592d3</citedby><cites>FETCH-LOGICAL-c419t-ae2edc68b2df4cb9bc9fb62d1ddc0ebc430faeda79eb5d328244ec482d45592d3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=18087300$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16802092$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>KONG, Ya-Hui</creatorcontrib><creatorcontrib>YE, Guang-Ming</creatorcontrib><creatorcontrib>KAI QU</creatorcontrib><creatorcontrib>PAN, Wen-Qi</creatorcontrib><creatorcontrib>LIU, Xiang-Hua</creatorcontrib><creatorcontrib>BO WAN</creatorcontrib><creatorcontrib>GUO, Jin-Hu</creatorcontrib><creatorcontrib>LONG YU</creatorcontrib><title>Cloning and characterization of a novel, human cellular retinaldehyde-binding protein CRALBP-like (CRALBPL) gene</title><title>Biotechnology letters</title><addtitle>Biotechnol Lett</addtitle><description>Cellular retinaldehyde-binding protein (CRALBP) plays a role in the vertebrate visual process as a substrate-routing protein. It belongs to a widespread lipid-binding SEC14-like protein family. All the members of the family have the lipid-binding domain called CRAL-TRIO. Here we have isolated a new human CRAL-TRIO domain containing a CRALBP-like (CRALBPL) gene from the cDNA library of human adult brain. The CRALBPL gene consisted of 1,694 bp and had an ORF encoding putatively 354 amino acids with a CRAL-TRIO domain from 118 to 279 aa. The expression pattern in 18 human tissues indicated that CRALBPL gene was mainly expressed in brain. The alignment of CRAL-TRIO domain showed that CRALBPL had 45% identity with human CRALBP. Subcellular location revealed that CRALBPL protein was located in the cytoplasm of HeLa cells. Western blotting indicated that the CRALBPL had a molecular weight of about 40 kDa.</description><subject>Amino Acid Sequence</subject><subject>Amino acids</subject><subject>Base Sequence</subject><subject>Biological and medical sciences</subject><subject>Biotechnology</subject><subject>Brain - metabolism</subject><subject>Carrier Proteins - biosynthesis</subject><subject>Carrier Proteins - chemistry</subject><subject>Carrier Proteins - genetics</subject><subject>Chromosome Mapping</subject><subject>Cloning</subject><subject>Cloning, Molecular</subject><subject>Fundamental and applied biological sciences. 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It belongs to a widespread lipid-binding SEC14-like protein family. All the members of the family have the lipid-binding domain called CRAL-TRIO. Here we have isolated a new human CRAL-TRIO domain containing a CRALBP-like (CRALBPL) gene from the cDNA library of human adult brain. The CRALBPL gene consisted of 1,694 bp and had an ORF encoding putatively 354 amino acids with a CRAL-TRIO domain from 118 to 279 aa. The expression pattern in 18 human tissues indicated that CRALBPL gene was mainly expressed in brain. The alignment of CRAL-TRIO domain showed that CRALBPL had 45% identity with human CRALBP. Subcellular location revealed that CRALBPL protein was located in the cytoplasm of HeLa cells. Western blotting indicated that the CRALBPL had a molecular weight of about 40 kDa.</abstract><cop>Dordrecht</cop><pub>Springer</pub><pmid>16802092</pmid><doi>10.1007/s10529-006-9096-5</doi><tpages>7</tpages></addata></record> |
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| subjects | Amino Acid Sequence Amino acids Base Sequence Biological and medical sciences Biotechnology Brain - metabolism Carrier Proteins - biosynthesis Carrier Proteins - chemistry Carrier Proteins - genetics Chromosome Mapping Cloning Cloning, Molecular Fundamental and applied biological sciences. Psychology HeLa Cells Humans Molecular Sequence Data Proteins Recombinant Proteins - biosynthesis RNA, Messenger - analysis |
| title | Cloning and characterization of a novel, human cellular retinaldehyde-binding protein CRALBP-like (CRALBPL) gene |
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