Comparative Genomic Characterization of Relaxin Peptide Family in Cattle and Buffalo
Relaxin family peptides significantly regulate reproduction, nutrient metabolism, and immune response in mammals. The present study aimed to identify and characterize the relaxin family peptides in cattle and buffalo at the genome level. The genomic and proteomic sequences of cattle, buffalo, goat,...
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| description | Relaxin family peptides significantly regulate reproduction, nutrient metabolism, and immune response in mammals. The present study aimed to identify and characterize the relaxin family peptides in cattle and buffalo at the genome level. The genomic and proteomic sequences of cattle, buffalo, goat, sheep, horse, and camel were accessed through the NCBI database, and BLAST was performed. We identified four relaxin peptides genes (RLN3, INSL3, INSL5, and INSL6) in Bos taurus, whereas three relaxin genes (RLN3, INSL3, and INSL6) in Bubalus bubalis. Evolutionary analysis revealed the conserved nature of relaxin family peptides in buffalo and cattle. Physicochemical properties revealed that relaxin proteins were thermostable, hydrophilic, and basic peptides except for INSL5 which was an acidic peptide. Three nonsynonymous mutations (two in RLN3 at positions A16 > T and P29 > A, and one in INSL6 at position R32 > Q) in Bos taurus, whereas two nonsynonymous mutations (one in RLN3 at positions G105 > w and one in INSL3 at position G22 > R) in Bubalus bubalis, were identified. INSL3 had one indel (insertion) at position 55 in Bos taurus. Gene duplication analysis revealed predominantly segmental duplications (INSL5/RLN3 and INSL6/INSL3 gene pairs) that helped expand this gene family, whereas Bubalus bubalis showed primarily tandem duplication (INSL3/RLN3). Our study concluded that relaxin family peptides remained conserved during the evolution, and gene duplications might help to adapt and enrich specific functions like reproduction, nutrient metabolism, and immune response. Further, the nonsynonymous mutations identified potentially affect these functions in buffalo. |
| doi_str_mv | 10.1155/2022/1581714 |
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The present study aimed to identify and characterize the relaxin family peptides in cattle and buffalo at the genome level. The genomic and proteomic sequences of cattle, buffalo, goat, sheep, horse, and camel were accessed through the NCBI database, and BLAST was performed. We identified four relaxin peptides genes (RLN3, INSL3, INSL5, and INSL6) in Bos taurus, whereas three relaxin genes (RLN3, INSL3, and INSL6) in Bubalus bubalis. Evolutionary analysis revealed the conserved nature of relaxin family peptides in buffalo and cattle. Physicochemical properties revealed that relaxin proteins were thermostable, hydrophilic, and basic peptides except for INSL5 which was an acidic peptide. Three nonsynonymous mutations (two in RLN3 at positions A16 > T and P29 > A, and one in INSL6 at position R32 > Q) in Bos taurus, whereas two nonsynonymous mutations (one in RLN3 at positions G105 > w and one in INSL3 at position G22 > R) in Bubalus bubalis, were identified. INSL3 had one indel (insertion) at position 55 in Bos taurus. Gene duplication analysis revealed predominantly segmental duplications (INSL5/RLN3 and INSL6/INSL3 gene pairs) that helped expand this gene family, whereas Bubalus bubalis showed primarily tandem duplication (INSL3/RLN3). Our study concluded that relaxin family peptides remained conserved during the evolution, and gene duplications might help to adapt and enrich specific functions like reproduction, nutrient metabolism, and immune response. Further, the nonsynonymous mutations identified potentially affect these functions in buffalo.</description><identifier>ISSN: 2314-6133</identifier><identifier>EISSN: 2314-6141</identifier><identifier>DOI: 10.1155/2022/1581714</identifier><language>eng</language><publisher>New York: Hindawi</publisher><subject>Amino acids ; Binding sites ; Bos taurus ; Bubalus bubalis ; Buffalo ; Cattle ; Chromosomes ; Comparative analysis ; Gene duplication ; Genes ; Genetic aspects ; Genetic research ; Genomes ; Genomics ; Identification and classification ; Immune response ; Immune system ; INSL3 gene ; Insulin ; Metabolism ; Molecular evolution ; Molecular weight ; Mutation ; Nature conservation ; Nutrients ; Peptides ; Phylogenetics ; Physicochemical properties ; Proteins ; Proteomics ; Relaxin ; Reproduction ; Reproduction (copying) ; Sheep ; Software ; Water buffalo</subject><ispartof>BioMed research international, 2022-10, Vol.2022, p.1-11</ispartof><rights>Copyright © 2022 Muhammad Saif-ur Rehman et al.</rights><rights>COPYRIGHT 2022 John Wiley & Sons, Inc.</rights><rights>Copyright © 2022 Muhammad Saif-ur Rehman et al. This is an open access article distributed under the Creative Commons Attribution License (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License. https://creativecommons.org/licenses/by/4.0</rights><rights>Copyright © 2022 Muhammad Saif-ur Rehman et al. 2022</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c453t-8f3122add2414ee152feea0de9f499a4c235e77ebcdd0a91888851729bb9f48f3</citedby><cites>FETCH-LOGICAL-c453t-8f3122add2414ee152feea0de9f499a4c235e77ebcdd0a91888851729bb9f48f3</cites><orcidid>0000-0002-8781-0510 ; 0000-0001-8670-3011 ; 0000-0001-7938-5051</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC9553489/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC9553489/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,885,27924,27925,53791,53793</link.rule.ids></links><search><contributor>Ali, Akhtar</contributor><contributor>Akhtar Ali</contributor><creatorcontrib>Rehman, Muhammad Saif-ur</creatorcontrib><creatorcontrib>Hassan, Faiz-ul</creatorcontrib><creatorcontrib>Rehman, Zia-ur</creatorcontrib><creatorcontrib>Hussain, Hafiz Noubahar</creatorcontrib><creatorcontrib>Shahid, Muhammad Adnan</creatorcontrib><creatorcontrib>Mushahid, Muhammad</creatorcontrib><creatorcontrib>Shokrollahi, Borhan</creatorcontrib><title>Comparative Genomic Characterization of Relaxin Peptide Family in Cattle and Buffalo</title><title>BioMed research international</title><description>Relaxin family peptides significantly regulate reproduction, nutrient metabolism, and immune response in mammals. The present study aimed to identify and characterize the relaxin family peptides in cattle and buffalo at the genome level. The genomic and proteomic sequences of cattle, buffalo, goat, sheep, horse, and camel were accessed through the NCBI database, and BLAST was performed. We identified four relaxin peptides genes (RLN3, INSL3, INSL5, and INSL6) in Bos taurus, whereas three relaxin genes (RLN3, INSL3, and INSL6) in Bubalus bubalis. Evolutionary analysis revealed the conserved nature of relaxin family peptides in buffalo and cattle. Physicochemical properties revealed that relaxin proteins were thermostable, hydrophilic, and basic peptides except for INSL5 which was an acidic peptide. Three nonsynonymous mutations (two in RLN3 at positions A16 > T and P29 > A, and one in INSL6 at position R32 > Q) in Bos taurus, whereas two nonsynonymous mutations (one in RLN3 at positions G105 > w and one in INSL3 at position G22 > R) in Bubalus bubalis, were identified. INSL3 had one indel (insertion) at position 55 in Bos taurus. Gene duplication analysis revealed predominantly segmental duplications (INSL5/RLN3 and INSL6/INSL3 gene pairs) that helped expand this gene family, whereas Bubalus bubalis showed primarily tandem duplication (INSL3/RLN3). Our study concluded that relaxin family peptides remained conserved during the evolution, and gene duplications might help to adapt and enrich specific functions like reproduction, nutrient metabolism, and immune response. Further, the nonsynonymous mutations identified potentially affect these functions in buffalo.</description><subject>Amino acids</subject><subject>Binding sites</subject><subject>Bos taurus</subject><subject>Bubalus bubalis</subject><subject>Buffalo</subject><subject>Cattle</subject><subject>Chromosomes</subject><subject>Comparative analysis</subject><subject>Gene duplication</subject><subject>Genes</subject><subject>Genetic aspects</subject><subject>Genetic research</subject><subject>Genomes</subject><subject>Genomics</subject><subject>Identification and classification</subject><subject>Immune response</subject><subject>Immune system</subject><subject>INSL3 gene</subject><subject>Insulin</subject><subject>Metabolism</subject><subject>Molecular evolution</subject><subject>Molecular weight</subject><subject>Mutation</subject><subject>Nature conservation</subject><subject>Nutrients</subject><subject>Peptides</subject><subject>Phylogenetics</subject><subject>Physicochemical properties</subject><subject>Proteins</subject><subject>Proteomics</subject><subject>Relaxin</subject><subject>Reproduction</subject><subject>Reproduction (copying)</subject><subject>Sheep</subject><subject>Software</subject><subject>Water 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Genomic Characterization of Relaxin Peptide Family in Cattle and Buffalo</title><author>Rehman, Muhammad Saif-ur ; Hassan, Faiz-ul ; Rehman, Zia-ur ; Hussain, Hafiz Noubahar ; Shahid, Muhammad Adnan ; Mushahid, Muhammad ; Shokrollahi, Borhan</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c453t-8f3122add2414ee152feea0de9f499a4c235e77ebcdd0a91888851729bb9f48f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2022</creationdate><topic>Amino acids</topic><topic>Binding sites</topic><topic>Bos taurus</topic><topic>Bubalus bubalis</topic><topic>Buffalo</topic><topic>Cattle</topic><topic>Chromosomes</topic><topic>Comparative analysis</topic><topic>Gene duplication</topic><topic>Genes</topic><topic>Genetic aspects</topic><topic>Genetic research</topic><topic>Genomes</topic><topic>Genomics</topic><topic>Identification and classification</topic><topic>Immune response</topic><topic>Immune system</topic><topic>INSL3 gene</topic><topic>Insulin</topic><topic>Metabolism</topic><topic>Molecular evolution</topic><topic>Molecular weight</topic><topic>Mutation</topic><topic>Nature conservation</topic><topic>Nutrients</topic><topic>Peptides</topic><topic>Phylogenetics</topic><topic>Physicochemical properties</topic><topic>Proteins</topic><topic>Proteomics</topic><topic>Relaxin</topic><topic>Reproduction</topic><topic>Reproduction (copying)</topic><topic>Sheep</topic><topic>Software</topic><topic>Water buffalo</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Rehman, Muhammad Saif-ur</creatorcontrib><creatorcontrib>Hassan, Faiz-ul</creatorcontrib><creatorcontrib>Rehman, Zia-ur</creatorcontrib><creatorcontrib>Hussain, Hafiz Noubahar</creatorcontrib><creatorcontrib>Shahid, Muhammad Adnan</creatorcontrib><creatorcontrib>Mushahid, Muhammad</creatorcontrib><creatorcontrib>Shokrollahi, Borhan</creatorcontrib><collection>Hindawi Publishing 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significantly regulate reproduction, nutrient metabolism, and immune response in mammals. The present study aimed to identify and characterize the relaxin family peptides in cattle and buffalo at the genome level. The genomic and proteomic sequences of cattle, buffalo, goat, sheep, horse, and camel were accessed through the NCBI database, and BLAST was performed. We identified four relaxin peptides genes (RLN3, INSL3, INSL5, and INSL6) in Bos taurus, whereas three relaxin genes (RLN3, INSL3, and INSL6) in Bubalus bubalis. Evolutionary analysis revealed the conserved nature of relaxin family peptides in buffalo and cattle. Physicochemical properties revealed that relaxin proteins were thermostable, hydrophilic, and basic peptides except for INSL5 which was an acidic peptide. Three nonsynonymous mutations (two in RLN3 at positions A16 > T and P29 > A, and one in INSL6 at position R32 > Q) in Bos taurus, whereas two nonsynonymous mutations (one in RLN3 at positions G105 > w and one in INSL3 at position G22 > R) in Bubalus bubalis, were identified. INSL3 had one indel (insertion) at position 55 in Bos taurus. Gene duplication analysis revealed predominantly segmental duplications (INSL5/RLN3 and INSL6/INSL3 gene pairs) that helped expand this gene family, whereas Bubalus bubalis showed primarily tandem duplication (INSL3/RLN3). Our study concluded that relaxin family peptides remained conserved during the evolution, and gene duplications might help to adapt and enrich specific functions like reproduction, nutrient metabolism, and immune response. Further, the nonsynonymous mutations identified potentially affect these functions in buffalo.</abstract><cop>New York</cop><pub>Hindawi</pub><doi>10.1155/2022/1581714</doi><tpages>11</tpages><orcidid>https://orcid.org/0000-0002-8781-0510</orcidid><orcidid>https://orcid.org/0000-0001-8670-3011</orcidid><orcidid>https://orcid.org/0000-0001-7938-5051</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | Amino acids Binding sites Bos taurus Bubalus bubalis Buffalo Cattle Chromosomes Comparative analysis Gene duplication Genes Genetic aspects Genetic research Genomes Genomics Identification and classification Immune response Immune system INSL3 gene Insulin Metabolism Molecular evolution Molecular weight Mutation Nature conservation Nutrients Peptides Phylogenetics Physicochemical properties Proteins Proteomics Relaxin Reproduction Reproduction (copying) Sheep Software Water buffalo |
| title | Comparative Genomic Characterization of Relaxin Peptide Family in Cattle and Buffalo |
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