{"doi":"10.1111/j.1432-1033.1988.tb14463.x","title":"Isolation and characterization of the bovine <i>k</i>‐casein gene","abstract":"<jats:p>\n<jats:list list-type=\"explicit-label\">\n<jats:list-item><jats:p>The bovine <jats:italic>k</jats:italic>‐casein gene has been isolated as a series of overlapping λ clones and shown to consist of five exons distributed over a total length of approximately 13 kb. Most of the mature protein‐coding sequence is contained in a single large exon.</jats:p></jats:list-item>\n<jats:list-item><jats:p>Approximately 65% of the gene has been sequenced together with portions of the 5′‐ and 3′‐flanking sequences. The immediate 5′‐flanking sequence contains several motifs which are characteristic of upstream regions including a TATA box, a CAAT box, a sequence similar to that recognized by transcription factor AP‐1 and a purine‐rich sequence resembling that found upstream in all other lactoprotein genes. Other possible regulatory sequences are found upstream of exon 4.</jats:p></jats:list-item>\n<jats:list-item><jats:p>The organization of the <jats:italic>k</jats:italic>‐casein gene, together with its upstream sequence, confirms previous conclusions that it is unrelated to the calcium‐sensitive‐casein gene familiy to which it is linked. Evidence is presented which supports a previous suggestion that <jats:italic>k</jats:italic>‐casein and the fibrinogens are evolutionarily related.</jats:p></jats:list-item>\n<jats:list-item><jats:p>Intron sequences contain several examples of the A family of the artiodactyl Alu‐like repeated sequences, together with a single example of a C‐family sequence. The remainders of the introns of the <jats:italic>k</jats:italic>‐casein gene, compared with the repeat elements and exons, are A + T‐rich.</jats:p></jats:list-item>\n<jats:list-item><jats:p>Among the Δ clones isolated, representatives were found of the A and B genetic variants which can be distinguished by restriction‐enzyme analysis. Several other examples of polymorphisms in the non‐coding region were found.</jats:p></jats:list-item>\n</jats:list>\n</jats:p>","journal":"European Journal of Biochemistry","year":1988,"id":30972,"datarank":13.829148898530423,"base_score":5.081404364984463,"endowment":5.081404364984463,"self_citation_contribution":0.7622106547476696,"citation_network_contribution":13.066938243782754,"self_endowment_contribution":0.7622106547476696,"citer_contribution":13.066938243782754,"corpus_percentile":null,"corpus_rank":null,"citation_count":160,"citer_count":160,"citers_with_citation_signal":153,"citers_with_endowment":153,"datacite_reuse_total":0,"is_dataset":false,"is_dataset_confidence":null,"is_oa":false,"file_count":0,"downloads":0,"has_version_chain":false,"published_date":null,"algorithm_id":"datarank_citation_only_1hop_v6","ranking_scope":"data_only","authors":[{"id":167042,"name":"A. Francis STEWART","orcid":null,"position":1,"is_corresponding":false},{"id":167043,"name":"Antony G. MACKINLAY","orcid":null,"position":2,"is_corresponding":false},{"id":167044,"name":"Tatiana V. KAPELINSKAYA","orcid":null,"position":3,"is_corresponding":false},{"id":167045,"name":"Tatiana M. TKACH","orcid":null,"position":4,"is_corresponding":false},{"id":167046,"name":"Stanislav I. GORODETSKY","orcid":null,"position":5,"is_corresponding":false},{"id":167041,"name":"Leeson J. ALEXANDER","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"base_score":5.081404364984463,"endowment":5.081404364984463,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"3208764","pmcid":null,"openalex_id":"https://openalex.org/W1966961397","authors":[],"funders":[],"total_grants":0,"fwci":1.7356,"citation_percentile":0.84582788,"influential_citations":4,"citation_trend":[{"year":2012,"count":7},{"year":2013,"count":1},{"year":2014,"count":8},{"year":2015,"count":3},{"year":2016,"count":2},{"year":2017,"count":4},{"year":2020,"count":4},{"year":2021,"count":2},{"year":2022,"count":3},{"year":2023,"count":2},{"year":2024,"count":3},{"year":2025,"count":1}],"oa_status":"closed","license":"http://onlinelibrary.wiley.com/termsAndConditions#vor","oa_locations":[{"url":"https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1111%2Fj.1432-1033.1988.tb14463.x","host_type":"publisher"},{"url":"https://febs.onlinelibrary.wiley.com/doi/pdf/10.1111/j.1432-1033.1988.tb14463.x","host_type":"publisher"},{"url":"https://doi.org/10.1111/j.1432-1033.1988.tb14463.x","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/3208764","host_type":"repository"}],"fields_of_study":["Protein Hydrolysis and Bioactive Peptides","Animal Genetics and Reproduction","Digestive system and related health","Biology","Alleles","Amino Acid Sequence","Animals","Base Sequence","Caseins","Cattle","Cloning, Molecular","Exons","Genes","Molecular Sequence Data","Polymorphism, Genetic","Restriction Mapping"],"mesh_terms":["Alleles","Amino Acid Sequence","Animals","Base Sequence","Caseins","Cattle","Cloning, Molecular","Exons","Genes","Molecular Sequence Data","Polymorphism, Genetic","Restriction Mapping"],"keywords":["Exon","Gene","Intron","Genetics","Biology","Coding region","TATA box","Consensus sequence","Regulatory sequence","Nucleic acid sequence","Sequence (biology)","CAAT box","Sequence analysis","Molecular biology","Promoter","Peptide sequence","Regulation of gene expression","Gene expression"],"sdg_mappings":[],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-06-09T06:06:12.021762Z","pmid":null,"pmcid":null,"fwci":null,"citation_percentile":null,"influential_citations":0,"oa_status":null,"license":null,"views":0,"total_file_size_bytes":0,"version_count":0,"clinical_trials":[],"software_tools":[],"db_accessions":[],"linked_datasets":[],"topics":[]}