{"doi":"10.1073/pnas.88.15.6677","title":"Molecular cloning of a membrane-associated human FK506- and rapamycin-binding protein, FKBP-13.","abstract":"<jats:p>The 12-kDa FK506-binding protein (FKBP-12) is a cytosolic receptor for the immunosuppressants FK506 and rapamycin. Here we report the molecular cloning and subcellular localization of a 13-kDa FKBP (FKBP-13), which has a 21-amino acid signal peptide and appears to be membrane-associated. Although no internal hydrophobic region, and thus no transmembrane domain, is apparent within the 120 amino acids of mature FKBP-13, a potential endoplasmic reticulum retention sequence (Arg-Thr-Glu-Leu) is found at its C terminus. FKBP-13 has 51% nucleotide sequence identity and 43% amino acid sequence identity to FKBP-12; the N-terminal sequences are divergent, but the 92-amino acid C-terminal sequence of FKBP-13 has 46 identical and 20 related residues when compared with FKBP-12. The conserved residues that comprise the drug binding site and rotamase active site of FKBP-12 are completely conserved in FKBP-13. Therefore, the three-dimensional structures of FKBP-12 and the FKBP-12/FK506 complex are likely to be excellent models of the corresponding FKBP-13 structure.</jats:p>","journal":"Proceedings of the National Academy of Sciences","year":1991,"id":666569,"datarank":0.7738582948821795,"base_score":5.159055299214529,"endowment":5.159055299214529,"self_citation_contribution":0.7738582948821795,"citation_network_contribution":0.0,"self_endowment_contribution":0.7738582948821795,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":173,"citer_count":0,"citers_with_citation_signal":0,"citers_with_endowment":0,"datacite_reuse_total":0,"is_dataset":false,"is_dataset_confidence":null,"is_data_producer":false,"deposit_databanks":null,"is_oa":false,"file_count":0,"downloads":0,"has_version_chain":false,"published_date":null,"fair_score":null,"fair_percentile":null,"algorithm_id":"datarank_citation_only_1hop_v6","ranking_scope":"data_only","authors":[{"id":1740726,"name":"M W Albers","orcid":null,"position":1,"is_corresponding":false},{"id":1740727,"name":"W S Lane","orcid":null,"position":2,"is_corresponding":false},{"id":1740728,"name":"B E Bierer","orcid":null,"position":3,"is_corresponding":false},{"id":1740729,"name":"S L Schreiber","orcid":null,"position":4,"is_corresponding":false},{"id":1619279,"name":"S J Burakoff","orcid":null,"position":5,"is_corresponding":false},{"id":1740725,"name":"Y J Jin","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"Molecular cloning of a membrane-associated human FK506- and rapamycin-binding protein, FKBP-13.","abstract":"<jats:p>The 12-kDa FK506-binding protein (FKBP-12) is a cytosolic receptor for the immunosuppressants FK506 and rapamycin. Here we report the molecular cloning and subcellular localization of a 13-kDa FKBP (FKBP-13), which has a 21-amino acid signal peptide and appears to be membrane-associated. Although no internal hydrophobic region, and thus no transmembrane domain, is apparent within the 120 amino acids of mature FKBP-13, a potential endoplasmic reticulum retention sequence (Arg-Thr-Glu-Leu) is found at its C terminus. FKBP-13 has 51% nucleotide sequence identity and 43% amino acid sequence identity to FKBP-12; the N-terminal sequences are divergent, but the 92-amino acid C-terminal sequence of FKBP-13 has 46 identical and 20 related residues when compared with FKBP-12. The conserved residues that comprise the drug binding site and rotamase active site of FKBP-12 are completely conserved in FKBP-13. Therefore, the three-dimensional structures of FKBP-12 and the FKBP-12/FK506 complex are likely to be excellent models of the corresponding FKBP-13 structure.</jats:p>","is_dataset_classified":null,"base_score":0.0,"endowment":0.0,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"1713687","pmcid":"PMC52151","openalex_id":null,"authors":[],"funders":[{"funder_name":"NIGMS NIH HHS","grant_id":"GM38627","title":null},{"funder_name":"NCI NIH HHS","grant_id":"P01CA39542","title":null}],"total_grants":2,"fwci":null,"citation_percentile":null,"influential_citations":0,"citation_trend":[],"oa_status":"green","license":null,"oa_locations":[{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/52151","host_type":"repository"},{"url":"https://pnas.org/doi/pdf/10.1073/pnas.88.15.6677","host_type":"publisher"}],"fields_of_study":[],"mesh_terms":["Cell Line","Humans","Polyenes","Sirolimus","Tacrolimus","Tacrolimus Binding Proteins","Carrier Proteins","RNA, Messenger","Immunosuppressive Agents","Anti-Bacterial Agents","Antifungal Agents","Blotting, Northern","Cloning, Molecular","Polymerase Chain Reaction","Amino Acid Sequence","Base Sequence","Protein Conformation","Sequence Homology, Nucleic Acid","Models, Molecular","Molecular Sequence Data"],"keywords":[],"sdg_mappings":[],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-08-13T14:51:57.431326Z","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,"fair_f":null,"fair_a":null,"fair_i":null,"fair_r":null,"fair_zscore":null,"fair_rationale":null,"fair_model":null,"fair_agent_version":null,"fair_fulltext_source":null,"fair_has_llm":null,"fair_computed_at":null,"clinical_trials":[],"software_tools":[],"db_accessions":[],"linked_datasets":[],"topics":[]}