ID IBP5_RAT Reviewed; 271 AA. AC P24594; DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-1992, sequence version 1. DT 24-JAN-2024, entry version 181. DE RecName: Full=Insulin-like growth factor-binding protein 5; DE Short=IBP-5; DE Short=IGF-binding protein 5; DE Short=IGFBP-5; DE Flags: Precursor; GN Name=Igfbp5; Synonyms=Igfbp-5; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 20-53. RC TISSUE=Ovary; RX PubMed=1709938; DOI=10.1016/s0021-9258(18)99272-0; RA Shimasaki S., Shimonaka M., Zhang H.-P., Ling N.; RT "Identification of five different insulin-like growth factor binding RT proteins (IGFBPs) from adult rat serum and molecular cloning of a novel RT IGFBP-5 in rat and human."; RL J. Biol. Chem. 266:10646-10653(1991). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=Sprague-Dawley; RX PubMed=7679898; DOI=10.1006/bbrc.1993.1154; RA Zhu X., Ling N., Shimasaki S.; RT "Cloning of the rat insulin-like growth factor binding protein-5 gene and RT DNA sequence analysis of its promoter region."; RL Biochem. Biophys. Res. Commun. 190:1045-1052(1993). CC -!- FUNCTION: IGF-binding proteins prolong the half-life of the IGFs and CC have been shown to either inhibit or stimulate the growth promoting CC effects of the IGFs on cell culture. They alter the interaction of IGFs CC with their cell surface receptors. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- TISSUE SPECIFICITY: Mostly in kidney. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M62781; AAA53533.1; -; mRNA. DR EMBL; L08275; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR PIR; JC1463; JC1463. DR RefSeq; NP_036949.1; NM_012817.1. DR AlphaFoldDB; P24594; -. DR SMR; P24594; -. DR MINT; P24594; -. DR STRING; 10116.ENSRNOP00000023530; -. DR MEROPS; I31.952; -. DR iPTMnet; P24594; -. DR PhosphoSitePlus; P24594; -. DR PaxDb; 10116-ENSRNOP00000023530; -. DR Ensembl; ENSRNOT00000023530.7; ENSRNOP00000023530.3; ENSRNOG00000017206.7. DR Ensembl; ENSRNOT00055016923; ENSRNOP00055013621; ENSRNOG00055010024. DR Ensembl; ENSRNOT00060011558; ENSRNOP00060008678; ENSRNOG00060007038. DR Ensembl; ENSRNOT00065013665; ENSRNOP00065010142; ENSRNOG00065008601. DR GeneID; 25285; -. DR KEGG; rno:25285; -. DR UCSC; RGD:2876; rat. DR AGR; RGD:2876; -. DR CTD; 3488; -. DR RGD; 2876; Igfbp5. DR eggNOG; ENOG502QUPK; Eukaryota. DR GeneTree; ENSGT00940000155890; -. DR InParanoid; P24594; -. DR OMA; YTERCAL; -. DR OrthoDB; 5394492at2759; -. DR PhylomeDB; P24594; -. DR TreeFam; TF331211; -. DR Reactome; R-RNO-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs). DR Reactome; R-RNO-8957275; Post-translational protein phosphorylation. DR PRO; PR:P24594; -. DR Proteomes; UP000002494; Chromosome 9. DR Bgee; ENSRNOG00000017206; Expressed in esophagus and 19 other cell types or tissues. DR ExpressionAtlas; P24594; baseline and differential. DR GO; GO:0005615; C:extracellular space; IBA:GO_Central. DR GO; GO:0042567; C:insulin-like growth factor ternary complex; ISO:RGD. DR GO; GO:0001968; F:fibronectin binding; ISO:RGD. DR GO; GO:0005520; F:insulin-like growth factor binding; IDA:RGD. DR GO; GO:0031994; F:insulin-like growth factor I binding; ISO:RGD. DR GO; GO:0031995; F:insulin-like growth factor II binding; IBA:GO_Central. DR GO; GO:0071320; P:cellular response to cAMP; ISO:RGD. DR GO; GO:0071407; P:cellular response to organic cyclic compound; ISO:RGD. DR GO; GO:0007565; P:female pregnancy; ISO:RGD. DR GO; GO:0042593; P:glucose homeostasis; ISO:RGD. DR GO; GO:0031069; P:hair follicle morphogenesis; ISO:RGD. DR GO; GO:0048009; P:insulin-like growth factor receptor signaling pathway; ISO:RGD. DR GO; GO:0035556; P:intracellular signal transduction; IEP:RGD. DR GO; GO:0048286; P:lung alveolus development; ISO:RGD. DR GO; GO:0060056; P:mammary gland involution; ISO:RGD. DR GO; GO:0030336; P:negative regulation of cell migration; ISO:RGD. DR GO; GO:0045926; P:negative regulation of growth; ISO:RGD. DR GO; GO:0043569; P:negative regulation of insulin-like growth factor receptor signaling pathway; ISO:RGD. DR GO; GO:1901862; P:negative regulation of muscle tissue development; ISO:RGD. DR GO; GO:0045668; P:negative regulation of osteoblast differentiation; ISO:RGD. DR GO; GO:1904205; P:negative regulation of skeletal muscle hypertrophy; ISO:RGD. DR GO; GO:0014912; P:negative regulation of smooth muscle cell migration; ISO:RGD. DR GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; ISO:RGD. DR GO; GO:0017148; P:negative regulation of translation; ISO:RGD. DR GO; GO:0001649; P:osteoblast differentiation; ISO:RGD. DR GO; GO:0043568; P:positive regulation of insulin-like growth factor receptor signaling pathway; ISO:RGD. DR GO; GO:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; ISO:RGD. DR GO; GO:1904754; P:positive regulation of vascular associated smooth muscle cell migration; ISO:RGD. DR GO; GO:1904707; P:positive regulation of vascular associated smooth muscle cell proliferation; ISO:RGD. DR GO; GO:0001558; P:regulation of cell growth; ISO:RGD. DR GO; GO:0040008; P:regulation of growth; ISO:RGD. DR GO; GO:0043567; P:regulation of insulin-like growth factor receptor signaling pathway; IBA:GO_Central. DR GO; GO:0060416; P:response to growth hormone; ISS:AgBase. DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD. DR GO; GO:0051146; P:striated muscle cell differentiation; ISO:RGD. DR GO; GO:0044342; P:type B pancreatic cell proliferation; ISO:RGD. DR CDD; cd00191; TY; 1. DR Gene3D; 4.10.40.20; -; 1. DR Gene3D; 4.10.800.10; Thyroglobulin type-1; 1. DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf. DR InterPro; IPR012213; IGFBP-5. DR InterPro; IPR000867; IGFBP-like. DR InterPro; IPR022321; IGFBP_1-6_chordata. DR InterPro; IPR017891; Insulin_GF-bd_Cys-rich_CS. DR InterPro; IPR000716; Thyroglobulin_1. DR InterPro; IPR036857; Thyroglobulin_1_sf. DR PANTHER; PTHR11551; INSULIN-LIKE GROWTH FACTOR BINDING PROTEIN; 1. DR PANTHER; PTHR11551:SF4; INSULIN-LIKE GROWTH FACTOR-BINDING PROTEIN 5; 1. DR Pfam; PF00219; IGFBP; 1. DR Pfam; PF00086; Thyroglobulin_1; 1. DR PRINTS; PR01976; IGFBPFAMILY. DR PRINTS; PR01981; IGFBPFAMILY5. DR SMART; SM00121; IB; 1. DR SMART; SM00211; TY; 1. DR SUPFAM; SSF57184; Growth factor receptor domain; 1. DR SUPFAM; SSF57610; Thyroglobulin type-1 domain; 1. DR PROSITE; PS00222; IGFBP_N_1; 1. DR PROSITE; PS51323; IGFBP_N_2; 1. DR PROSITE; PS00484; THYROGLOBULIN_1_1; 1. DR PROSITE; PS51162; THYROGLOBULIN_1_2; 1. DR Genevisible; P24594; RN. PE 1: Evidence at protein level; KW Direct protein sequencing; Disulfide bond; Growth factor binding; KW Phosphoprotein; Reference proteome; Secreted; Signal. FT SIGNAL 1..19 FT /evidence="ECO:0000255" FT CHAIN 20..271 FT /note="Insulin-like growth factor-binding protein 5" FT /id="PRO_0000014388" FT DOMAIN 22..102 FT /note="IGFBP N-terminal" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00653" FT DOMAIN 188..262 FT /note="Thyroglobulin type-1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500" FT REGION 109..129 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 109..125 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 115 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P24593" FT DISULFID 26..52 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00653" FT DISULFID 29..54 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00653" FT DISULFID 37..55 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00653" FT DISULFID 44..58 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00653" FT DISULFID 66..79 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00653" FT DISULFID 73..99 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00653" FT DISULFID 191..218 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500" FT DISULFID 229..240 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500" FT DISULFID 242..262 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500" SQ SEQUENCE 271 AA; 30298 MW; 545B4C48F9BB5493 CRC64; MVISVVLLLL AACAVPAQGL GSFVHCEPCD EKALSMCPPS PLGCELVKEP GCGCCMTCAL AEGQSCGVYT ERCAQGLRCL PRQDEEKPLH ALLHGRGVCL NEKSYGEQTK IERDSREHEE PTTSEMAEET YSPKVFRPKH TRISELKAEA VKKDRRKKLT QSKFVGGAEN TAHPRVIPAP EMRQESDQGP CRRHMEASLQ EFKASPRMVP RAVYLPNCDR KGFYKRKQCK PSRGRKRGIC WCVDKYGMKL PGMEYVDGDF QCHAFDSSNV E //