ID IBP5_HUMAN Reviewed; 272 AA. AC P24593; Q5U0A3; DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-1992, sequence version 1. DT 05-FEB-2025, entry version 232. 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=IBP5; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Osteosarcoma; RX PubMed=1850258; DOI=10.1016/0006-291x(91)90912-q; RA Kiefer M.C., Ioh R.S., Bauer D.M., Zapf J.; RT "Molecular cloning of a new human insulin-like growth factor binding RT protein."; RL Biochem. Biophys. Res. Commun. 176:219-225(1991). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Placenta; 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 [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=7511611; DOI=10.1016/s0021-9258(17)34142-x; RA Allander S.V., Larsson C., Ehrenborg E., Suwanichkul A., Weber G., RA Morris S.L., Bajalica S., Kiefer M.C., Luthman H., Powell D.R.; RT "Characterization of the chromosomal gene and promoter for human insulin- RT like growth factor binding protein-5."; RL J. Biol. Chem. 269:10891-10898(1994). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RA Yu W., Gibbs R.A.; RL Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT TRP-138. RG NIEHS SNPs program; RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [8] RP PROTEIN SEQUENCE OF 24-43. RX PubMed=1850257; DOI=10.1016/0006-291x(91)90911-p; RA Andress D.L., Birnbaum R.S.; RT "A novel human insulin-like growth factor binding protein secreted by RT osteoblast-like cells."; RL Biochem. Biophys. Res. Commun. 176:213-218(1991). RN [9] RP FUNCTION, AND INTERACTION WITH IGF1. RX PubMed=7683690; DOI=10.1083/jcb.121.3.679; RA Jones J.I., Gockerman A., Busby W.H. Jr., Camacho-Hubner C., Clemmons D.R.; RT "Extracellular matrix contains insulin-like growth factor binding protein- RT 5: potentiation of the effects of IGF-I."; RL J. Cell Biol. 121:679-687(1993). RN [10] RP PROTEIN SEQUENCE OF 141-178 AND 209-223, AND GLYCOSYLATION AT THR-172. RC TISSUE=Plasma; RX PubMed=9883900; DOI=10.1016/s0014-5793(98)01497-5; RA Standker L., Wobst P., Mark S., Forssmann W.-G.; RT "Isolation and characterization of circulating 13-kDa C-terminal fragments RT of human insulin-like growth factor binding protein-5."; RL FEBS Lett. 441:281-286(1998). RN [11] RP FUNCTION, CLEAVAGE BY C1S, AND SUBCELLULAR LOCATION. RX PubMed=18930415; DOI=10.1016/j.joca.2008.08.004; RA Busby W.H. Jr., Yocum S.A., Rowland M., Kellner D., Lazerwith S., RA Sverdrup F., Yates M., Radabaugh M., Clemmons D.R.; RT "Complement 1s is the serine protease that cleaves IGFBP-5 in human RT osteoarthritic joint fluid."; RL Osteoarthritis Cartilage 17:547-555(2009). RN [12] RP FUNCTION, INTERACTION WITH CAV1, AND SUBCELLULAR LOCATION. RX PubMed=20345844; DOI=10.1111/j.1582-4934.2010.01063.x; RA Yamaguchi Y., Yasuoka H., Stolz D.B., Feghali-Bostwick C.A.; RT "Decreased caveolin-1 levels contribute to fibrosis and deposition of RT extracellular IGFBP-5."; RL J. Cell. Mol. Med. 15:957-969(2011). RN [13] RP DISULFIDE BONDS, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=22117064; DOI=10.1074/jbc.m111.285528; RA Nili M., Mukherjee A., Shinde U., David L., Rotwein P.; RT "Defining the disulfide bonds of insulin-like growth factor-binding RT protein-5 by tandem mass spectrometry with electron transfer dissociation RT and collision-induced dissociation."; RL J. Biol. Chem. 287:1510-1519(2012). RN [14] RP PHOSPHORYLATION AT SER-116. RX PubMed=26091039; DOI=10.1016/j.cell.2015.05.028; RA Tagliabracci V.S., Wiley S.E., Guo X., Kinch L.N., Durrant E., Wen J., RA Xiao J., Cui J., Nguyen K.B., Engel J.L., Coon J.J., Grishin N., RA Pinna L.A., Pagliarini D.J., Dixon J.E.; RT "A single kinase generates the majority of the secreted phosphoproteome."; RL Cell 161:1619-1632(2015). RN [15] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH NUCLEOLIN/NCL. RX PubMed=26103640; DOI=10.1371/journal.pone.0130546; RA Su Y., Nishimoto T., Feghali-Bostwick C.; RT "IGFBP-5 Promotes Fibrosis Independently of Its Translocation to the RT Nucleus and Its Interaction with Nucleolin and IGF."; RL PLoS ONE 10:e0130546-e0130546(2015). RN [16] RP FUNCTION, AND INTERACTION WITH ROR1. RX PubMed=36949068; DOI=10.1038/s41467-023-37306-1; RA Lin W., Niu R., Park S.M., Zou Y., Kim S.S., Xia X., Xing S., Yang Q., RA Sun X., Yuan Z., Zhou S., Zhang D., Kwon H.J., Park S., Il Kim C., Koo H., RA Liu Y., Wu H., Zheng M., Yoo H., Shi B., Park J.B., Yin J.; RT "IGFBP5 is an ROR1 ligand promoting glioblastoma invasion via ROR1/HER2- RT CREB signaling axis."; RL Nat. Commun. 14:1578-1578(2023). RN [17] RP STRUCTURE BY NMR OF 60-106. RX PubMed=9822601; DOI=10.1093/emboj/17.22.6558; RA Kalus W., Zweckstetter M., Renner C., Sanchez Y., Georgescu J., Grol M., RA Demuth D., Schumacher R., Dony C., Lang K., Holak T.A.; RT "Structure of the IGF-binding domain of the insulin-like growth factor- RT binding protein-5 (IGFBP-5): implications for IGF and IGF-I receptor RT interactions."; RL EMBO J. 17:6558-6572(1998). CC -!- FUNCTION: Multifunctional protein that plays a critical role in CC regulating the availability of IGFs to their receptors and thereby CC regulates IGF-mediated cellular processes including proliferation, CC differentiation, and apoptosis in a cell-type specific manner CC (PubMed:18930415, PubMed:7683690). Increases the cell proliferation of CC osteoblasts, intestinal smooth muscle cells and neuroblastoma cells. CC Enhances adhesion and survival of epithelial cells but decreases CC adhesion of mesenchymal cells (By similarity). Once secreted, acts as a CC major mediator of mTORC1-dependent feedback inhibition of IGF1 CC signaling (By similarity). Plays also a role in the induction of CC extracellular matrix (ECM) production and deposition independently of CC its nuclear translocation and binding to IGFs (PubMed:20345844, CC PubMed:26103640). Acts itself as a growth factor that can act CC independently of IGFs to regulate bone formation. Acts as a ligand for CC the ROR1 receptor which triggers formation of ROR1/HER2 heterodimer to CC enhance CREB oncogenic signaling (PubMed:36949068). CC {ECO:0000250|UniProtKB:Q07079, ECO:0000269|PubMed:18930415, CC ECO:0000269|PubMed:20345844, ECO:0000269|PubMed:26103640, CC ECO:0000269|PubMed:36949068, ECO:0000269|PubMed:7683690}. CC -!- SUBUNIT: Interacts with IGF1; this interaction enhances the growth CC stimulatory effects of IGF1 on fibroblasts (PubMed:7683690). Interacts CC with CAV1; this interaction allows trafficking of IGFBP5 from the CC plasma membrane to the nucleus (PubMed:20345844). Interacts with NCL; CC this interaction is necessary for IGFBP5 localization to the nucleus CC (PubMed:26103640). {ECO:0000269|PubMed:20345844, CC ECO:0000269|PubMed:26103640, ECO:0000269|PubMed:7683690}. CC -!- INTERACTION: CC P24593; Q8TB40: ABHD4; NbExp=3; IntAct=EBI-720480, EBI-7131019; CC P24593; Q8IVF2-3: AHNAK2; NbExp=3; IntAct=EBI-720480, EBI-12078468; CC P24593; Q86WK6: AMIGO1; NbExp=3; IntAct=EBI-720480, EBI-19125216; CC P24593; Q68DC2: ANKS6; NbExp=3; IntAct=EBI-720480, EBI-7054139; CC P24593; Q96BI3: APH1A; NbExp=3; IntAct=EBI-720480, EBI-2606935; CC P24593; P41181: AQP2; NbExp=3; IntAct=EBI-720480, EBI-12701138; CC P24593; Q13520: AQP6; NbExp=3; IntAct=EBI-720480, EBI-13059134; CC P24593; O43315: AQP9; NbExp=3; IntAct=EBI-720480, EBI-17444777; CC P24593; P07306: ASGR1; NbExp=3; IntAct=EBI-720480, EBI-1172335; CC P24593; Q8WZ55: BSND; NbExp=3; IntAct=EBI-720480, EBI-7996695; CC P24593; P19397: CD53; NbExp=3; IntAct=EBI-720480, EBI-6657396; CC P24593; Q9HA82: CERS4; NbExp=3; IntAct=EBI-720480, EBI-2622997; CC P24593; Q9H9P2: CHODL; NbExp=3; IntAct=EBI-720480, EBI-17447707; CC P24593; P57739: CLDN2; NbExp=3; IntAct=EBI-720480, EBI-751440; CC P24593; P56880: CLDN20; NbExp=3; IntAct=EBI-720480, EBI-23801559; CC P24593; P56747: CLDN6; NbExp=3; IntAct=EBI-720480, EBI-12955011; CC P24593; O95471: CLDN7; NbExp=3; IntAct=EBI-720480, EBI-740744; CC P24593; O95484: CLDN9; NbExp=3; IntAct=EBI-720480, EBI-18341636; CC P24593; Q6ZS10: CLEC17A; NbExp=4; IntAct=EBI-720480, EBI-11977093; CC P24593; O43889-2: CREB3; NbExp=4; IntAct=EBI-720480, EBI-625022; CC P24593; P25024: CXCR1; NbExp=3; IntAct=EBI-720480, EBI-3905522; CC P24593; Q9NYP7: ELOVL5; NbExp=3; IntAct=EBI-720480, EBI-11037623; CC P24593; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-720480, EBI-781551; CC P24593; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-720480, EBI-18304435; CC P24593; Q96P31-6: FCRL3; NbExp=3; IntAct=EBI-720480, EBI-17443171; CC P24593; Q8TBE3: FNDC9; NbExp=3; IntAct=EBI-720480, EBI-12142257; CC P24593; P36382: GJA5; NbExp=3; IntAct=EBI-720480, EBI-750433; CC P24593; P48165: GJA8; NbExp=3; IntAct=EBI-720480, EBI-17458373; CC P24593; O75712: GJB3; NbExp=3; IntAct=EBI-720480, EBI-3908586; CC P24593; O95377: GJB5; NbExp=3; IntAct=EBI-720480, EBI-3909454; CC P24593; Q8NBJ4: GOLM1; NbExp=3; IntAct=EBI-720480, EBI-712073; CC P24593; Q8TDV0: GPR151; NbExp=3; IntAct=EBI-720480, EBI-11955647; CC P24593; Q8TDT2: GPR152; NbExp=3; IntAct=EBI-720480, EBI-13345167; CC P24593; O60883: GPR37L1; NbExp=3; IntAct=EBI-720480, EBI-2927498; CC P24593; O15529: GPR42; NbExp=3; IntAct=EBI-720480, EBI-18076404; CC P24593; Q9NZD1: GPRC5D; NbExp=3; IntAct=EBI-720480, EBI-13067820; CC P24593; Q8TED1: GPX8; NbExp=3; IntAct=EBI-720480, EBI-11721746; CC P24593; Q7Z5P4: HSD17B13; NbExp=3; IntAct=EBI-720480, EBI-18053395; CC P24593; O95279: KCNK5; NbExp=3; IntAct=EBI-720480, EBI-3934936; CC P24593; Q8IYS2: KIAA2013; NbExp=3; IntAct=EBI-720480, EBI-2866116; CC P24593; Q86VI4: LAPTM4B; NbExp=3; IntAct=EBI-720480, EBI-3267258; CC P24593; Q6UX15-2: LAYN; NbExp=3; IntAct=EBI-720480, EBI-19944128; CC P24593; Q5T700: LDLRAD1; NbExp=3; IntAct=EBI-720480, EBI-10173166; CC P24593; Q86WI0: LHFPL1; NbExp=3; IntAct=EBI-720480, EBI-18268016; CC P24593; Q9GZY8-5: MFF; NbExp=3; IntAct=EBI-720480, EBI-11956541; CC P24593; Q6N075: MFSD5; NbExp=3; IntAct=EBI-720480, EBI-3920969; CC P24593; Q9Y676: MRPS18B; NbExp=3; IntAct=EBI-720480, EBI-750085; CC P24593; Q96HJ5: MS4A3; NbExp=3; IntAct=EBI-720480, EBI-12806656; CC P24593; Q9GZW8: MS4A7; NbExp=3; IntAct=EBI-720480, EBI-721391; CC P24593; Q6IBW4-4: NCAPH2; NbExp=3; IntAct=EBI-720480, EBI-10247000; CC P24593; Q13113: PDZK1IP1; NbExp=3; IntAct=EBI-720480, EBI-716063; CC P24593; Q8NFJ6: PROKR2; NbExp=3; IntAct=EBI-720480, EBI-12902928; CC P24593; Q9UBD6: RHCG; NbExp=3; IntAct=EBI-720480, EBI-15853497; CC P24593; Q3KNW5: SLC10A6; NbExp=3; IntAct=EBI-720480, EBI-18159983; CC P24593; Q9UKG4: SLC13A4; NbExp=3; IntAct=EBI-720480, EBI-12808018; CC P24593; Q9H2H9: SLC38A1; NbExp=4; IntAct=EBI-720480, EBI-9978441; CC P24593; Q96JW4: SLC41A2; NbExp=3; IntAct=EBI-720480, EBI-10290130; CC P24593; Q96GZ6: SLC41A3; NbExp=3; IntAct=EBI-720480, EBI-7225508; CC P24593; Q9NPE6: SPAG4; NbExp=3; IntAct=EBI-720480, EBI-10819434; CC P24593; Q8N205-2: SYNE4; NbExp=3; IntAct=EBI-720480, EBI-12099160; CC P24593; Q8WY91: THAP4; NbExp=3; IntAct=EBI-720480, EBI-726691; CC P24593; Q96MV1: TLCD4; NbExp=3; IntAct=EBI-720480, EBI-12947623; CC P24593; Q96A25: TMEM106A; NbExp=3; IntAct=EBI-720480, EBI-3915978; CC P24593; Q9BVX2: TMEM106C; NbExp=3; IntAct=EBI-720480, EBI-2821497; CC P24593; Q7Z7N9: TMEM179B; NbExp=3; IntAct=EBI-720480, EBI-11724423; CC P24593; Q96Q45-2: TMEM237; NbExp=5; IntAct=EBI-720480, EBI-10982110; CC P24593; Q9NWC5: TMEM45A; NbExp=3; IntAct=EBI-720480, EBI-10823938; CC P24593; Q4KMG9: TMEM52B; NbExp=3; IntAct=EBI-720480, EBI-18178701; CC P24593; O15393-2: TMPRSS2; NbExp=3; IntAct=EBI-720480, EBI-12345267; CC P24593; Q9Y320: TMX2; NbExp=3; IntAct=EBI-720480, EBI-6447886; CC P24593; O95859: TSPAN12; NbExp=3; IntAct=EBI-720480, EBI-2466403; CC P24593; Q5TGU0: TSPO2; NbExp=3; IntAct=EBI-720480, EBI-12195249; CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18930415, CC ECO:0000269|PubMed:20345844}. Cytoplasm {ECO:0000269|PubMed:20345844, CC ECO:0000269|PubMed:26103640}. Nucleus {ECO:0000269|PubMed:20345844, CC ECO:0000269|PubMed:26103640}. CC -!- TISSUE SPECIFICITY: Osteosarcoma, and at lower levels in liver, kidney CC and brain. CC -!- PTM: Cleaved by C1S in extracellular space. CC {ECO:0000269|PubMed:18930415}. 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; M65062; AAD04730.1; -; mRNA. DR EMBL; M62782; AAA53505.1; -; mRNA. DR EMBL; L27559; AAA72051.1; -; Genomic_DNA. DR EMBL; L27556; AAA72051.1; JOINED; Genomic_DNA. DR EMBL; L27557; AAA72051.1; JOINED; Genomic_DNA. DR EMBL; L27558; AAA72051.1; JOINED; Genomic_DNA. DR EMBL; AF055033; AAC09368.1; -; mRNA. DR EMBL; BT019706; AAV38512.1; -; mRNA. DR EMBL; BT019707; AAV38513.1; -; mRNA. DR EMBL; AY534685; AAS16353.1; -; Genomic_DNA. DR EMBL; BC011453; AAH11453.1; -; mRNA. DR CCDS; CCDS2405.1; -. DR PIR; A53748; A53748. DR RefSeq; NP_000590.1; NM_000599.3. DR PDB; 1BOE; NMR; -; A=60-106. DR PDB; 1H59; X-ray; 2.10 A; B=60-112. DR PDB; 7UFG; EM; 3.28 A; C/D=21-272. DR PDBsum; 1BOE; -. DR PDBsum; 1H59; -. DR PDBsum; 7UFG; -. DR AlphaFoldDB; P24593; -. DR EMDB; EMD-26475; -. DR SMR; P24593; -. DR BioGRID; 109709; 122. DR DIP; DIP-48433N; -. DR IntAct; P24593; 104. DR STRING; 9606.ENSP00000233813; -. DR BindingDB; P24593; -. DR ChEMBL; CHEMBL2665; -. DR DrugBank; DB01277; Mecasermin. DR MEROPS; I31.952; -. DR GlyCosmos; P24593; 2 sites, 1 glycan. DR GlyGen; P24593; 5 sites, 3 O-linked glycans (5 sites). DR iPTMnet; P24593; -. DR PhosphoSitePlus; P24593; -. DR BioMuta; IGFBP5; -. DR DMDM; 124069; -. DR MassIVE; P24593; -. DR PaxDb; 9606-ENSP00000233813; -. DR PeptideAtlas; P24593; -. DR ProteomicsDB; 54219; -. DR Pumba; P24593; -. DR Antibodypedia; 3978; 522 antibodies from 39 providers. DR DNASU; 3488; -. DR Ensembl; ENST00000233813.5; ENSP00000233813.4; ENSG00000115461.5. DR GeneID; 3488; -. DR KEGG; hsa:3488; -. DR MANE-Select; ENST00000233813.5; ENSP00000233813.4; NM_000599.4; NP_000590.1. DR UCSC; uc002vgj.5; human. DR AGR; HGNC:5474; -. DR CTD; 3488; -. DR DisGeNET; 3488; -. DR GeneCards; IGFBP5; -. DR HGNC; HGNC:5474; IGFBP5. DR HPA; ENSG00000115461; Tissue enhanced (cervix, ovary). DR MIM; 146734; gene. DR neXtProt; NX_P24593; -. DR OpenTargets; ENSG00000115461; -. DR PharmGKB; PA29707; -. DR VEuPathDB; HostDB:ENSG00000115461; -. DR eggNOG; ENOG502QUPK; Eukaryota. DR GeneTree; ENSGT00940000155890; -. DR HOGENOM; CLU_070833_1_1_1; -. DR InParanoid; P24593; -. DR OMA; YTERCAL; -. DR OrthoDB; 6068400at2759; -. DR PhylomeDB; P24593; -. DR TreeFam; TF331211; -. DR BioCyc; MetaCyc:ENSG00000115461-MONOMER; -. DR PathwayCommons; P24593; -. DR Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs). DR Reactome; R-HSA-8957275; Post-translational protein phosphorylation. DR SignaLink; P24593; -. DR SIGNOR; P24593; -. DR BioGRID-ORCS; 3488; 15 hits in 1155 CRISPR screens. DR ChiTaRS; IGFBP5; human. DR EvolutionaryTrace; P24593; -. DR GeneWiki; IGFBP5; -. DR GenomeRNAi; 3488; -. DR Pharos; P24593; Tchem. DR PRO; PR:P24593; -. DR Proteomes; UP000005640; Chromosome 2. DR RNAct; P24593; protein. DR Bgee; ENSG00000115461; Expressed in renal medulla and 212 other cell types or tissues. DR ExpressionAtlas; P24593; baseline and differential. DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0005615; C:extracellular space; IBA:GO_Central. DR GO; GO:0016942; C:insulin-like growth factor binding protein complex; IC:BHF-UCL. DR GO; GO:0042567; C:insulin-like growth factor ternary complex; IDA:BHF-UCL. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0001968; F:fibronectin binding; IBA:GO_Central. DR GO; GO:0031994; F:insulin-like growth factor I binding; IPI:BHF-UCL. DR GO; GO:0031995; F:insulin-like growth factor II binding; IBA:GO_Central. DR GO; GO:0048018; F:receptor ligand activity; IDA:UniProt. DR GO; GO:0008283; P:cell population proliferation; IDA:UniProt. DR GO; GO:0071320; P:cellular response to cAMP; IDA:UniProtKB. DR GO; GO:0071407; P:cellular response to organic cyclic compound; IDA:UniProtKB. DR GO; GO:0007565; P:female pregnancy; IEA:Ensembl. DR GO; GO:0042593; P:glucose homeostasis; IEA:Ensembl. DR GO; GO:0031069; P:hair follicle morphogenesis; IEA:Ensembl. DR GO; GO:0048009; P:insulin-like growth factor receptor signaling pathway; IEA:Ensembl. DR GO; GO:0035556; P:intracellular signal transduction; IEA:Ensembl. DR GO; GO:0048286; P:lung alveolus development; IEA:Ensembl. DR GO; GO:0060056; P:mammary gland involution; IEA:Ensembl. DR GO; GO:0030336; P:negative regulation of cell migration; IDA:BHF-UCL. DR GO; GO:0045926; P:negative regulation of growth; IEA:Ensembl. DR GO; GO:0043569; P:negative regulation of insulin-like growth factor receptor signaling pathway; IDA:BHF-UCL. DR GO; GO:1901862; P:negative regulation of muscle tissue development; IEA:Ensembl. DR GO; GO:0045668; P:negative regulation of osteoblast differentiation; IEA:Ensembl. DR GO; GO:1904205; P:negative regulation of skeletal muscle hypertrophy; IEA:Ensembl. DR GO; GO:0014912; P:negative regulation of smooth muscle cell migration; IDA:BHF-UCL. DR GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; IDA:BHF-UCL. DR GO; GO:0017148; P:negative regulation of translation; IDA:BHF-UCL. DR GO; GO:0001649; P:osteoblast differentiation; IEA:Ensembl. DR GO; GO:0043568; P:positive regulation of insulin-like growth factor receptor signaling pathway; IEA:Ensembl. DR GO; GO:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IEA:Ensembl. DR GO; GO:1904754; P:positive regulation of vascular associated smooth muscle cell migration; IGI:BHF-UCL. DR GO; GO:1904707; P:positive regulation of vascular associated smooth muscle cell proliferation; IGI:BHF-UCL. DR GO; GO:0001558; P:regulation of cell growth; IEA:Ensembl. 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:0007165; P:signal transduction; NAS:ProtInc. DR GO; GO:0051146; P:striated muscle cell differentiation; IEA:Ensembl. DR GO; GO:0044342; P:type B pancreatic cell proliferation; IEA:Ensembl. DR CDD; cd00191; TY; 1. DR FunFam; 4.10.40.20:FF:000001; Insulin-like growth factor binding protein 5; 1. DR FunFam; 4.10.800.10:FF:000005; Putative insulin-like growth factor-binding protein 5; 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. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Direct protein sequencing; Disulfide bond; KW Glycoprotein; Growth factor binding; Nucleus; Phosphoprotein; KW Proteomics identification; Reference proteome; Secreted; Signal. FT SIGNAL 1..20 FT /evidence="ECO:0000255" FT CHAIN 21..272 FT /note="Insulin-like growth factor-binding protein 5" FT /id="PRO_0000014385" FT DOMAIN 23..103 FT /note="IGFBP N-terminal" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00653" FT DOMAIN 189..263 FT /note="Thyroglobulin type-1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500" FT REGION 111..130 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 111..122 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 116 FT /note="Phosphoserine; by FAM20C" FT /evidence="ECO:0000269|PubMed:26091039" FT CARBOHYD 172 FT /note="O-linked (HexNAc...) threonine" FT /evidence="ECO:0000269|PubMed:9883900" FT DISULFID 27..53 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00653" FT DISULFID 30..55 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00653" FT DISULFID 38..56 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00653" FT DISULFID 45..59 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00653, FT ECO:0000269|PubMed:22117064" FT DISULFID 67..80 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00653, FT ECO:0000269|PubMed:22117064" FT DISULFID 74..100 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00653" FT DISULFID 192..219 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500, FT ECO:0000269|PubMed:22117064" FT DISULFID 230..241 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500, FT ECO:0000269|PubMed:22117064" FT DISULFID 243..263 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500, FT ECO:0000269|PubMed:22117064" FT VARIANT 138 FT /note="R -> W (in dbSNP:rs11575194)" FT /evidence="ECO:0000269|Ref.6" FT /id="VAR_019284" FT STRAND 79..81 FT /evidence="ECO:0007829|PDB:1H59" FT TURN 84..86 FT /evidence="ECO:0007829|PDB:1BOE" FT HELIX 89..94 FT /evidence="ECO:0007829|PDB:1H59" FT STRAND 98..101 FT /evidence="ECO:0007829|PDB:1H59" SQ SEQUENCE 272 AA; 30570 MW; 0A7AD37C6EEA3A81 CRC64; MVLLTAVLLL LAAYAGPAQS LGSFVHCEPC DEKALSMCPP SPLGCELVKE PGCGCCMTCA LAEGQSCGVY TERCAQGLRC LPRQDEEKPL HALLHGRGVC LNEKSYREQV KIERDSREHE EPTTSEMAEE TYSPKIFRPK HTRISELKAE AVKKDRRKKL TQSKFVGGAE NTAHPRIISA PEMRQESEQG PCRRHMEASL QELKASPRMV PRAVYLPNCD RKGFYKRKQC KPSRGRKRGI CWCVDKYGMK LPGMEYVDGD FQCHTFDSSN VE //