IBP5_HUMAN
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 03-AUG-2022, entry version 219.
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 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 [10]
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 [11]
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 [12]
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: 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 -!- 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.
CC -!- TISSUE SPECIFICITY: Osteosarcoma, and at lower levels in liver, kidney
CC and brain.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/igfbp5/";
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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 PDBsum; 1BOE; -.
DR PDBsum; 1H59; -.
DR AlphaFoldDB; P24593; -.
DR SMR; P24593; -.
DR BioGRID; 109709; 112.
DR DIP; DIP-48433N; -.
DR IntAct; P24593; 82.
DR STRING; 9606.ENSP00000233813; -.
DR BindingDB; P24593; -.
DR ChEMBL; CHEMBL2665; -.
DR DrugBank; DB01277; Mecasermin.
DR MEROPS; I31.952; -.
DR GlyGen; P24593; 2 sites, 1 O-linked glycan (1 site).
DR iPTMnet; P24593; -.
DR PhosphoSitePlus; P24593; -.
DR BioMuta; IGFBP5; -.
DR DMDM; 124069; -.
DR jPOST; P24593; -.
DR MassIVE; P24593; -.
DR PaxDb; P24593; -.
DR PeptideAtlas; P24593; -.
DR PRIDE; P24593; -.
DR ProteomicsDB; 54219; -.
DR Antibodypedia; 3978; 452 antibodies from 38 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 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; 979270at2759; -.
DR PhylomeDB; P24593; -.
DR TreeFam; TF331211; -.
DR BioCyc; MetaCyc:ENSG00000115461-MON; -.
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 1077 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 210 other tissues.
DR ExpressionAtlas; P24593; baseline and differential.
DR Genevisible; P24593; HS.
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: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:0007568; P:aging; IEA:Ensembl.
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 protein kinase B signaling; 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 Gene3D; 4.10.800.10; -; 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:SF4; PTHR11551:SF4; 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; SSF57184; 1.
DR SUPFAM; SSF57610; SSF57610; 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; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Growth factor binding; Phosphoprotein; Reference proteome; Secreted;
KW 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..126
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 45..59
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500,
FT ECO:0000269|PubMed:22117064"
FT DISULFID 67..80
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500,
FT ECO:0000269|PubMed:22117064"
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
