IBP3_RAT
ID IBP3_RAT Reviewed; 292 AA.
AC P15473;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 2.
DT 25-MAY-2022, entry version 166.
DE RecName: Full=Insulin-like growth factor-binding protein 3;
DE Short=IBP-3;
DE Short=IGF-binding protein 3;
DE Short=IGFBP-3;
DE Flags: Precursor;
GN Name=Igfbp3; Synonyms=Igfbp-3;
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].
RX PubMed=2480787; DOI=10.1016/s0006-291x(89)80052-x;
RA Shimasaki S., Koba A., Mercado M., Shimonaka M., Ling N.;
RT "Complementary DNA structure of the high molecular weight rat insulin-like
RT growth factor binding protein (IGF-BP3) and tissue distribution of its
RT mRNA.";
RL Biochem. Biophys. Res. Commun. 165:907-912(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=1689154; DOI=10.1016/0006-291x(90)90894-s;
RA Albiston A.L., Herington A.C.;
RT "Cloning and characterization of the growth hormone-dependent insulin-like
RT growth factor binding protein (IGFBP-3) in the rat.";
RL Biochem. Biophys. Res. Commun. 166:892-897(1990).
RN [3]
RP PROTEIN SEQUENCE OF 28-68.
RX PubMed=3190697; DOI=10.1016/s0006-291x(88)80758-7;
RA Zapf J., Born W., Chang J.Y., James P., Froesch E.R., Fischer J.A.;
RT "Isolation and NH2-terminal amino acid sequences of rat serum carrier
RT proteins for insulin-like growth factors.";
RL Biochem. Biophys. Res. Commun. 156:1187-1194(1988).
RN [4]
RP PROTEIN SEQUENCE OF 28-42.
RX PubMed=2443135; DOI=10.1016/s0006-291x(87)80136-5;
RA Baxter R.C., Martin J.L.;
RT "Binding proteins for insulin-like growth factors in adult rat serum.
RT Comparison with other human and rat binding proteins.";
RL Biochem. Biophys. Res. Commun. 147:408-415(1987).
RN [5]
RP PROTEIN SEQUENCE OF 28-49.
RC TISSUE=Serum;
RX PubMed=2480123; DOI=10.1016/0006-291x(89)91053-x;
RA Shimonaka M., Schroeder R., Shimasaki S., Ling N.;
RT "Identification of a novel binding protein for insulin-like growth factors
RT in adult rat serum.";
RL Biochem. Biophys. Res. Commun. 165:189-195(1989).
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. Also exhibits IGF-independent
CC antiproliferative and apoptotic effects mediated by its receptor
CC TMEM219/IGFBP-3R. Promotes testicular germ cell apoptosis (By
CC similarity). {ECO:0000250|UniProtKB:P17936}.
CC -!- SUBUNIT: Interacts with XLKD1. Binds IGF2 more than IGF1. Forms a
CC ternary complex of about 140 to 150 kDa with IGF1 or IGF2 and a 85 kDa
CC glycoprotein (ALS). Interacts with TMEM219 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- PTM: Phosphorylated by FAM20C in the extracellular medium.
CC {ECO:0000250|UniProtKB:P17936}.
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DR EMBL; M31837; AAA41383.1; -; mRNA.
DR EMBL; M33300; AAB00989.1; -; mRNA.
DR PIR; A36748; A36748.
DR RefSeq; NP_036720.2; NM_012588.2.
DR AlphaFoldDB; P15473; -.
DR SMR; P15473; -.
DR STRING; 10116.ENSRNOP00000011678; -.
DR MEROPS; I31.952; -.
DR GlyGen; P15473; 4 sites.
DR PhosphoSitePlus; P15473; -.
DR PaxDb; P15473; -.
DR PRIDE; P15473; -.
DR DNASU; 24484; -.
DR GeneID; 24484; -.
DR KEGG; rno:24484; -.
DR UCSC; RGD:2874; rat.
DR CTD; 3486; -.
DR RGD; 2874; Igfbp3.
DR eggNOG; ENOG502QWC0; Eukaryota.
DR InParanoid; P15473; -.
DR OrthoDB; 979270at2759; -.
DR PhylomeDB; P15473; -.
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:P15473; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0000792; C:heterochromatin; IDA:RGD.
DR GO; GO:0042568; C:insulin-like growth factor binary complex; IDA:RGD.
DR GO; GO:0042567; C:insulin-like growth factor ternary complex; IDA:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0031091; C:platelet alpha granule; IDA:RGD.
DR GO; GO:0001968; F:fibronectin binding; ISO:RGD.
DR GO; GO:0005520; F:insulin-like growth factor binding; ISO: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; IPI:RGD.
DR GO; GO:0008160; F:protein tyrosine phosphatase activator activity; ISS:UniProtKB.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0071392; P:cellular response to estradiol stimulus; IEP:RGD.
DR GO; GO:1904017; P:cellular response to Thyroglobulin triiodothyronine; IEP:RGD.
DR GO; GO:0007565; P:female pregnancy; IEP:RGD.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:RGD.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; 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:2000844; P:negative regulation of testosterone secretion; IMP:RGD.
DR GO; GO:0001649; P:osteoblast differentiation; ISO:RGD.
DR GO; GO:1902512; P:positive regulation of apoptotic DNA fragmentation; IMP:RGD.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:RGD.
DR GO; GO:0010666; P:positive regulation of cardiac muscle cell apoptotic process; IMP:RGD.
DR GO; GO:0043568; P:positive regulation of insulin-like growth factor receptor signaling pathway; ISO:RGD.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; ISO:RGD.
DR GO; GO:0045663; P:positive regulation of myoblast differentiation; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; ISO:RGD.
DR GO; GO:0001558; P:regulation of cell growth; ISO:RGD.
DR GO; GO:0010906; P:regulation of glucose metabolic process; 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:0061771; P:response to caloric restriction; IEP:RGD.
DR GO; GO:0060416; P:response to growth hormone; IEP:RGD.
DR GO; GO:0001666; P:response to hypoxia; IEP:RGD.
DR GO; GO:0032868; P:response to insulin; IEP:RGD.
DR GO; GO:1990418; P:response to insulin-like growth factor stimulus; IEP:RGD.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0044342; P:type B pancreatic cell proliferation; ISO:RGD.
DR CDD; cd00191; TY; 1.
DR Gene3D; 4.10.800.10; -; 1.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR012211; IGFBP-3.
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:SF3; PTHR11551:SF3; 1.
DR Pfam; PF00219; IGFBP; 1.
DR Pfam; PF00086; Thyroglobulin_1; 1.
DR PRINTS; PR01976; IGFBPFAMILY.
DR PRINTS; PR01979; IGFBPFAMILY3.
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 Apoptosis; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Growth factor binding; Phosphoprotein; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000269|PubMed:2443135,
FT ECO:0000269|PubMed:2480123, ECO:0000269|PubMed:3190697"
FT CHAIN 28..292
FT /note="Insulin-like growth factor-binding protein 3"
FT /id="PRO_0000014380"
FT DOMAIN 36..119
FT /note="IGFBP N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT DOMAIN 211..286
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT REGION 127..161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 191..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..160
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..207
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 149
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P17936"
FT MOD_RES 202
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P17936"
FT CARBOHYD 118
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 124
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 137
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 200
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 214..241
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 252..263
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 265..286
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT CONFLICT 8
FT /note="Missing (in Ref. 2; AAB00989)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 292 AA; 31680 MW; 1887D5E2A528F3B2 CRC64;
MHPARPALWA AALTALTLLR GPPVARAGAG AVGAGPVVRC EPCDARALAQ CAPPPTAPAC
TELVREPGCG CCLTCALREG DACGVYTERC GTGLRCQPRP AEQYPLKALL NGRGFCANAS
AASNLSAYLP SQPSPGNTTE SEEDHNAGSV ESQVVPSTHR VTDSKFHPLH SKMEVIIKGQ
ARDSQRYKVD YESQSTDTQN FSSESKRETE YGPCRREMED TLNHLKFLNV LSPRGVHIPN
CDKKGFYKKK QCRPSKGRKR GFCWCVDKYG QPLPGYDTKG KDDVHCLSVQ SQ
