IBP3_BOVIN
ID IBP3_BOVIN Reviewed; 291 AA.
AC P20959; A6QPI3; Q9GJV5;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 3.
DT 03-AUG-2022, entry version 164.
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;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1711841; DOI=10.1016/0006-291x(91)90641-j;
RA Spratt S.K., Tatsuno G.P., Sommer A.;
RT "Cloning and characterization of bovine insulin-like growth factor binding
RT protein-3 (bIGFBP-3).";
RL Biochem. Biophys. Res. Commun. 177:1025-1032(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC TISSUE=Liver;
RX PubMed=9202228; DOI=10.1210/endo.138.7.5288;
RA Erondu N.E., Toland B., Boes M., Dake B., Moser D.R., Bar R.S.;
RT "Bovine insulin-like growth factor binding protein-3: organization of the
RT chromosomal gene and functional analysis of its promoter.";
RL Endocrinology 138:2856-2862(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal lung;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PROTEIN SEQUENCE OF 28-52.
RX PubMed=1701128; DOI=10.1210/endo-127-6-2795;
RA Conover C.A., Ronk M., Lombana F., Powell D.R.;
RT "Structural and biological characterization of bovine insulin-like growth
RT factor binding protein-3.";
RL Endocrinology 127:2795-2803(1990).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 194-266.
RX PubMed=9363609; DOI=10.1111/j.1365-2052.1997.tb03277.x;
RA Maciulla J.H., Zhang H.M., Denise S.K.;
RT "A novel polymorphism in the bovine insulin-like growth factor binding
RT protein-3 (IGFBP3) gene.";
RL Anim. Genet. 28:375-375(1997).
RN [6]
RP INTERACTION WITH XLKD1.
RX PubMed=12912978; DOI=10.1074/jbc.m306411200;
RA Huang S.S., Tang F.-M., Huang Y.-H., Liu I.-H., Hsu S.-C., Chen S.-T.,
RA Huang J.S.;
RT "Cloning, expression, characterization and role in autocrine cell growth of
RT cell surface retention sequence binding protein-1.";
RL J. Biol. Chem. 278:43855-43869(2003).
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.
CC {ECO:0000250|UniProtKB:P17936}.
CC -!- SUBUNIT: Interacts with TMEM219 (By similarity). Binds IGF2 more than
CC IGF1. Forms a ternary complex of about 140 to 150 kDa with IGF1 or IGF2
CC and a 85 kDa glycoprotein (ALS). Interacts with XLKD1. {ECO:0000250,
CC ECO:0000269|PubMed:12912978}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Plasma; expressed by most tissues.
CC -!- PTM: Phosphorylated by FAM20C in the extracellular medium.
CC {ECO:0000250|UniProtKB:P17936}.
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DR EMBL; M76478; AAA30582.1; -; mRNA.
DR EMBL; AF305199; AAG29824.1; -; mRNA.
DR EMBL; AF305712; AAG29825.1; -; Genomic_DNA.
DR EMBL; BC149336; AAI49337.1; -; mRNA.
DR EMBL; U83465; AAB41430.1; -; Genomic_DNA.
DR PIR; JN0064; JN0064.
DR RefSeq; NP_776981.1; NM_174556.1.
DR AlphaFoldDB; P20959; -.
DR SMR; P20959; -.
DR STRING; 9913.ENSBTAP00000047769; -.
DR MEROPS; I31.952; -.
DR PaxDb; P20959; -.
DR PRIDE; P20959; -.
DR Ensembl; ENSBTAT00000053426; ENSBTAP00000047769; ENSBTAG00000003994.
DR GeneID; 282261; -.
DR KEGG; bta:282261; -.
DR CTD; 3486; -.
DR VEuPathDB; HostDB:ENSBTAG00000003994; -.
DR VGNC; VGNC:30085; IGFBP3.
DR eggNOG; ENOG502QWC0; Eukaryota.
DR GeneTree; ENSGT00940000158092; -.
DR HOGENOM; CLU_070833_1_1_1; -.
DR InParanoid; P20959; -.
DR OMA; ALEQCKP; -.
DR OrthoDB; 979270at2759; -.
DR TreeFam; TF331211; -.
DR Reactome; R-BTA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-BTA-8957275; Post-translational protein phosphorylation.
DR Proteomes; UP000009136; Chromosome 4.
DR Bgee; ENSBTAG00000003994; Expressed in mesenteric lymph node and 103 other tissues.
DR ExpressionAtlas; P20959; baseline and differential.
DR GO; GO:0005615; C:extracellular space; IDA:AgBase.
DR GO; GO:0042567; C:insulin-like growth factor ternary complex; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0001968; F:fibronectin binding; IBA:GO_Central.
DR GO; GO:0031994; F:insulin-like growth factor I binding; IBA:GO_Central.
DR GO; GO:0031995; F:insulin-like growth factor II binding; IBA:GO_Central.
DR GO; GO:0008160; F:protein tyrosine phosphatase activator activity; ISS:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0000165; P:MAPK cascade; IEA:Ensembl.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; IEA:Ensembl.
DR GO; GO:0014912; P:negative regulation of smooth muscle cell migration; IEA:Ensembl.
DR GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; IEA:Ensembl.
DR GO; GO:0001649; P:osteoblast differentiation; IEA:Ensembl.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0043568; P:positive regulation of insulin-like growth factor receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IEA:Ensembl.
DR GO; GO:0045663; P:positive regulation of myoblast differentiation; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IEA:Ensembl.
DR GO; GO:0001558; P:regulation of cell growth; IEA:Ensembl.
DR GO; GO:0010906; P:regulation of glucose metabolic process; IEA:Ensembl.
DR GO; GO:0043567; P:regulation of insulin-like growth factor receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0032868; P:response to insulin; IDA:AgBase.
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; 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:1701128"
FT CHAIN 28..291
FT /note="Insulin-like growth factor-binding protein 3"
FT /id="PRO_0000014377"
FT DOMAIN 36..119
FT /note="IGFBP N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT DOMAIN 210..285
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT REGION 28..134
FT /note="IGF-binding"
FT /evidence="ECO:0000255"
FT REGION 132..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 177..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..158
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..206
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 148
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P17936"
FT MOD_RES 201
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P17936"
FT CARBOHYD 118
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 136
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 199
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 213..240
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 251..262
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 264..285
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT CONFLICT 5..7
FT /note="RPA -> PPR (in Ref. 1; AAA30582)"
FT /evidence="ECO:0000305"
FT CONFLICT 66..67
FT /note="EP -> DA (in Ref. 1; AAA30582)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 291 AA; 31570 MW; 19DEC2F09528AE12 CRC64;
MLRARPALWA AALTALTLLR GPPAARAGAG TMGAGPVVRC EPCDARAVAQ CAPPPPSPPC
AELVREPGCG CCLTCALREG QPCGVYTERC GSGLRCQPPP GDPRPLQALL DGRGLCANAS
AVGRLRPYLL PSASGNGSES EEDHSMGSTE NQAGPSTHRV PVSKFHPIHT KMDVIKKGHA
KDSQRYKVDY ESQSTDTQNF SSESKRETEY GPCRREMEDT LNHLKFLNML SPRGIHIPNC
DKKGFYKKKQ CRPSKGRKRG FCWCVDKYGQ PLPGFDVKGK GDVHCYSMES K
