IBP3_PIG
ID IBP3_PIG Reviewed; 293 AA.
AC P16611; Q6S6K2; Q9TTI0;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 3.
DT 25-MAY-2022, entry version 150.
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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=12553871; DOI=10.1677/joe.0.1760227;
RA Pampusch M.S., Kamanga-Sollo E., White M.E., Hathaway M.R., Dayton W.R.;
RT "Effect of recombinant porcine IGF-binding protein-3 on proliferation of
RT embryonic porcine myogenic cell cultures in the presence and absence of
RT IGF-I.";
RL J. Endocrinol. 176:227-235(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=14715717; DOI=10.1210/en.2003-1552;
RA Ongeri E.M., Zhu Q., Verderame M.F., Hammond J.M.;
RT "Insulin-like growth factor-binding protein-3 in porcine ovarian granulosa
RT cells: gene cloning, promoter mapping, and follicle-stimulating hormone
RT regulation.";
RL Endocrinology 145:1776-1785(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 28-293.
RX PubMed=1688850; DOI=10.1016/s0021-9258(19)39961-2;
RA Shimasaki S., Shimonaka M., Ui M., Inouye S., Shibata F., Ling N.;
RT "Structural characterization of a follicle-stimulating hormone action
RT inhibitor in porcine ovarian follicular fluid. Its identification as the
RT insulin-like growth factor-binding protein.";
RL J. Biol. Chem. 265:2198-2202(1990).
RN [4]
RP PROTEIN SEQUENCE OF 28-42.
RX PubMed=1722398; DOI=10.1016/0006-291x(91)92056-p;
RA Coleman M.E., Pan Y.-C.E., Etherton T.D.;
RT "Identification and NH2-terminal amino acid sequence of three insulin-like
RT growth factor-binding proteins in porcine serum.";
RL Biochem. Biophys. Res. Commun. 181:1131-1136(1991).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 143-293.
RA Liu D., Zhang Y., Zhang X., Yang G.;
RT "Study on SNPs of porcine IGFBP-3 gene.";
RL Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
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; AF085482; AAF23229.1; -; mRNA.
DR EMBL; AY464121; AAR87008.1; -; Genomic_DNA.
DR EMBL; J05228; AAA31054.1; -; mRNA.
DR EMBL; AY422045; AAQ97624.1; -; Genomic_DNA.
DR PIR; A35037; A35037.
DR PIR; JH0516; JH0516.
DR RefSeq; NP_001005156.1; NM_001005156.1.
DR AlphaFoldDB; P16611; -.
DR SMR; P16611; -.
DR STRING; 9823.ENSSSCP00000017719; -.
DR MEROPS; I31.952; -.
DR PaxDb; P16611; -.
DR PRIDE; P16611; -.
DR GeneID; 448812; -.
DR KEGG; ssc:448812; -.
DR CTD; 3486; -.
DR eggNOG; ENOG502QWC0; Eukaryota.
DR InParanoid; P16611; -.
DR OMA; ALEQCKP; -.
DR OrthoDB; 979270at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005615; C:extracellular space; ISS:AgBase.
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:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0045663; P:positive regulation of myoblast differentiation; ISS:UniProtKB.
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; ISS:AgBase.
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:1722398"
FT CHAIN 28..293
FT /note="Insulin-like growth factor-binding protein 3"
FT /id="PRO_0000045904"
FT DOMAIN 36..119
FT /note="IGFBP N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT DOMAIN 212..287
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT REGION 132..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 178..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..208
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 150
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P17936"
FT MOD_RES 203
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P17936"
FT CARBOHYD 118
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 138
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 201
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 215..242
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 253..264
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 266..287
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT CONFLICT 23
FT /note="P -> S (in Ref. 1; AAF23229)"
FT /evidence="ECO:0000305"
FT CONFLICT 32
FT /note="A -> V (in Ref. 1 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 170
FT /note="V -> I (in Ref. 1; AAF23229)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 293 AA; 31690 MW; B2ECED337B91DA83 CRC64;
MQRARPALWA AALIALALLR GPPAARAGSG AAGTGPVVRC EPCDARALAQ CAPPPAAPPC
AELVREPGCG CCLTCALREG QACGVYTERC GAGLRCQPPP GEPRPLQALL DGRGICANAS
AAGRLRAYLL PAPPAPGNGS ESEEDRSVDS MENQALPSTH RVPDSKLHSV HTKMDVIKKG
HAKDSQRYKV DYESQSTDTQ NFSSESKRET EYGPCRREME DTLNHLKFLN MLSPRGIHIP
NCDKKGFYKK KQCRPSKGRK RGFCWCVDKY GQPLPGFDVK GKGDVHCYSM ESK
