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   24-JAN-2024, entry version 157.
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   MEROPS; I31.952; -.
DR   GlyCosmos; P16611; 3 sites, No reported glycans.
DR   PaxDb; 9823-ENSSSCP00000017719; -.
DR   GeneID; 448812; -.
DR   KEGG; ssc:448812; -.
DR   CTD; 3486; -.
DR   eggNOG; ENOG502QWC0; Eukaryota.
DR   InParanoid; P16611; -.
DR   OMA; EQCKPLA; -.
DR   OrthoDB; 5394492at2759; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   Proteomes; UP000694570; Unplaced.
DR   Proteomes; UP000694571; Unplaced.
DR   Proteomes; UP000694720; Unplaced.
DR   Proteomes; UP000694722; Unplaced.
DR   Proteomes; UP000694723; Unplaced.
DR   Proteomes; UP000694724; Unplaced.
DR   Proteomes; UP000694725; Unplaced.
DR   Proteomes; UP000694726; Unplaced.
DR   Proteomes; UP000694727; Unplaced.
DR   Proteomes; UP000694728; 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; 4.10.40.20; -; 1.
DR   Gene3D; 4.10.800.10; Thyroglobulin type-1; 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; INSULIN-LIKE GROWTH FACTOR BINDING PROTEIN; 1.
DR   PANTHER; PTHR11551:SF3; INSULIN-LIKE GROWTH FACTOR-BINDING PROTEIN 3; 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; 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   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        40..69
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT   DISULFID        43..71
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT   DISULFID        51..72
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT   DISULFID        60..75
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT   DISULFID        83..96
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT   DISULFID        90..116
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
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
//