IBP2_PIG
ID IBP2_PIG Reviewed; 316 AA.
AC P24853; Q9XSC7;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 2.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Insulin-like growth factor-binding protein 2;
DE Short=IBP-2;
DE Short=IGF-binding protein 2;
DE Short=IGFBP-2;
DE Short=pIGFBP-2;
DE Flags: Precursor;
GN Name=IGFBP2;
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], AND FUNCTION.
RX PubMed=10601973; DOI=10.1677/jme.0.0230277;
RA Badinga L., Song S., Simmen R.C.M., Clarke J.B., Clemmons D.R.,
RA Simmen F.A.;
RT "Complex mediation of uterine endometrial epithelial cell growth by
RT insulin-like growth factor-II (IGF-II) and IGF-binding protein-2.";
RL J. Mol. Endocrinol. 23:277-285(1999).
RN [2]
RP PROTEIN SEQUENCE OF 33-55.
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).
CC -!- FUNCTION: May have both growth-inhibiting and growth-promoting effects,
CC depending on tissue type; increases IGF-induced DNA synthesis in the
CC uterine epithelium. IGF-binding proteins prolong the half-life of the
CC IGFs and have been shown to either inhibit or stimulate the growth
CC promoting effects of the IGFs on cell culture. They alter the
CC interaction of IGFs with their cell surface receptors.
CC {ECO:0000269|PubMed:10601973}.
CC -!- SUBUNIT: Binds IGF2 more than IGF1.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- DOMAIN: The C-terminus is required for IGF-binding and growth
CC inhibition. {ECO:0000250}.
CC -!- PTM: O-glycosylated. {ECO:0000250}.
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DR EMBL; AF120326; AAD33246.1; -; mRNA.
DR PIR; JH0515; JH0515.
DR RefSeq; NP_999168.1; NM_214003.1.
DR AlphaFoldDB; P24853; -.
DR BMRB; P24853; -.
DR SMR; P24853; -.
DR STRING; 9823.ENSSSCP00000026205; -.
DR PaxDb; P24853; -.
DR PeptideAtlas; P24853; -.
DR Ensembl; ENSSSCT00000046489; ENSSSCP00000058079; ENSSSCG00000035392.
DR Ensembl; ENSSSCT00025066360; ENSSSCP00025028359; ENSSSCG00025048742.
DR Ensembl; ENSSSCT00030032504; ENSSSCP00030014613; ENSSSCG00030023423.
DR Ensembl; ENSSSCT00035033861; ENSSSCP00035013370; ENSSSCG00035025709.
DR Ensembl; ENSSSCT00040063583; ENSSSCP00040026850; ENSSSCG00040047179.
DR Ensembl; ENSSSCT00045012214; ENSSSCP00045008336; ENSSSCG00045007360.
DR Ensembl; ENSSSCT00050099451; ENSSSCP00050043019; ENSSSCG00050072827.
DR Ensembl; ENSSSCT00055035208; ENSSSCP00055027961; ENSSSCG00055017972.
DR Ensembl; ENSSSCT00060102645; ENSSSCP00060044757; ENSSSCG00060074969.
DR Ensembl; ENSSSCT00065084063; ENSSSCP00065036647; ENSSSCG00065061351.
DR Ensembl; ENSSSCT00070035784; ENSSSCP00070029905; ENSSSCG00070018133.
DR GeneID; 397064; -.
DR KEGG; ssc:397064; -.
DR CTD; 3485; -.
DR VGNC; VGNC:109491; IGFBP2.
DR eggNOG; ENOG502QRWQ; Eukaryota.
DR GeneTree; ENSGT00940000158542; -.
DR InParanoid; P24853; -.
DR OMA; AEPCAEM; -.
DR OrthoDB; 979270at2759; -.
DR ChiTaRS; IGFBP2; pig.
DR Proteomes; UP000008227; Chromosome 15.
DR Proteomes; UP000314985; Chromosome 15.
DR Bgee; ENSSSCG00000035392; Expressed in forelimb bud and 44 other tissues.
DR ExpressionAtlas; P24853; baseline and differential.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0031994; F:insulin-like growth factor I binding; ISS:UniProtKB.
DR GO; GO:0031995; F:insulin-like growth factor II binding; ISS:UniProtKB.
DR GO; GO:0042104; P:positive regulation of activated T cell proliferation; ISS:UniProtKB.
DR GO; GO:0045927; P:positive regulation of growth; IMP:UniProtKB.
DR GO; GO:0043567; P:regulation of insulin-like growth factor receptor signaling pathway; ISS:UniProtKB.
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; IPR012210; IGFBP-2.
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 Pfam; PF00219; IGFBP; 1.
DR Pfam; PF00086; Thyroglobulin_1; 1.
DR PRINTS; PR01976; IGFBPFAMILY.
DR PRINTS; PR01978; IGFBPFAMILY2.
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 Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Growth factor binding; Growth regulation; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..316
FT /note="Insulin-like growth factor-binding protein 2"
FT /id="PRO_0000014372"
FT DOMAIN 31..126
FT /note="IGFBP N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT DOMAIN 215..297
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT REGION 189..217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 292..294
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT COMPBIAS 189..211
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 218..252
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 263..274
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 276..297
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
SQ SEQUENCE 316 AA; 33937 MW; E7812F2DA2A870C4 CRC64;
MLPRLGGTAL SLLPLLLLLL GTGGRGARAE VLFRCPPCTP ESLAACRPPP AAPPSAGAGP
AGDSRAPCEL VREPGCGCCS VCARLEGERC GVYTPRCAQG LRCYPHPGSE LPLQALVLGE
GTCEKRRDAE YGASPEQVAD NGDDAEGGLV ENHVDGNVNL LGGTGGAGRK PLKSGMKELA
VFREKVTEQH RQMGKGGKHH LGLEEPKKLR PPPARTPCQQ ELDQVLERIS TMRLPDERGP
LEHLYSLHIP NCDKHGLYNL KQCKMSLNGQ RGECWCVNPN TGKLIQGAPT IRGDPECHLF
YNEQQGARGA HTQRMQ
