ID   IBP2_SHEEP              Reviewed;         317 AA.
AC   Q29400;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   25-MAY-2022, entry version 112.
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   Flags: Precursor;
GN   Name=IGFBP2;
OS   Ovis aries (Sheep).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Ovis.
OX   NCBI_TaxID=9940;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Liver;
RX   PubMed=1381182; DOI=10.1677/jme.0.0090031;
RA   Delhanty P.J., Han V.K.;
RT   "The characterization and expression of ovine insulin-like growth factor-
RT   binding protein-2.";
RL   J. Mol. Endocrinol. 9:31-38(1992).
CC   -!- FUNCTION: Inhibits IGF-mediated growth and developmental rates (By
CC       similarity). 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. {ECO:0000250}.
CC   -!- SUBUNIT: Binds IGF2 more than IGF1. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed in abundance in selected adult tissues,
CC       namely liver, kidney, adrenal, pituitary and choroid plexus.
CC       {ECO:0000269|PubMed:1381182}.
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; S44612; AAB23135.1; -; mRNA.
DR   PIR; I46916; I46916.
DR   RefSeq; NP_001009436.1; NM_001009436.1.
DR   AlphaFoldDB; Q29400; -.
DR   BMRB; Q29400; -.
DR   SMR; Q29400; -.
DR   STRING; 9940.ENSOARP00000020858; -.
DR   MEROPS; I31.953; -.
DR   GeneID; 443469; -.
DR   KEGG; oas:443469; -.
DR   CTD; 3485; -.
DR   eggNOG; ENOG502QRWQ; Eukaryota.
DR   OrthoDB; 979270at2759; -.
DR   Proteomes; UP000002356; Unplaced.
DR   GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; IDA:AgBase.
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:0040008; P:regulation of growth; IEA:UniProtKB-KW.
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   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Growth factor binding; Growth regulation;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..33
FT                   /evidence="ECO:0000250"
FT   CHAIN           34..317
FT                   /note="Insulin-like growth factor-binding protein 2"
FT                   /id="PRO_0000014374"
FT   DOMAIN          35..126
FT                   /note="IGFBP N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT   DOMAIN          216..298
FT                   /note="Thyroglobulin type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT   REGION          125..151
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          189..218
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           293..295
FT                   /note="Cell attachment site"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        189..212
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        219..253
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT   DISULFID        264..275
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT   DISULFID        277..298
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
SQ   SEQUENCE   317 AA;  34189 MW;  613CD1C5BF06D84E CRC64;
     MQPRLGGPAL LLLPPLLLLL LLGAGGGDCG ARAEVLFRCP PCTPESLAAC KPPPGAAAGP
     AGDARVPCEL VREPGCGCCS VCARLEGERC GVYTPRCGQG LRCYPNPGSE LPLRALVHGE
     GTCEKHGDAE YSASPEQVAD NGEEHSEGGQ VENHVDGNVN LMGGGGGAGR KPLKFRMKEL
     AVFREKVTEQ HRQMGKGGKH HLGLEEPKKL RPPPARTPCQ QELDQVLERI STMRLPDERG
     PLEHLYSLHI PNCDKHGLYN LKQCKMSLNG QRGECWCVNP NTGKLIQGAP TIRGDPECHL
     FYNEQQGARG VHTQRMQ