ID   IBP2_CHICK              Reviewed;         311 AA.
AC   P49705;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 125.
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   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RC   TISSUE=Embryonic retina;
RX   PubMed=8546813; DOI=10.1677/jme.0.0150049;
RA   Schoen T.J., Mazuruk K., Waldbillig R.J., Potts J., Beebe D.C.,
RA   Chader G.J., Rodriguez I.R.;
RT   "Cloning and characterization of a chick embryo cDNA and gene for IGF-
RT   binding protein-2.";
RL   J. Mol. Endocrinol. 15:49-59(1995).
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   -!- DEVELOPMENTAL STAGE: Expressed in embryonic day-15 eye, brain, skeletal
CC       muscle, heart and intestine, but virtually absent from embryonic day-15
CC       liver. {ECO:0000269|PubMed:8546813}.
CC   -!- DOMAIN: The C-terminus is required for IGF-binding and growth
CC       inhibition. {ECO:0000250}.
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DR   EMBL; U15086; AAA92885.1; -; mRNA.
DR   RefSeq; NP_990690.1; NM_205359.1.
DR   AlphaFoldDB; P49705; -.
DR   SMR; P49705; -.
DR   STRING; 9031.ENSGALP00000018675; -.
DR   MEROPS; I31.953; -.
DR   PaxDb; P49705; -.
DR   PRIDE; P49705; -.
DR   GeneID; 396315; -.
DR   KEGG; gga:396315; -.
DR   CTD; 3485; -.
DR   VEuPathDB; HostDB:geneid_396315; -.
DR   eggNOG; ENOG502QRWQ; Eukaryota.
DR   InParanoid; P49705; -.
DR   OrthoDB; 979270at2759; -.
DR   PhylomeDB; P49705; -.
DR   PRO; PR:P49705; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
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: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   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; Growth factor binding; Growth regulation;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..36
FT                   /evidence="ECO:0000250"
FT   CHAIN           37..311
FT                   /note="Insulin-like growth factor-binding protein 2"
FT                   /id="PRO_0000014375"
FT   DOMAIN          38..120
FT                   /note="IGFBP N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT   DOMAIN          209..291
FT                   /note="Thyroglobulin type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT   REGION          112..168
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          188..210
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           286..288
FT                   /note="Cell attachment site"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        188..205
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        212..246
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT   DISULFID        257..268
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT   DISULFID        270..291
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
SQ   SEQUENCE   311 AA;  33538 MW;  5AC8D3E08121F45E CRC64;
     MALGGVGRGG AARAAWPRLL LAALAPALAL AGPALPEVLF RCPPCTAERL AACSPAARPP
     CPELVREPGC GCCPVCARLE DEACGVYTPR CAAGLRCYPD PGAELPPQAL VQGQGTCARP
     PDTDEYGAST EPPADNGDDR SESILAENHV DSTGGMMSGA SSRKPLKTGM KEMPVMREKV
     NEQQRQMGKV GKAHHNHEDS KKSRMPTGRT PCQQELDQVL ERISTMRLPD ERGPLEHLYS
     LHIPNCDKHG LYNLKQCKMS VNGQRGECWC VDPIHGKVIQ GAPTIRGDPE CHLFYTAHEQ
     EDRGAHALRS Q