ID   IBP2_XENTR              Reviewed;         284 AA.
AC   A4IIA2;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Insulin-like growth factor-binding protein 2 {ECO:0000250|UniProtKB:P18065};
DE            Short=IGF-binding protein 2 {ECO:0000250|UniProtKB:P18065};
DE            Short=IGFBP-2 {ECO:0000250|UniProtKB:P18065};
DE   Flags: Precursor;
GN   Name=igfbp2 {ECO:0000312|EMBL:AAI35929.1};
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1] {ECO:0000312|EMBL:AAI35929.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Tadpole {ECO:0000312|EMBL:AAI35929.1};
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (MAR-2007) 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 (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with igf1 and igf2. {ECO:0000250|UniProtKB:Q9PTH3}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
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DR   EMBL; BC135928; AAI35929.1; -; mRNA.
DR   RefSeq; NP_001093707.1; NM_001100237.1.
DR   AlphaFoldDB; A4IIA2; -.
DR   SMR; A4IIA2; -.
DR   STRING; 8364.ENSXETP00000042987; -.
DR   PaxDb; A4IIA2; -.
DR   DNASU; 100101720; -.
DR   Ensembl; ENSXETT00000094605; ENSXETP00000070923; ENSXETG00000035913.
DR   GeneID; 100101720; -.
DR   KEGG; xtr:100101720; -.
DR   CTD; 3485; -.
DR   Xenbase; XB-GENE-487299; igfbp2.
DR   eggNOG; ENOG502QRWQ; Eukaryota.
DR   InParanoid; A4IIA2; -.
DR   OrthoDB; 979270at2759; -.
DR   Reactome; R-XTR-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR   Proteomes; UP000008143; Chromosome 9.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000033133; Expressed in 2-cell stage embryo and 12 other tissues.
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   Developmental protein; Disulfide bond; Growth factor binding;
KW   Growth regulation; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..284
FT                   /note="Insulin-like growth factor-binding protein 2"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000381737"
FT   DOMAIN          23..106
FT                   /note="IGFBP N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT   DOMAIN          184..266
FT                   /note="Thyroglobulin type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT   REGION          108..184
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           261..263
FT                   /note="Cell attachment site"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        109..131
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        147..184
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        187..221
FT                   /evidence="ECO:0000250|UniProtKB:P18065,
FT                   ECO:0000255|PROSITE-ProRule:PRU00500"
FT   DISULFID        232..243
FT                   /evidence="ECO:0000250|UniProtKB:P18065,
FT                   ECO:0000255|PROSITE-ProRule:PRU00500"
FT   DISULFID        245..266
FT                   /evidence="ECO:0000250|UniProtKB:P18065,
FT                   ECO:0000255|PROSITE-ProRule:PRU00500"
SQ   SEQUENCE   284 AA;  30891 MW;  A60A73CCACB91E88 CRC64;
     MGLSRYLLGL LLGVLCTPAP AEVLFRCPPC SPERLATCPG SAPRPPCAEL VRAPGCGCCP
     VCARLEGESC GVYTARCAGG LRCYPHPGSE LPLQALVLGL GTCGKRRDTE YGSSQERGTE
     LPEERSDNML VDNKLEAGPA VAGEAAPRKP SKKEMKEIAV TRERANEQQR SKSNKSEDKK
     RPARSLCQLQ LDQVLERISG MHLPDDRGPL EHLYALHIPN CDKNGFFNLK QCKMSVNGQR
     GECWCVNPIT GKALPGSPTI RGDPECHLYY TSPEEGRAHT QRAP