ID   IBP2_XENLA              Reviewed;         281 AA.
AC   Q5XHC5;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 80.
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;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1] {ECO:0000312|EMBL:AAH84133.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney {ECO:0000312|EMBL:AAH84133.1};
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (OCT-2004) 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; BC084133; AAH84133.1; -; mRNA.
DR   RefSeq; XP_018091144.1; XM_018235655.1.
DR   AlphaFoldDB; Q5XHC5; -.
DR   SMR; Q5XHC5; -.
DR   GeneID; 108701262; -.
DR   KEGG; xla:108701262; -.
DR   Xenbase; XB-GENE-865692; igfbp2.L.
DR   OrthoDB; 979270at2759; -.
DR   Proteomes; UP000186698; Chromosome 9_10L.
DR   Bgee; 108701262; Expressed in kidney and 11 other tissues.
DR   GO; GO:0005576; C:extracellular region; 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: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..281
FT                   /note="Insulin-like growth factor-binding protein 2"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000381736"
FT   DOMAIN          23..106
FT                   /note="IGFBP N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT   DOMAIN          180..262
FT                   /note="Thyroglobulin type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT   REGION          107..127
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          139..180
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           257..259
FT                   /note="Cell attachment site"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        151..180
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        183..217
FT                   /evidence="ECO:0000250|UniProtKB:P18065,
FT                   ECO:0000255|PROSITE-ProRule:PRU00500"
FT   DISULFID        228..239
FT                   /evidence="ECO:0000250|UniProtKB:P18065,
FT                   ECO:0000255|PROSITE-ProRule:PRU00500"
FT   DISULFID        241..262
FT                   /evidence="ECO:0000250|UniProtKB:P18065,
FT                   ECO:0000255|PROSITE-ProRule:PRU00500"
SQ   SEQUENCE   281 AA;  30592 MW;  60C594777FBE16C8 CRC64;
     MVLSEHLLVL LGAVLCAPAL SDVLFRCPPC SPERLAACPG NSPRSPCAEL VRAPGCGCCP
     VCARLEGESC GVYTARCAGG LRCYPHPGSE LPLQALVLGL GTCGKRRDAE YGSSQERGTE
     LPEDQSDNML VDNNLVAGPA VPGDFMPRKS SKAHAVNRER ANEQHRSKTN KSEDKKRPAR
     SLCQLQLDQV LERISGMHLP DDRGPLEHLY ALPIPNCDKN GFFNLKQCKM SVNGQRGECW
     CVNPITGKVL PGSPTVRGDP ECHLFYTNPE EERRAHTQRA P