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IBP5_XENLA
ID   IBP5_XENLA              Reviewed;         265 AA.
AC   Q90WV8;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Insulin-like growth factor-binding protein 5;
DE            Short=IBP-5;
DE            Short=IGF-binding protein 5;
DE            Short=IGFBP-5;
DE            Short=xIGFBP-5;
DE   Flags: Precursor;
GN   Name=igfbp5 {ECO:0000312|EMBL:AAL12250.1};
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:0000305, ECO:0000312|EMBL:AAL12250.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP   DEVELOPMENTAL STAGE.
RC   TISSUE=Embryo {ECO:0000269|PubMed:11709186};
RX   PubMed=11709186; DOI=10.1016/s1534-5807(01)00069-7;
RA   Pera E.M., Wessely O., Li S.-Y., De Robertis E.M.;
RT   "Neural and head induction by insulin-like growth factor signals.";
RL   Dev. Cell 1:655-665(2001).
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. Promotes anterior neural development
CC       by stimulating insulin growth factor (IGF) signaling via IGF receptors.
CC       {ECO:0000269|PubMed:11709186, ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11709186}.
CC   -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC       Expressed on the dorsal side during gastrulation. Becomes confined to
CC       the floor plate, notochord and dorsal endoderm during neurulation.
CC       Expressed in additional domains at the tailbud stage in cranial nerves,
CC       ear vesicle, dorsal fin and somites. Dorsal midline expression becomes
CC       restricted to the floor plate and hypochord.
CC       {ECO:0000269|PubMed:11709186}.
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DR   EMBL; AY052629; AAL12250.1; -; mRNA.
DR   RefSeq; NP_001083938.1; NM_001090469.1.
DR   RefSeq; XP_018089692.1; XM_018234203.1.
DR   AlphaFoldDB; Q90WV8; -.
DR   SMR; Q90WV8; -.
DR   MEROPS; I31.952; -.
DR   PRIDE; Q90WV8; -.
DR   GeneID; 399201; -.
DR   KEGG; xla:399201; -.
DR   CTD; 399201; -.
DR   Xenbase; XB-GENE-485077; igfbp5.L.
DR   OMA; YTERCAL; -.
DR   OrthoDB; 979270at2759; -.
DR   Proteomes; UP000186698; Chromosome 9_10L.
DR   Bgee; 399201; Expressed in internal ear and 19 other tissues.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0005520; F:insulin-like growth factor binding; IEA:InterPro.
DR   GO; GO:0009952; P:anterior/posterior pattern specification; IMP:UniProtKB.
DR   GO; GO:0048009; P:insulin-like growth factor receptor signaling pathway; IDA:UniProtKB.
DR   GO; GO:0007399; P:nervous system development; IMP:UniProtKB.
DR   CDD; cd00191; TY; 1.
DR   Gene3D; 4.10.800.10; -; 1.
DR   InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR   InterPro; IPR012213; IGFBP-5.
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   PANTHER; PTHR11551:SF4; PTHR11551:SF4; 1.
DR   Pfam; PF00219; IGFBP; 1.
DR   Pfam; PF00086; Thyroglobulin_1; 1.
DR   PRINTS; PR01976; IGFBPFAMILY.
DR   PRINTS; PR01981; IGFBPFAMILY5.
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   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..265
FT                   /note="Insulin-like growth factor-binding protein 5"
FT                   /id="PRO_0000223894"
FT   DOMAIN          24..104
FT                   /note="IGFBP N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT   DOMAIN          182..256
FT                   /note="Thyroglobulin type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT   REGION          111..137
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        46..60
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT   DISULFID        68..81
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT   DISULFID        185..212
FT                   /evidence="ECO:0000250|UniProtKB:P24593,
FT                   ECO:0000255|PROSITE-ProRule:PRU00500"
FT   DISULFID        223..234
FT                   /evidence="ECO:0000250|UniProtKB:P24593,
FT                   ECO:0000255|PROSITE-ProRule:PRU00500"
FT   DISULFID        236..256
FT                   /evidence="ECO:0000250|UniProtKB:P24593,
FT                   ECO:0000255|PROSITE-ProRule:PRU00500"
SQ   SEQUENCE   265 AA;  29995 MW;  E0B943382778A8DA CRC64;
     MEMLLPMCLL LVSLCLGQCQ ALGSFVHCEP CDDKAMSMCP PTPVGCELVK EPGCGCCMTC
     ALAEGHRCGV YTEHCAKGLR CLPEQGEEKP LHALLHGRGV CLNLKNHRDQ SKIDRESREE
     DPTTSETEDI YQSKHRGKMR LSDQKAIALN TFRQKKHSQS RIVSVEKVQS PSTPEHSIEI
     DMGPCRRQVE TLMQEMKLSH RVYPRAFYLP NCDRKGFYKR KQCKPSRGRK RGLCWCVDKY
     GLKLPGIDYV NGDLQCHSFD SSNTE
 
 
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