IBP5_RAT
ID IBP5_RAT Reviewed; 271 AA.
AC P24594;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 03-AUG-2022, entry version 173.
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 Flags: Precursor;
GN Name=Igfbp5; Synonyms=Igfbp-5;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 20-53.
RC TISSUE=Ovary;
RX PubMed=1709938; DOI=10.1016/s0021-9258(18)99272-0;
RA Shimasaki S., Shimonaka M., Zhang H.-P., Ling N.;
RT "Identification of five different insulin-like growth factor binding
RT proteins (IGFBPs) from adult rat serum and molecular cloning of a novel
RT IGFBP-5 in rat and human.";
RL J. Biol. Chem. 266:10646-10653(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Sprague-Dawley;
RX PubMed=7679898; DOI=10.1006/bbrc.1993.1154;
RA Zhu X., Ling N., Shimasaki S.;
RT "Cloning of the rat insulin-like growth factor binding protein-5 gene and
RT DNA sequence analysis of its promoter region.";
RL Biochem. Biophys. Res. Commun. 190:1045-1052(1993).
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.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Mostly in kidney.
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DR EMBL; M62781; AAA53533.1; -; mRNA.
DR EMBL; L08275; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; JC1463; JC1463.
DR RefSeq; NP_036949.1; NM_012817.1.
DR AlphaFoldDB; P24594; -.
DR SMR; P24594; -.
DR MINT; P24594; -.
DR STRING; 10116.ENSRNOP00000023530; -.
DR MEROPS; I31.952; -.
DR iPTMnet; P24594; -.
DR PhosphoSitePlus; P24594; -.
DR PaxDb; P24594; -.
DR PRIDE; P24594; -.
DR Ensembl; ENSRNOT00000023530; ENSRNOP00000023530; ENSRNOG00000017206.
DR GeneID; 25285; -.
DR KEGG; rno:25285; -.
DR UCSC; RGD:2876; rat.
DR CTD; 3488; -.
DR RGD; 2876; Igfbp5.
DR eggNOG; ENOG502QUPK; Eukaryota.
DR GeneTree; ENSGT00940000155890; -.
DR InParanoid; P24594; -.
DR OMA; YTERCAL; -.
DR OrthoDB; 979270at2759; -.
DR PhylomeDB; P24594; -.
DR TreeFam; TF331211; -.
DR Reactome; R-RNO-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-RNO-8957275; Post-translational protein phosphorylation.
DR PRO; PR:P24594; -.
DR Proteomes; UP000002494; Chromosome 9.
DR Bgee; ENSRNOG00000017206; Expressed in esophagus and 19 other tissues.
DR ExpressionAtlas; P24594; baseline and differential.
DR Genevisible; P24594; RN.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0042567; C:insulin-like growth factor ternary complex; ISO:RGD.
DR GO; GO:0001968; F:fibronectin binding; ISO:RGD.
DR GO; GO:0005520; F:insulin-like growth factor binding; IDA:RGD.
DR GO; GO:0031994; F:insulin-like growth factor I binding; ISO:RGD.
DR GO; GO:0031995; F:insulin-like growth factor II binding; IBA:GO_Central.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0071320; P:cellular response to cAMP; ISO:RGD.
DR GO; GO:0071407; P:cellular response to organic cyclic compound; ISO:RGD.
DR GO; GO:0007565; P:female pregnancy; ISO:RGD.
DR GO; GO:0042593; P:glucose homeostasis; ISO:RGD.
DR GO; GO:0031069; P:hair follicle morphogenesis; ISO:RGD.
DR GO; GO:0048009; P:insulin-like growth factor receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0035556; P:intracellular signal transduction; IEP:RGD.
DR GO; GO:0048286; P:lung alveolus development; ISO:RGD.
DR GO; GO:0060056; P:mammary gland involution; ISO:RGD.
DR GO; GO:0030336; P:negative regulation of cell migration; ISO:RGD.
DR GO; GO:0045926; P:negative regulation of growth; ISO:RGD.
DR GO; GO:0043569; P:negative regulation of insulin-like growth factor receptor signaling pathway; ISO:RGD.
DR GO; GO:1901862; P:negative regulation of muscle tissue development; ISO:RGD.
DR GO; GO:0045668; P:negative regulation of osteoblast differentiation; ISO:RGD.
DR GO; GO:1904205; P:negative regulation of skeletal muscle hypertrophy; ISO:RGD.
DR GO; GO:0014912; P:negative regulation of smooth muscle cell migration; ISO:RGD.
DR GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; ISO:RGD.
DR GO; GO:0017148; P:negative regulation of translation; ISO:RGD.
DR GO; GO:0001649; P:osteoblast differentiation; ISO:RGD.
DR GO; GO:0043568; P:positive regulation of insulin-like growth factor receptor signaling pathway; ISO:RGD.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISO:RGD.
DR GO; GO:1904754; P:positive regulation of vascular associated smooth muscle cell migration; ISO:RGD.
DR GO; GO:1904707; P:positive regulation of vascular associated smooth muscle cell proliferation; ISO:RGD.
DR GO; GO:0001558; P:regulation of cell growth; ISO:RGD.
DR GO; GO:0040008; P:regulation of growth; ISO:RGD.
DR GO; GO:0043567; P:regulation of insulin-like growth factor receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0060416; P:response to growth hormone; ISS:AgBase.
DR GO; GO:0051146; P:striated muscle cell differentiation; ISO:RGD.
DR GO; GO:0044342; P:type B pancreatic cell proliferation; ISO:RGD.
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 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Growth factor binding;
KW Phosphoprotein; Reference proteome; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..271
FT /note="Insulin-like growth factor-binding protein 5"
FT /id="PRO_0000014388"
FT DOMAIN 22..102
FT /note="IGFBP N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT DOMAIN 188..262
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT REGION 109..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..125
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 115
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P24593"
FT DISULFID 44..58
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 66..79
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 191..218
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 229..240
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 242..262
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
SQ SEQUENCE 271 AA; 30298 MW; 545B4C48F9BB5493 CRC64;
MVISVVLLLL AACAVPAQGL GSFVHCEPCD EKALSMCPPS PLGCELVKEP GCGCCMTCAL
AEGQSCGVYT ERCAQGLRCL PRQDEEKPLH ALLHGRGVCL NEKSYGEQTK IERDSREHEE
PTTSEMAEET YSPKVFRPKH TRISELKAEA VKKDRRKKLT QSKFVGGAEN TAHPRVIPAP
EMRQESDQGP CRRHMEASLQ EFKASPRMVP RAVYLPNCDR KGFYKRKQCK PSRGRKRGIC
WCVDKYGMKL PGMEYVDGDF QCHAFDSSNV E
