ID   IBP5_MOUSE              Reviewed;         271 AA.
AC   Q07079;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   24-JAN-2024, entry version 193.
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   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   TISSUE=Myoblast;
RX   PubMed=7693664; DOI=10.1016/s0021-9258(18)41529-3;
RA   James P.L., Jones S.B., Busby W.H. Jr., Clemmons D.R., Rotwein P.;
RT   "A highly conserved insulin-like growth factor-binding protein (IGFBP-5) is
RT   expressed during myoblast differentiation.";
RL   J. Biol. Chem. 268:22305-22312(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Spleen;
RX   PubMed=7518410; DOI=10.1006/geno.1994.1195;
RA   Kou K., Jenkins N.A., Gilbert D.J., Copeland N.G., Rotwein P.;
RT   "Organization, expression, and chromosomal location of the mouse insulin-
RT   like growth factor binding protein 5 gene.";
RL   Genomics 20:412-418(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Kidney;
RX   PubMed=7529732; DOI=10.1016/0303-7207(94)90051-5;
RA   Schuller A.G.P., Groffen C., van Neck J.W., Zwarthoff E.C., Drop S.L.S.;
RT   "cDNA cloning and mRNA expression of the six mouse insulin-like growth
RT   factor binding proteins.";
RL   Mol. Cell. Endocrinol. 104:57-66(1994).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Kidney;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
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: Most abundant in kidney, uterus and gastrocnemius
CC       muscle.
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DR   EMBL; L12447; AAC37636.1; -; mRNA.
DR   EMBL; U02025; AAC01750.1; -; Genomic_DNA.
DR   EMBL; U02023; AAC01750.1; JOINED; Genomic_DNA.
DR   EMBL; U02027; AAC01750.1; JOINED; Genomic_DNA.
DR   EMBL; U02024; AAC01750.1; JOINED; Genomic_DNA.
DR   EMBL; X81583; CAA57273.1; -; mRNA.
DR   EMBL; BC054812; AAH54812.1; -; mRNA.
DR   EMBL; BC057447; AAH57447.1; -; mRNA.
DR   CCDS; CCDS15037.1; -.
DR   PIR; I48604; I48604.
DR   RefSeq; NP_034648.2; NM_010518.2.
DR   AlphaFoldDB; Q07079; -.
DR   SMR; Q07079; -.
DR   BioGRID; 200557; 5.
DR   IntAct; Q07079; 1.
DR   STRING; 10090.ENSMUSP00000027377; -.
DR   MEROPS; I31.952; -.
DR   iPTMnet; Q07079; -.
DR   PhosphoSitePlus; Q07079; -.
DR   PaxDb; 10090-ENSMUSP00000027377; -.
DR   PeptideAtlas; Q07079; -.
DR   ProteomicsDB; 267082; -.
DR   Pumba; Q07079; -.
DR   Antibodypedia; 3978; 496 antibodies from 39 providers.
DR   DNASU; 16011; -.
DR   Ensembl; ENSMUST00000027377.9; ENSMUSP00000027377.9; ENSMUSG00000026185.9.
DR   GeneID; 16011; -.
DR   KEGG; mmu:16011; -.
DR   UCSC; uc007bkx.1; mouse.
DR   AGR; MGI:96440; -.
DR   CTD; 3488; -.
DR   MGI; MGI:96440; Igfbp5.
DR   VEuPathDB; HostDB:ENSMUSG00000026185; -.
DR   eggNOG; ENOG502QUPK; Eukaryota.
DR   GeneTree; ENSGT00940000155890; -.
DR   HOGENOM; CLU_070833_1_1_1; -.
DR   InParanoid; Q07079; -.
DR   OMA; YTERCAL; -.
DR   OrthoDB; 5394492at2759; -.
DR   PhylomeDB; Q07079; -.
DR   TreeFam; TF331211; -.
DR   Reactome; R-MMU-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR   Reactome; R-MMU-8957275; Post-translational protein phosphorylation.
DR   BioGRID-ORCS; 16011; 2 hits in 77 CRISPR screens.
DR   ChiTaRS; Igfbp5; mouse.
DR   PRO; PR:Q07079; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   RNAct; Q07079; Protein.
DR   Bgee; ENSMUSG00000026185; Expressed in ciliary body and 299 other cell types or tissues.
DR   ExpressionAtlas; Q07079; baseline and differential.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0016942; C:insulin-like growth factor binding protein complex; IC:MGI.
DR   GO; GO:0042567; C:insulin-like growth factor ternary complex; ISS:BHF-UCL.
DR   GO; GO:0001968; F:fibronectin binding; IDA:MGI.
DR   GO; GO:0005520; F:insulin-like growth factor binding; IPI:MGI.
DR   GO; GO:0031994; F:insulin-like growth factor I binding; ISO:MGI.
DR   GO; GO:0031995; F:insulin-like growth factor II binding; IBA:GO_Central.
DR   GO; GO:0071320; P:cellular response to cAMP; ISO:MGI.
DR   GO; GO:0071407; P:cellular response to organic cyclic compound; ISO:MGI.
DR   GO; GO:0007565; P:female pregnancy; IMP:BHF-UCL.
DR   GO; GO:0042593; P:glucose homeostasis; IMP:MGI.
DR   GO; GO:0031069; P:hair follicle morphogenesis; IMP:MGI.
DR   GO; GO:0048009; P:insulin-like growth factor receptor signaling pathway; IMP:MGI.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:Ensembl.
DR   GO; GO:0048286; P:lung alveolus development; IMP:BHF-UCL.
DR   GO; GO:0060056; P:mammary gland involution; IMP:MGI.
DR   GO; GO:0030336; P:negative regulation of cell migration; ISO:MGI.
DR   GO; GO:0045926; P:negative regulation of growth; IMP:BHF-UCL.
DR   GO; GO:0043569; P:negative regulation of insulin-like growth factor receptor signaling pathway; IMP:MGI.
DR   GO; GO:1901862; P:negative regulation of muscle tissue development; IMP:BHF-UCL.
DR   GO; GO:0045668; P:negative regulation of osteoblast differentiation; IGI:MGI.
DR   GO; GO:1904205; P:negative regulation of skeletal muscle hypertrophy; IMP:BHF-UCL.
DR   GO; GO:0014912; P:negative regulation of smooth muscle cell migration; ISO:MGI.
DR   GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; ISO:MGI.
DR   GO; GO:0017148; P:negative regulation of translation; ISO:MGI.
DR   GO; GO:0001649; P:osteoblast differentiation; IEP:BHF-UCL.
DR   GO; GO:0043568; P:positive regulation of insulin-like growth factor receptor signaling pathway; IGI:MGI.
DR   GO; GO:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IMP:MGI.
DR   GO; GO:1904754; P:positive regulation of vascular associated smooth muscle cell migration; ISO:MGI.
DR   GO; GO:1904707; P:positive regulation of vascular associated smooth muscle cell proliferation; ISO:MGI.
DR   GO; GO:0001558; P:regulation of cell growth; IGI:MGI.
DR   GO; GO:0040008; P:regulation of growth; IGI:MGI.
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; IMP:MGI.
DR   GO; GO:0044342; P:type B pancreatic cell proliferation; IGI:MGI.
DR   CDD; cd00191; TY; 1.
DR   Gene3D; 4.10.40.20; -; 1.
DR   Gene3D; 4.10.800.10; Thyroglobulin type-1; 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; INSULIN-LIKE GROWTH FACTOR BINDING PROTEIN; 1.
DR   PANTHER; PTHR11551:SF4; INSULIN-LIKE GROWTH FACTOR-BINDING PROTEIN 5; 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; Growth factor receptor domain; 1.
DR   SUPFAM; SSF57610; Thyroglobulin type-1 domain; 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.
DR   Genevisible; Q07079; MM.
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_0000014386"
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        26..52
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT   DISULFID        29..54
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT   DISULFID        37..55
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT   DISULFID        44..58
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT   DISULFID        66..79
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT   DISULFID        73..99
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
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"
FT   CONFLICT        112
FT                   /note="Missing (in Ref. 2; AAC01750)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   271 AA;  30372 MW;  F55A58729861F6F0 CRC64;
     MVISVVLLLL AAYAVPAQGL GSFVHCEPCD EKALSMCPPS PLGCELVKEP GCGCCMTCAL
     AEGQSCGVYT ERCAQGLRCL PRQDEEKPLH ALLHGRGVCL NEKSYGEQTK IERDSREHEE
     PTTSEMAEET YSPKVFRPKH TRISELKAEA VKKDRRKKLT QSKFVGGAEN TAHPRVIPAP
     EMRQESEQGP CRRHMEASLQ EFKASPRMVP RAVYLPNCDR KGFYKRKQCK PSRGRKRGIC
     WCVDKYGMKL PGMEYVDGDF QCHAFDSSNV E
//