IBP5_MOUSE
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 03-AUG-2022, entry version 185.
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; Q07079; -.
DR PeptideAtlas; Q07079; -.
DR PRIDE; Q07079; -.
DR ProteomicsDB; 267082; -.
DR Antibodypedia; 3978; 452 antibodies from 38 providers.
DR DNASU; 16011; -.
DR Ensembl; ENSMUST00000027377; ENSMUSP00000027377; ENSMUSG00000026185.
DR GeneID; 16011; -.
DR KEGG; mmu:16011; -.
DR UCSC; uc007bkx.1; mouse.
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; 979270at2759; -.
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 72 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 298 other tissues.
DR ExpressionAtlas; Q07079; baseline and differential.
DR Genevisible; Q07079; MM.
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:0007568; P:aging; IEA:Ensembl.
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 protein kinase B signaling; 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; 4.10.800.10; -; 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_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 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"
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
