IBP1_MOUSE
ID IBP1_MOUSE Reviewed; 272 AA.
AC P47876; Q5SVY8; Q61732;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Insulin-like growth factor-binding protein 1;
DE Short=IBP-1;
DE Short=IGF-binding protein 1;
DE Short=IGFBP-1;
DE Flags: Precursor;
GN Name=Igfbp1; Synonyms=Igfbp-1;
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].
RC TISSUE=Liver;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-124.
RC STRAIN=NIH Swiss;
RX PubMed=7509771; DOI=10.1002/hep.1840190317;
RA Lee J., Greenbaum L., Haber B.A., Nagle D., Lee V., Miles V., Mohn K.L.,
RA Bucan M., Taub R.;
RT "Structure and localization of the IGFBP-1 gene and its expression during
RT liver regeneration.";
RL Hepatology 19:656-665(1994).
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 cell migration (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Binds equally well IGF1 and IGF2.
CC -!- SUBCELLULAR LOCATION: Secreted.
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DR EMBL; X81579; CAA57269.1; -; mRNA.
DR EMBL; AL607124; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466574; EDL40608.1; -; Genomic_DNA.
DR EMBL; X67493; CAA47832.1; -; Genomic_DNA.
DR CCDS; CCDS24427.1; -.
DR PIR; I48600; I48600.
DR PIR; S25113; S25113.
DR RefSeq; NP_032367.3; NM_008341.4.
DR AlphaFoldDB; P47876; -.
DR SMR; P47876; -.
DR DIP; DIP-60631N; -.
DR IntAct; P47876; 2.
DR STRING; 10090.ENSMUSP00000020704; -.
DR MEROPS; I31.951; -.
DR iPTMnet; P47876; -.
DR PhosphoSitePlus; P47876; -.
DR PaxDb; P47876; -.
DR PeptideAtlas; P47876; -.
DR PRIDE; P47876; -.
DR ProteomicsDB; 273250; -.
DR Antibodypedia; 3841; 685 antibodies from 39 providers.
DR DNASU; 16006; -.
DR Ensembl; ENSMUST00000020704; ENSMUSP00000020704; ENSMUSG00000020429.
DR GeneID; 16006; -.
DR KEGG; mmu:16006; -.
DR UCSC; uc007hzh.2; mouse.
DR CTD; 3484; -.
DR MGI; MGI:96436; Igfbp1.
DR VEuPathDB; HostDB:ENSMUSG00000020429; -.
DR eggNOG; ENOG502QWRP; Eukaryota.
DR GeneTree; ENSGT00940000157394; -.
DR HOGENOM; CLU_070833_3_0_1; -.
DR InParanoid; P47876; -.
DR OMA; HCAPCTE; -.
DR OrthoDB; 979270at2759; -.
DR PhylomeDB; P47876; -.
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; 16006; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Igfbp1; mouse.
DR PRO; PR:P47876; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P47876; protein.
DR Bgee; ENSMUSG00000020429; Expressed in left lobe of liver and 38 other tissues.
DR Genevisible; P47876; MM.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO: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; ISO:MGI.
DR GO; GO:0007568; P:aging; IEA:Ensembl.
DR GO; GO:0008286; P:insulin receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0030307; P:positive regulation of cell growth; IEA:Ensembl.
DR GO; GO:0043567; P:regulation of insulin-like growth factor receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0042246; P:tissue regeneration; IEA:Ensembl.
DR CDD; cd00191; TY; 1.
DR Gene3D; 4.10.800.10; -; 1.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR000867; IGFBP-like.
DR InterPro; IPR022322; IGFBP1.
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; PR01977; IGFBPFAMILY1.
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 Disulfide bond; Growth factor binding; Phosphoprotein; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000250"
FT CHAIN 26..272
FT /note="Insulin-like growth factor-binding protein 1"
FT /id="PRO_0000014366"
FT DOMAIN 28..109
FT /note="IGFBP N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT DOMAIN 186..264
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT MOTIF 259..261
FT /note="Cell attachment site"
FT MOD_RES 139
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08833"
FT MOD_RES 157
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08833"
FT MOD_RES 169
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08833"
FT MOD_RES 170
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P08833"
FT MOD_RES 171
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P08833"
FT MOD_RES 255
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08833"
FT DISULFID 73..86
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 80..106
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 189..219
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 230..241
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 243..264
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT CONFLICT 23
FT /note="A -> V (in Ref. 1; CAA57269)"
FT /evidence="ECO:0000305"
FT CONFLICT 106..107
FT /note="CV -> SL (in Ref. 4; CAA47832)"
FT /evidence="ECO:0000305"
FT CONFLICT 229
FT /note="Q -> E (in Ref. 1; CAA57269)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 272 AA; 29570 MW; CD4FCD3C5AB69B60 CRC64;
MPEFLTVVSW PFLILLSFQI GVAAGAPQPW HCAPCTAERL GLCPPVPASC PEISRPAGCG
CCPTCALPMG AACGVATARC AQGLSCRALP GEPRPLHALT RGQGACVPEP AAPATSTLFS
SQHEEAKAAV VSADELSESP EMTEEQLLDS FHLMAPSRED QPILWNAIST YSSMRAREIA
DLKKWKEPCQ RELYKVLERL AAAQQKAGDE IYKFYLPNCN KNGFYHSKQC ETSLDGEAGL
CWCVYPWSGK KIPGSLETRG DPNCHQYFNV HN
