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Insulin-like growth factor-binding protein 1 (IBP-1) (IGF-binding protein 1) (IGFBP-1)

 IBP1_MOUSE              Reviewed;         272 AA.
P47876; Q5SVY8; Q61732;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
03-OCT-2012, sequence version 2.
07-JUN-2017, entry version 141.
RecName: Full=Insulin-like growth factor-binding protein 1;
Short=IBP-1;
Short=IGF-binding protein 1;
Short=IGFBP-1;
Flags: Precursor;
Name=Igfbp1; Synonyms=Igfbp-1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
PubMed=7529732; DOI=10.1016/0303-7207(94)90051-5;
Schuller A.G.P., Groffen C., van Neck J.W., Zwarthoff E.C.,
Drop S.L.S.;
"cDNA cloning and mRNA expression of the six mouse insulin-like growth
factor binding proteins.";
Mol. Cell. Endocrinol. 104:57-66(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-124.
STRAIN=NIH Swiss;
PubMed=7509771; DOI=10.1002/hep.1840190317;
Lee J., Greenbaum L., Haber B.A., Nagle D., Lee V., Miles V.,
Mohn K.L., Bucan M., Taub R.;
"Structure and localization of the IGFBP-1 gene and its expression
during liver regeneration.";
Hepatology 19:656-665(1994).
-!- FUNCTION: IGF-binding proteins prolong the half-life of the IGFs
and have been shown to either inhibit or stimulate the growth
promoting effects of the IGFs on cell culture. They alter the
interaction of IGFs with their cell surface receptors. Promotes
cell migration (By similarity). {ECO:0000250}.
-!- SUBUNIT: Binds equally well IGF1 and IGF2.
-!- SUBCELLULAR LOCATION: Secreted.
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EMBL; X81579; CAA57269.1; -; mRNA.
EMBL; AL607124; CAI24501.1; -; Genomic_DNA.
EMBL; CH466574; EDL40608.1; -; Genomic_DNA.
EMBL; X67493; CAA47832.1; -; Genomic_DNA.
CCDS; CCDS24427.1; -.
PIR; I48600; I48600.
PIR; S25113; S25113.
RefSeq; NP_032367.3; NM_008341.4.
UniGene; Mm.21300; -.
ProteinModelPortal; P47876; -.
SMR; P47876; -.
DIP; DIP-60631N; -.
STRING; 10090.ENSMUSP00000020704; -.
MEROPS; I31.951; -.
iPTMnet; P47876; -.
PhosphoSitePlus; P47876; -.
PaxDb; P47876; -.
PeptideAtlas; P47876; -.
PRIDE; P47876; -.
Ensembl; ENSMUST00000020704; ENSMUSP00000020704; ENSMUSG00000020429.
GeneID; 16006; -.
KEGG; mmu:16006; -.
UCSC; uc007hzh.2; mouse.
CTD; 3484; -.
MGI; MGI:96436; Igfbp1.
eggNOG; ENOG410IITJ; Eukaryota.
eggNOG; ENOG4111H9A; LUCA.
GeneTree; ENSGT00550000074457; -.
HOGENOM; HOG000253012; -.
HOVERGEN; HBG002631; -.
InParanoid; P47876; -.
OMA; GLCWCVY; -.
OrthoDB; EOG091G0EIN; -.
TreeFam; TF331211; -.
Reactome; R-MMU-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
Reactome; R-MMU-8957275; Post-translational protein phosphorylation.
PRO; PR:P47876; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000020429; -.
CleanEx; MM_IGFBP1; -.
Genevisible; P47876; MM.
GO; GO:0005615; C:extracellular space; IDA:MGI.
GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
GO; GO:0005520; F:insulin-like growth factor binding; IPI:MGI.
GO; GO:0031994; F:insulin-like growth factor I binding; ISO:MGI.
GO; GO:0031995; F:insulin-like growth factor II binding; ISO:MGI.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0008286; P:insulin receptor signaling pathway; IEA:Ensembl.
GO; GO:0030307; P:positive regulation of cell growth; IEA:Ensembl.
GO; GO:0043567; P:regulation of insulin-like growth factor receptor signaling pathway; IBA:GO_Central.
GO; GO:0042246; P:tissue regeneration; IEA:Ensembl.
Gene3D; 4.10.800.10; -; 1.
InterPro; IPR009030; Growth_fac_rcpt_.
InterPro; IPR000867; IGFBP-like.
InterPro; IPR022322; IGFBP1.
InterPro; IPR009168; IGFBP1-6.
InterPro; IPR022321; IGFBP_1-6_chordata.
InterPro; IPR017891; Insulin_GF-bd_Cys-rich_CS.
InterPro; IPR000716; Thyroglobulin_1.
PANTHER; PTHR11551; PTHR11551; 1.
Pfam; PF00219; IGFBP; 1.
Pfam; PF00086; Thyroglobulin_1; 1.
PRINTS; PR01976; IGFBPFAMILY.
PRINTS; PR01977; IGFBPFAMILY1.
SMART; SM00121; IB; 1.
SMART; SM00211; TY; 1.
SUPFAM; SSF57184; SSF57184; 1.
SUPFAM; SSF57610; SSF57610; 1.
PROSITE; PS00222; IGFBP_N_1; 1.
PROSITE; PS51323; IGFBP_N_2; 1.
PROSITE; PS00484; THYROGLOBULIN_1_1; 1.
PROSITE; PS51162; THYROGLOBULIN_1_2; 1.
2: Evidence at transcript level;
Complete proteome; Disulfide bond; Growth factor binding;
Phosphoprotein; Reference proteome; Secreted; Signal.
SIGNAL 1 25 {ECO:0000250}.
CHAIN 26 272 Insulin-like growth factor-binding
protein 1.
/FTId=PRO_0000014366.
DOMAIN 28 109 IGFBP N-terminal. {ECO:0000255|PROSITE-
ProRule:PRU00653}.
DOMAIN 186 264 Thyroglobulin type-1.
{ECO:0000255|PROSITE-ProRule:PRU00500}.
MOTIF 259 261 Cell attachment site.
MOD_RES 139 139 Phosphoserine.
{ECO:0000250|UniProtKB:P08833}.
MOD_RES 157 157 Phosphoserine.
{ECO:0000250|UniProtKB:P08833}.
MOD_RES 169 169 Phosphoserine.
{ECO:0000250|UniProtKB:P08833}.
MOD_RES 170 170 Phosphothreonine.
{ECO:0000250|UniProtKB:P08833}.
MOD_RES 171 171 Phosphotyrosine.
{ECO:0000250|UniProtKB:P08833}.
MOD_RES 255 255 Phosphoserine.
{ECO:0000250|UniProtKB:P08833}.
DISULFID 73 86 {ECO:0000255|PROSITE-ProRule:PRU00500}.
DISULFID 80 106 {ECO:0000255|PROSITE-ProRule:PRU00500}.
DISULFID 189 219 {ECO:0000255|PROSITE-ProRule:PRU00500}.
DISULFID 230 241 {ECO:0000255|PROSITE-ProRule:PRU00500}.
DISULFID 243 264 {ECO:0000255|PROSITE-ProRule:PRU00500}.
CONFLICT 23 23 A -> V (in Ref. 1; CAA57269).
{ECO:0000305}.
CONFLICT 106 107 CV -> SL (in Ref. 4; CAA47832).
{ECO:0000305}.
CONFLICT 229 229 Q -> E (in Ref. 1; CAA57269).
{ECO:0000305}.
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


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