IBP1_RAT
ID IBP1_RAT Reviewed; 272 AA.
AC P21743;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, 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 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].
RC TISSUE=Decidua;
RX PubMed=1691820; DOI=10.1210/mend-4-2-329;
RA Murphy L.J., Seneviratne C., Ballejo G., Croze F., Kennedy T.G.;
RT "Identification and characterization of a rat decidual insulin-like growth
RT factor-binding protein complementary DNA.";
RL Mol. Endocrinol. 4:329-336(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=1705004; DOI=10.1128/mcb.11.3.1393-1401.1991;
RA Mohn K.L., Melby A.E., Tewari D.S., Laz T.M., Taub R.A.;
RT "The gene encoding rat insulin-like growth factor-binding protein 1 is
RT rapidly and highly induced in regenerating liver.";
RL Mol. Cell. Biol. 11:1393-1401(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1283442; DOI=10.1210/mend.6.12.1283442;
RA Ooi G.T., Tseng L.Y.H., Tran M.Q., Rechler M.M.;
RT "Insulin rapidly decreases insulin-like growth factor-binding protein-1
RT gene transcription in streptozotocin-diabetic rats.";
RL Mol. Endocrinol. 6:2219-2228(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=7514892; DOI=10.1016/0167-4781(94)90106-6;
RA Lacson R.G., Oehler D., Yang E., Goswami R., Unterman T.G.;
RT "Dideoxy sequencing and structural analysis of the rat insulin-like growth
RT factor binding protein-1 gene.";
RL Biochim. Biophys. Acta 1218:95-98(1994).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 [6]
RP PROTEIN SEQUENCE OF 26-59.
RX PubMed=2164920; DOI=10.1210/endo-127-2-789;
RA Unterman T.G., Oehler D.T., Gotway M.B., Morris P.W.;
RT "Production of the rat type 1 insulin-like growth factor-binding protein by
RT well differentiated H4EIIC3 hepatoma cells: identification, purification,
RT and N-terminal amino acid analysis.";
RL Endocrinology 127:789-797(1990).
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; M58634; AAA41380.1; -; mRNA.
DR EMBL; M89791; AAA41382.1; -; mRNA.
DR EMBL; L22979; AAA82581.1; -; Genomic_DNA.
DR EMBL; BC078889; AAH78889.1; -; mRNA.
DR PIR; A36082; A36082.
DR RefSeq; NP_037276.1; NM_013144.1.
DR AlphaFoldDB; P21743; -.
DR SMR; P21743; -.
DR STRING; 10116.ENSRNOP00000011338; -.
DR MEROPS; I31.951; -.
DR PaxDb; P21743; -.
DR PRIDE; P21743; -.
DR Ensembl; ENSRNOT00000077177; ENSRNOP00000069247; ENSRNOG00000058780.
DR GeneID; 25685; -.
DR KEGG; rno:25685; -.
DR UCSC; RGD:2872; rat.
DR CTD; 3484; -.
DR RGD; 2872; Igfbp1.
DR eggNOG; ENOG502QWRP; Eukaryota.
DR GeneTree; ENSGT00940000157394; -.
DR HOGENOM; CLU_070833_3_0_1; -.
DR InParanoid; P21743; -.
DR OMA; HCAPCTE; -.
DR OrthoDB; 979270at2759; -.
DR PhylomeDB; P21743; -.
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:P21743; -.
DR Proteomes; UP000002494; Chromosome 14.
DR Bgee; ENSRNOG00000058780; Expressed in liver and 7 other tissues.
DR Genevisible; P21743; RN.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0005520; F:insulin-like growth factor binding; ISO: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; ISO:RGD.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0006006; P:glucose metabolic process; TAS:RGD.
DR GO; GO:0008286; P:insulin receptor signaling pathway; IEP:RGD.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; TAS:RGD.
DR GO; GO:0030307; P:positive regulation of cell growth; IEP:RGD.
DR GO; GO:0043567; P:regulation of insulin-like growth factor receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0042246; P:tissue regeneration; IEP:RGD.
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 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Growth factor binding;
KW Phosphoprotein; Reference proteome; Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000269|PubMed:2164920"
FT CHAIN 26..272
FT /note="Insulin-like growth factor-binding protein 1"
FT /id="PRO_0000014368"
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 REGION 115..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 79
FT /note="R -> A (in Ref. 1 and 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 111..112
FT /note="AA -> PP (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 201
FT /note="A -> R (in Ref. 3; AAA41382)"
FT /evidence="ECO:0000305"
FT CONFLICT 265
FT /note="H -> N (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 272 AA; 29684 MW; 12B9F3A42200753D CRC64;
MPEFLTVVSW PFLILLSFQV RVVAGAPQPW HCAPCTAERL ELCPPVPASC PEISRPAGCG
CCPTCALPLG AACGVATARC AQGLSCRALP GEPRPLHALT RGQGACVLEP AAPATSSLSG
SQHEEAKAAV ASEDELAESP EMTEEQLLDS FHLMAPSRED QPILWNAIST YSSMRAREIT
DLKKWKEPCQ RELYKVLERL AAAQQKAGDE IYKFYLPNCN KNGFYHSKQC ETSLDGEAGL
CWCVYPWSGK KIPGSLETRG DPNCHQYFNV QN
