IBP1_BOVIN
ID IBP1_BOVIN Reviewed; 263 AA.
AC P24591; Q2T9Z3;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 141.
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 AltName: Full=bIGFBP-1;
DE Flags: Precursor;
GN Name=IGFBP1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Holstein-Friesian; TISSUE=Liver;
RX PubMed=1722724; DOI=10.3109/10425179109020798;
RA Sneyers M., Kettmann R., Massart S., Renaville R., Burny A., Portetelle D.;
RT "Cloning and characterization of a cDNA encoding the bovine insulin-like
RT growth factor binding protein 1 (bIGFBP-1).";
RL DNA Seq. 1:407-408(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
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; X54979; CAA38723.1; -; mRNA.
DR EMBL; BC111197; AAI11198.1; -; mRNA.
DR PIR; S23009; S23009.
DR RefSeq; NP_776979.2; NM_174554.3.
DR AlphaFoldDB; P24591; -.
DR SMR; P24591; -.
DR STRING; 9913.ENSBTAP00000055280; -.
DR MEROPS; I31.951; -.
DR PaxDb; P24591; -.
DR PRIDE; P24591; -.
DR Ensembl; ENSBTAT00000064194; ENSBTAP00000055280; ENSBTAG00000046768.
DR GeneID; 282259; -.
DR KEGG; bta:282259; -.
DR CTD; 3484; -.
DR VEuPathDB; HostDB:ENSBTAG00000046768; -.
DR VGNC; VGNC:30083; IGFBP1.
DR eggNOG; ENOG502QWRP; Eukaryota.
DR GeneTree; ENSGT00940000157394; -.
DR HOGENOM; CLU_070833_3_0_1; -.
DR InParanoid; P24591; -.
DR OMA; HCAPCTE; -.
DR OrthoDB; 979270at2759; -.
DR TreeFam; TF331211; -.
DR Reactome; R-BTA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-BTA-8957275; Post-translational protein phosphorylation.
DR Proteomes; UP000009136; Chromosome 4.
DR Bgee; ENSBTAG00000046768; Expressed in liver and 38 other tissues.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0031994; F:insulin-like growth factor I binding; IBA:GO_Central.
DR GO; GO:0031995; F:insulin-like growth factor II binding; IBA:GO_Central.
DR GO; GO:0043567; P:regulation of insulin-like growth factor receptor signaling pathway; IBA:GO_Central.
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 CHAIN 26..263
FT /note="Insulin-like growth factor-binding protein 1"
FT /id="PRO_0000014364"
FT DOMAIN 28..109
FT /note="IGFBP N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT DOMAIN 177..255
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT REGION 102..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 250..252
FT /note="Cell attachment site"
FT COMPBIAS 104..131
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 122
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08833"
FT MOD_RES 127
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08833"
FT MOD_RES 130
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08833"
FT MOD_RES 148
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08833"
FT MOD_RES 160
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08833"
FT MOD_RES 162
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P08833"
FT MOD_RES 246
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 180..210
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 221..232
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 234..255
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT CONFLICT 109..111
FT /note="TPS -> SPC (in Ref. 1; CAA38723)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 263 AA; 28794 MW; 10E25A72F8BC23B7 CRC64;
MPEVLAVRAW PLLLSLAVQL GATVGAPQPW RCAPCSAERM ALCPPVPASC PELTRSAGCG
CCPMCALPLG AACGVATARC ARGLSCRALP GEPRPLHALT RGQGACMTTP SDEATDTKDT
TSPENVSPES SEITQEQLLD NFHLMAESSE DLPILWNAIS NYESLRALEI SDVKKWKEPC
QRELYKVLDR LAREQQKAGD KLYKFYLPNC NKNGFYHSKQ CETSLEGEPG LCWCVYPWSG
KRILGSVAVR GDPKCQQYFN LQN
