ID   IBP1_PIG                Reviewed;         262 AA.
AC   Q75ZP3;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 87.
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;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=15859522; DOI=10.1007/s10528-005-1069-1;
RA   Inage-Miyake Y., Shimanuki S., Itoh T., Murakami Y., Kimura M., Suzuki H.,
RA   Miyake M., Toki D., Uenishi H., Awata T., Hamasima N.;
RT   "Assignment of the gene for porcine insulin-like growth factor binding
RT   protein 1 to chromosome 18 and detection of polymorphisms in intron 2 by
RT   PCR-RFLP.";
RL   Biochem. Genet. 43:79-85(2005).
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. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
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DR   EMBL; AB119126; BAC84982.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q75ZP3; -.
DR   SMR; Q75ZP3; -.
DR   STRING; 9823.ENSSSCP00000017718; -.
DR   PaxDb; Q75ZP3; -.
DR   eggNOG; ENOG502QWRP; Eukaryota.
DR   InParanoid; Q75ZP3; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
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; IPR000716; Thyroglobulin_1.
DR   InterPro; IPR036857; Thyroglobulin_1_sf.
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; PS51323; IGFBP_N_2; 1.
DR   PROSITE; PS00484; THYROGLOBULIN_1_1; 1.
DR   PROSITE; PS51162; THYROGLOBULIN_1_2; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Growth factor binding; Phosphoprotein; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..262
FT                   /note="Insulin-like growth factor-binding protein 1"
FT                   /id="PRO_0000014367"
FT   DOMAIN          28..108
FT                   /note="IGFBP N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT   DOMAIN          176..254
FT                   /note="Thyroglobulin type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT   REGION          101..133
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           249..251
FT                   /note="Cell attachment site"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        119..133
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         126
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P08833"
FT   MOD_RES         129
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P08833"
FT   MOD_RES         147
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P08833"
FT   MOD_RES         161
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P08833"
FT   MOD_RES         245
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P08833"
FT   DISULFID        72..85
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT   DISULFID        79..105
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT   DISULFID        179..209
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT   DISULFID        220..231
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT   DISULFID        233..254
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
SQ   SEQUENCE   262 AA;  28331 MW;  C811AB73192219C8 CRC64;
     MPEVPAVRAW PLLLSLALQL GAAAGAPQPL HCAPCSAERL ALCPPVPASC PEATRPAGCG
     CCPTCALPLG ACGVATARCA RGLSCRALPG EPRPLHALTR GQGACMPAPS AEATETKDPA
     APETTSPEST EMTQEQLLDS FHLMATSSED LPILWNAINN YESMKALEAT DIKKWKEPCQ
     RELYKVLDRL AREQQKAGDR LYKFYLPNCN KNGFYHSKQC ETSLEGEPGL CWCVYPWSGK
     KILGSTAVRG DPKCHQYFNS QN