ID   IBP1_ICTTR              Reviewed;         272 AA.
AC   Q6Q484;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 81.
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   Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS   tridecemlineatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC   Xerinae; Marmotini; Ictidomys.
OX   NCBI_TaxID=43179;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Li Y., Klimanis D., Hallenbeck J.M.;
RT   "Cloning and characterization of insulin-like growth factor binding protein
RT   1 (IGFBP-1) from thirteen-lined ground squirrel.";
RL   Submitted (FEB-2004) 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. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
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DR   EMBL; AY560836; AAS67029.1; -; mRNA.
DR   AlphaFoldDB; Q6Q484; -.
DR   SMR; Q6Q484; -.
DR   STRING; 43179.ENSSTOP00000007832; -.
DR   eggNOG; ENOG502QWRP; Eukaryota.
DR   InParanoid; Q6Q484; -.
DR   Proteomes; UP000005215; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005520; F:insulin-like growth factor binding; IEA:InterPro.
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_0000250501"
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        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"
SQ   SEQUENCE   272 AA;  29814 MW;  DE32A10BA23FF949 CRC64;
     MPEVPAAGLW PFLLLLAVQV STVASSTQPW HCAPCSAEKL ALCPPVPSSC PELSRPAGCG
     CCPMCALPLG AACGVATARY ARGLSCRALP GEPRPLHALT RGQGACVPEP ATPTASGLSS
     IEKEEAKASM VPERVPPESA EMTEEQLLES FHLMASSSED QPILWNAIST YKSMRAREMA
     DIKKWKQPCR RELYKVLERL AKAQQKAGEE IYKFYLPNCN KNGFYHSKQC ETSLDGEAEL
     CWCVYPWSGR RIPGSLEIRG DPNCHQYFNV QN