ID   IBP6_RAT                Reviewed;         226 AA.
AC   P35572; Q499W1;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   03-AUG-2022, entry version 158.
DE   RecName: Full=Insulin-like growth factor-binding protein 6;
DE            Short=IBP-6;
DE            Short=IGF-binding protein 6;
DE            Short=IGFBP-6;
DE   Flags: Precursor;
GN   Name=Igfbp6; Synonyms=Igfbp-6;
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].
RX   PubMed=1719383; DOI=10.1210/mend-5-7-938;
RA   Shimasaki S., Gao L., Shimonaka M., Ling N.;
RT   "Isolation and molecular cloning of insulin-like growth factor-binding
RT   protein-6.";
RL   Mol. Endocrinol. 5:938-948(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Sprague-Dawley;
RX   PubMed=7682065; DOI=10.1006/bbrc.1993.1350;
RA   Zhu X., Ling N., Shimasaki S.;
RT   "Structural characterization of the rat insulin-like growth factor binding
RT   protein-6 gene.";
RL   Biochem. Biophys. Res. Commun. 191:1237-1243(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Prostate;
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   [4]
RP   PROTEIN SEQUENCE OF 26-38.
RX   PubMed=1709938; DOI=10.1016/s0021-9258(18)99272-0;
RA   Shimasaki S., Shimonaka M., Zhang H.-P., Ling N.;
RT   "Identification of five different insulin-like growth factor binding
RT   proteins (IGFBPs) from adult rat serum and molecular cloning of a novel
RT   IGFBP-5 in rat and human.";
RL   J. Biol. Chem. 266:10646-10653(1991).
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. Activates the MAPK signaling pathway
CC       and induces cell migration. {ECO:0000250|UniProtKB:P24592}.
CC   -!- SUBUNIT: Interacts (via C-terminal domain) with PHB2.
CC       {ECO:0000250|UniProtKB:P24592}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- PTM: O-glycosylated.
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DR   EMBL; M69055; AAA42019.1; -; mRNA.
DR   EMBL; L11006; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC099742; AAH99742.1; -; mRNA.
DR   PIR; JN0464; JN0464.
DR   RefSeq; NP_037236.1; NM_013104.3.
DR   AlphaFoldDB; P35572; -.
DR   SMR; P35572; -.
DR   STRING; 10116.ENSRNOP00000014807; -.
DR   MEROPS; I31.952; -.
DR   PaxDb; P35572; -.
DR   Ensembl; ENSRNOT00000014807; ENSRNOP00000014807; ENSRNOG00000010977.
DR   GeneID; 25641; -.
DR   KEGG; rno:25641; -.
DR   CTD; 3489; -.
DR   RGD; 2877; Igfbp6.
DR   eggNOG; ENOG502QV3Q; Eukaryota.
DR   GeneTree; ENSGT00940000160528; -.
DR   HOGENOM; CLU_070833_1_0_1; -.
DR   InParanoid; P35572; -.
DR   OMA; CVDELGA; -.
DR   OrthoDB; 979270at2759; -.
DR   PhylomeDB; P35572; -.
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   PRO; PR:P35572; -.
DR   Proteomes; UP000002494; Chromosome 7.
DR   Bgee; ENSRNOG00000010977; Expressed in esophagus and 20 other tissues.
DR   Genevisible; P35572; RN.
DR   GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR   GO; GO:0005615; C:extracellular space; IDA:RGD.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:RGD.
DR   GO; GO:0042568; C:insulin-like growth factor binary complex; ISO:RGD.
DR   GO; GO:0001968; F:fibronectin binding; IBA:GO_Central.
DR   GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR   GO; GO:0031994; F:insulin-like growth factor I binding; IPI:RGD.
DR   GO; GO:0031995; F:insulin-like growth factor II binding; IPI:RGD.
DR   GO; GO:0016477; P:cell migration; ISS:UniProtKB.
DR   GO; GO:0043410; P:positive regulation of MAPK cascade; ISS:UniProtKB.
DR   GO; GO:0032874; P:positive regulation of stress-activated MAPK cascade; ISO:RGD.
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; IPR022326; IGFBP-6.
DR   InterPro; IPR000867; IGFBP-like.
DR   InterPro; IPR022321; IGFBP_1-6_chordata.
DR   InterPro; IPR000716; Thyroglobulin_1.
DR   InterPro; IPR036857; Thyroglobulin_1_sf.
DR   PANTHER; PTHR11551:SF14; PTHR11551:SF14; 1.
DR   Pfam; PF00219; IGFBP; 1.
DR   Pfam; PF00086; Thyroglobulin_1; 1.
DR   PRINTS; PR01976; IGFBPFAMILY.
DR   PRINTS; PR01982; IGFBPFAMILY6.
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   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein;
KW   Growth factor binding; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000269|PubMed:1709938"
FT   CHAIN           26..226
FT                   /note="Insulin-like growth factor-binding protein 6"
FT                   /id="PRO_0000014391"
FT   DOMAIN          26..99
FT                   /note="IGFBP N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT   DOMAIN          145..220
FT                   /note="Thyroglobulin type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT   REGION          92..148
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          205..226
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        101..129
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        211..226
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        30..33
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT   DISULFID        49..55
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT   DISULFID        63..76
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT   DISULFID        70..96
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT   DISULFID        148..176
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT   DISULFID        187..198
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT   DISULFID        200..220
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
SQ   SEQUENCE   226 AA;  24193 MW;  212D419303AE3137 CRC64;
     MTWDGLPTQP LLMLLMLLFA AGSESALAGC PGCGPGVQEE DAGSPADGCA ETGGCFRREG
     QPCGVYIPKC APGLQCQPRE NEETPLRALL IGQGRCQRAR GPSEETTKES KPHGGASRPR
     DRDRQKNPRT SAAPIRPSPV QDGEMGPCRR HLDSVLQQLQ TEVFRGGANG LYVPNCDLRG
     FYRKQQCRSS QGNRRGPCWC VDPMGQPLPV SPDGQGSSQC SARSSG