IBP6_MOUSE
ID IBP6_MOUSE Reviewed; 238 AA.
AC P47880; Q91X24;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 166.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=7529732; DOI=10.1016/0303-7207(94)90051-5;
RA Schuller A.G.P., Groffen C., van Neck J.W., Zwarthoff E.C., Drop S.L.S.;
RT "cDNA cloning and mRNA expression of the six mouse insulin-like growth
RT factor binding proteins.";
RL Mol. Cell. Endocrinol. 104:57-66(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon;
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).
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; X81584; CAA57274.1; -; mRNA.
DR EMBL; AC110512; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC123791; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC012723; AAH12723.1; -; mRNA.
DR EMBL; CH466550; EDL04005.1; -; Genomic_DNA.
DR CCDS; CCDS27871.1; -.
DR PIR; I48605; I48605.
DR RefSeq; NP_032370.2; NM_008344.3.
DR AlphaFoldDB; P47880; -.
DR SMR; P47880; -.
DR DIP; DIP-60634N; -.
DR IntAct; P47880; 2.
DR STRING; 10090.ENSMUSP00000023807; -.
DR MEROPS; I31.952; -.
DR PhosphoSitePlus; P47880; -.
DR CPTAC; non-CPTAC-3582; -.
DR PaxDb; P47880; -.
DR PeptideAtlas; P47880; -.
DR PRIDE; P47880; -.
DR ProteomicsDB; 267184; -.
DR Antibodypedia; 1291; 367 antibodies from 35 providers.
DR DNASU; 16012; -.
DR Ensembl; ENSMUST00000023807; ENSMUSP00000023807; ENSMUSG00000023046.
DR GeneID; 16012; -.
DR KEGG; mmu:16012; -.
DR UCSC; uc011zzz.1; mouse.
DR CTD; 3489; -.
DR MGI; MGI:96441; Igfbp6.
DR VEuPathDB; HostDB:ENSMUSG00000023046; -.
DR eggNOG; ENOG502QV3Q; Eukaryota.
DR GeneTree; ENSGT00940000160528; -.
DR HOGENOM; CLU_070833_1_0_1; -.
DR InParanoid; P47880; -.
DR OMA; CVDELGA; -.
DR OrthoDB; 979270at2759; -.
DR PhylomeDB; P47880; -.
DR TreeFam; TF331211; -.
DR Reactome; R-MMU-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR BioGRID-ORCS; 16012; 2 hits in 71 CRISPR screens.
DR PRO; PR:P47880; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; P47880; protein.
DR Bgee; ENSMUSG00000023046; Expressed in tarsal region and 181 other tissues.
DR Genevisible; P47880; MM.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0042568; C:insulin-like growth factor binary complex; ISO:MGI.
DR GO; GO:0001968; F:fibronectin binding; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0031994; F:insulin-like growth factor I binding; ISO:MGI.
DR GO; GO:0031995; F:insulin-like growth factor II binding; ISO:MGI.
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:MGI.
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; IPR017891; Insulin_GF-bd_Cys-rich_CS.
DR InterPro; IPR000716; Thyroglobulin_1.
DR InterPro; IPR036857; Thyroglobulin_1_sf.
DR PANTHER; PTHR11551:SF14; PTHR11551:SF14; 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; 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; Glycoprotein; Growth factor binding; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000250"
FT CHAIN 26..238
FT /note="Insulin-like growth factor-binding protein 6"
FT /id="PRO_0000014390"
FT DOMAIN 26..108
FT /note="IGFBP N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT DOMAIN 157..232
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT REGION 104..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 218..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..141
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..238
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 30..33
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 41..45
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 58..64
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 72..85
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 79..105
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 160..188
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 199..210
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 212..232
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT CONFLICT 35
FT /note="A -> P (in Ref. 1; CAA57274)"
FT /evidence="ECO:0000305"
FT CONFLICT 93
FT /note="A -> T (in Ref. 1; CAA57274)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 238 AA; 25347 MW; DDBAFD5DB0413CF7 CRC64;
MTWDGLPTQP LLMLLMLLFA AGSGSALAGC PGCGAGMQTG CRGGCVEEED AGSPADGCTE
AGGCLRREGQ PCGVYSPKCA PGLQCQPREN EEAPLRALLI GQGRCQRARG PSEETTKESK
PQGGASRSRD TNHRDRQKNP RTSAAPIRPN PVQDSEMGPC RRHLDSVLQQ LQTEVFRGGA
RGLYVPNCDL RGFYRKQQCR SSQGNRRGPC WCVDPMGQPL PVSPDGQGST QCSARSSG
