ID   IBP4_MOUSE              Reviewed;         254 AA.
AC   P47879; O35666; Q3TMV0;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 2.
DT   24-JAN-2024, entry version 173.
DE   RecName: Full=Insulin-like growth factor-binding protein 4;
DE            Short=IBP-4;
DE            Short=IGF-binding protein 4;
DE            Short=IGFBP-4;
DE   Flags: Precursor;
GN   Name=Igfbp4; Synonyms=Igfbp-4;
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 [GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=7531538;
RA   Bethel C.R., Vitullo J.C., Miller R.E., Aron D.C.;
RT   "Molecular cloning of mouse insulin-like growth factor binding protein 4
RT   (IGFBP4) cDNA and expression of a fusion protein with IGF-binding
RT   activity.";
RL   Biochem. Mol. Biol. Int. 34:385-392(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Bone marrow;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Liver;
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   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-114.
RC   STRAIN=BALB/cJ; TISSUE=Brain;
RX   PubMed=9468222; DOI=10.1089/dna.1998.17.51;
RA   Glantschnig H., Varga F., Luegmayr E., Klaushofer K.;
RT   "Characterization of the mouse insulin-like growth factor binding protein 4
RT   gene regulatory region and expression studies.";
RL   DNA Cell Biol. 17:51-60(1998).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Kidney, and Liver;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
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.
CC   -!- SUBUNIT: Binds IGF2 more than IGF1.
CC   -!- INTERACTION:
CC       P47879; Q61091: Fzd8; NbExp=3; IntAct=EBI-15706768, EBI-6171689;
CC       P47879; O75581: LRP6; Xeno; NbExp=4; IntAct=EBI-15706768, EBI-910915;
CC   -!- SUBCELLULAR LOCATION: Secreted.
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DR   EMBL; X81582; CAA57272.1; -; mRNA.
DR   EMBL; X76066; CAA53667.1; -; Genomic_DNA.
DR   EMBL; AK150229; BAE29395.1; -; mRNA.
DR   EMBL; AK165688; BAE38340.1; -; mRNA.
DR   EMBL; BC019836; AAH19836.1; -; mRNA.
DR   EMBL; Z95492; CAB08859.1; -; Genomic_DNA.
DR   CCDS; CCDS25371.1; -.
DR   PIR; I48599; I48599.
DR   PIR; I48603; I48603.
DR   RefSeq; NP_034647.1; NM_010517.3.
DR   AlphaFoldDB; P47879; -.
DR   SMR; P47879; -.
DR   DIP; DIP-60633N; -.
DR   IntAct; P47879; 2.
DR   STRING; 10090.ENSMUSP00000017637; -.
DR   MEROPS; I31.952; -.
DR   GlyCosmos; P47879; 1 site, No reported glycans.
DR   GlyGen; P47879; 1 site.
DR   iPTMnet; P47879; -.
DR   PhosphoSitePlus; P47879; -.
DR   SwissPalm; P47879; -.
DR   CPTAC; non-CPTAC-3986; -.
DR   EPD; P47879; -.
DR   MaxQB; P47879; -.
DR   PaxDb; 10090-ENSMUSP00000017637; -.
DR   PeptideAtlas; P47879; -.
DR   ProteomicsDB; 267081; -.
DR   Antibodypedia; 16491; 687 antibodies from 40 providers.
DR   DNASU; 16010; -.
DR   Ensembl; ENSMUST00000017637.13; ENSMUSP00000017637.7; ENSMUSG00000017493.13.
DR   GeneID; 16010; -.
DR   KEGG; mmu:16010; -.
DR   UCSC; uc007lie.1; mouse.
DR   AGR; MGI:96439; -.
DR   CTD; 3487; -.
DR   MGI; MGI:96439; Igfbp4.
DR   VEuPathDB; HostDB:ENSMUSG00000017493; -.
DR   eggNOG; ENOG502QTC8; Eukaryota.
DR   GeneTree; ENSGT00940000159647; -.
DR   HOGENOM; CLU_070833_3_0_1; -.
DR   InParanoid; P47879; -.
DR   OMA; ELDCHQA; -.
DR   OrthoDB; 5394492at2759; -.
DR   PhylomeDB; P47879; -.
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   Reactome; R-MMU-8957275; Post-translational protein phosphorylation.
DR   BioGRID-ORCS; 16010; 3 hits in 77 CRISPR screens.
DR   ChiTaRS; Igfbp4; mouse.
DR   PRO; PR:P47879; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; P47879; Protein.
DR   Bgee; ENSMUSG00000017493; Expressed in external carotid artery and 262 other cell types or tissues.
DR   ExpressionAtlas; P47879; baseline and differential.
DR   GO; GO:0005615; C:extracellular space; IDA:MGI.
DR   GO; GO:0005520; F:insulin-like growth factor binding; IPI:MGI.
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:0000165; P:MAPK cascade; IGI:MGI.
DR   GO; GO:0043568; P:positive regulation of insulin-like growth factor receptor signaling pathway; IGI:MGI.
DR   GO; GO:0043410; P:positive regulation of MAPK cascade; IGI:MGI.
DR   GO; GO:0001558; P:regulation of cell growth; IGI:MGI.
DR   GO; GO:0010906; P:regulation of glucose metabolic process; IGI:MGI.
DR   GO; GO:0040008; P:regulation of growth; IGI:MGI.
DR   GO; GO:0043567; P:regulation of insulin-like growth factor receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0014070; P:response to organic cyclic compound; IEA:Ensembl.
DR   GO; GO:0044342; P:type B pancreatic cell proliferation; IGI:MGI.
DR   CDD; cd00191; TY; 1.
DR   Gene3D; 4.10.40.20; -; 1.
DR   Gene3D; 4.10.800.10; Thyroglobulin type-1; 1.
DR   InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR   InterPro; IPR022327; IGFBP-4.
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; INSULIN-LIKE GROWTH FACTOR BINDING PROTEIN; 1.
DR   PANTHER; PTHR11551:SF7; INSULIN-LIKE GROWTH FACTOR-BINDING PROTEIN 4; 1.
DR   Pfam; PF00219; IGFBP; 1.
DR   Pfam; PF00086; Thyroglobulin_1; 1.
DR   PRINTS; PR01976; IGFBPFAMILY.
DR   PRINTS; PR01980; IGFBPFAMILY4.
DR   SMART; SM00121; IB; 1.
DR   SMART; SM00211; TY; 1.
DR   SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR   SUPFAM; SSF57610; Thyroglobulin type-1 domain; 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.
DR   Genevisible; P47879; MM.
PE   1: Evidence at protein level;
KW   Disulfide bond; Glycoprotein; Growth factor binding; Phosphoprotein;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000250"
FT   CHAIN           22..254
FT                   /note="Insulin-like growth factor-binding protein 4"
FT                   /id="PRO_0000014383"
FT   DOMAIN          23..103
FT                   /note="IGFBP N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT   DOMAIN          167..245
FT                   /note="Thyroglobulin type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT   MOD_RES         251
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P22692"
FT   CARBOHYD        125
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        27..53
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT   DISULFID        30..55
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT   DISULFID        38..56
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT   DISULFID        44..59
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT   DISULFID        67..80
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT   DISULFID        74..100
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT   DISULFID        131..138
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT   DISULFID        170..200
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT   DISULFID        211..222
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT   DISULFID        224..245
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT   CONFLICT        4..5
FT                   /note="FG -> CS (in Ref. 1; CAA57272)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        13
FT                   /note="A -> T (in Ref. 1; CAA57272)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        56
FT                   /note="C -> S (in Ref. 1; CAA57272)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        67
FT                   /note="C -> G (in Ref. 1; CAA57272)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   254 AA;  27807 MW;  58EF89CB514AEE17 CRC64;
     MLPFGLVAAL LLAAGPRPSL GDEAIHCPPC SEEKLARCRP PVGCEELVRE PGCGCCATCA
     LGLGMPCGVY TPRCGSGMRC YPPRGVEKPL RTLMHGQGVC TELSEIEAIQ ESLQTSDKDE
     SEHPNNSFNP CSAHDHRCLQ KHMAKIRDRS KMKIVGTPRE EPRPVPQGSC QSELHRALER
     LAASQSRTHE DLFIIPIPNC DRNGNFHPKQ CHPALDGQRG KCWCVDRKTG VKLPGGLEPK
     GELDCHQLAD SFQE
//