IBP4_MOUSE
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 03-AUG-2022, entry version 165.
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 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; P47879; -.
DR PeptideAtlas; P47879; -.
DR PRIDE; P47879; -.
DR ProteomicsDB; 267081; -.
DR Antibodypedia; 16491; 655 antibodies from 39 providers.
DR DNASU; 16010; -.
DR Ensembl; ENSMUST00000017637; ENSMUSP00000017637; ENSMUSG00000017493.
DR GeneID; 16010; -.
DR KEGG; mmu:16010; -.
DR UCSC; uc007lie.1; mouse.
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; KAPQGCA; -.
DR OrthoDB; 979270at2759; -.
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 72 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 260 other tissues.
DR ExpressionAtlas; P47879; baseline and differential.
DR Genevisible; P47879; MM.
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:0006954; P:inflammatory response; IEA:Ensembl.
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:0044342; P:type B pancreatic cell proliferation; IGI:MGI.
DR CDD; cd00191; TY; 1.
DR Gene3D; 4.10.800.10; -; 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:SF7; PTHR11551:SF7; 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; 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 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:PRU00500"
FT DISULFID 30..55
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 38..59
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 44..56
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 67..80
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 74..100
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
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
