IBP4_RAT
ID IBP4_RAT Reviewed; 254 AA.
AC P21744; Q68J74;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 2.
DT 03-AUG-2022, entry version 167.
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 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 [GENOMIC DNA].
RX PubMed=1704481; DOI=10.1210/mend-4-10-1451;
RA Shimasaki S., Uchiyama F., Shimonaka M., Ling N.;
RT "Molecular cloning of the cDNAs encoding a novel insulin-like growth
RT factor-binding protein from rat and human.";
RL Mol. Endocrinol. 4:1451-1458(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Sprague-Dawley;
RX PubMed=7679899; DOI=10.1006/bbrc.1993.1155;
RA Gao L., Ling N., Shimasaki S.;
RT "Structure of the rat insulin-like growth factor binding protein-4 gene.";
RL Biochem. Biophys. Res. Commun. 190:1053-1059(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar; TISSUE=Mandibular condyle;
RA Hajjar D., Ricarte-Filho J.C.M., dos Santos M.F., Kimura E.T.;
RT "IGFBP3, 4, 5 and 6 expression at the mandibular condylar cartilage during
RT rat growth and development.";
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC 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 PROTEIN SEQUENCE OF 22-61.
RC TISSUE=Serum;
RX PubMed=2480123; DOI=10.1016/0006-291x(89)91053-x;
RA Shimonaka M., Schroeder R., Shimasaki S., Ling N.;
RT "Identification of a novel binding protein for insulin-like growth factors
RT in adult rat serum.";
RL Biochem. Biophys. Res. Commun. 165:189-195(1989).
RN [6]
RP DISULFIDE BONDS.
RX PubMed=11182766; DOI=10.1677/joe.0.1680283;
RA Chelius D., Baldwin M.A., Lu X., Spencer E.M.;
RT "Expression, purification and characterization of the structure and
RT disulfide linkages of insulin-like growth factor binding protein-4.";
RL J. Endocrinol. 168:283-296(2001).
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 -!- SUBCELLULAR LOCATION: Secreted.
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DR EMBL; L08276; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AY686592; AAT96376.1; -; mRNA.
DR EMBL; BC098750; AAH98750.1; -; mRNA.
DR PIR; JC1464; JC1464.
DR RefSeq; NP_001004274.1; NM_001004274.2.
DR AlphaFoldDB; P21744; -.
DR SMR; P21744; -.
DR BioGRID; 262076; 2.
DR STRING; 10116.ENSRNOP00000014153; -.
DR MEROPS; I31.952; -.
DR GlyGen; P21744; 1 site.
DR PaxDb; P21744; -.
DR PRIDE; P21744; -.
DR Ensembl; ENSRNOT00000014153; ENSRNOP00000014153; ENSRNOG00000010635.
DR GeneID; 360622; -.
DR KEGG; rno:360622; -.
DR UCSC; RGD:2875; rat.
DR CTD; 3487; -.
DR RGD; 2875; Igfbp4.
DR eggNOG; ENOG502QTC8; Eukaryota.
DR GeneTree; ENSGT00940000159647; -.
DR HOGENOM; CLU_070833_3_0_1; -.
DR InParanoid; P21744; -.
DR OMA; KAPQGCA; -.
DR OrthoDB; 979270at2759; -.
DR PhylomeDB; P21744; -.
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 Reactome; R-RNO-8957275; Post-translational protein phosphorylation.
DR PRO; PR:P21744; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000010635; Expressed in liver and 19 other tissues.
DR Genevisible; P21744; RN.
DR GO; GO:0005615; C:extracellular space; ISO:RGD.
DR GO; GO:0005520; F:insulin-like growth factor binding; ISO:RGD.
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; IEP:RGD.
DR GO; GO:0035556; P:intracellular signal transduction; TAS:RGD.
DR GO; GO:0000165; P:MAPK cascade; IEA:Ensembl.
DR GO; GO:0043568; P:positive regulation of insulin-like growth factor receptor signaling pathway; ISO:RGD.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; ISO:RGD.
DR GO; GO:0001558; P:regulation of cell growth; ISO:RGD.
DR GO; GO:0010906; P:regulation of glucose metabolic process; ISO:RGD.
DR GO; GO:0040008; P:regulation of growth; ISO:RGD.
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; ISO:RGD.
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 Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Growth factor binding; Phosphoprotein; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000269|PubMed:2480123"
FT CHAIN 22..254
FT /note="Insulin-like growth factor-binding protein 4"
FT /id="PRO_0000014384"
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 REGION 149..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 ECO:0000269|PubMed:11182766"
FT DISULFID 44..56
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500,
FT ECO:0000269|PubMed:11182766"
FT DISULFID 67..80
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500,
FT ECO:0000269|PubMed:11182766"
FT DISULFID 74..100
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500,
FT ECO:0000269|PubMed:11182766"
FT DISULFID 131..138
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500,
FT ECO:0000269|PubMed:11182766"
FT DISULFID 170..200
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500,
FT ECO:0000269|PubMed:11182766"
FT DISULFID 211..222
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500,
FT ECO:0000269|PubMed:11182766"
FT DISULFID 224..245
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500,
FT ECO:0000269|PubMed:11182766"
SQ SEQUENCE 254 AA; 27745 MW; 97D37AC98BD0E787 CRC64;
MLPFGLVAAL LLAAGPRPSL GDEAIHCPPC SEEKLARCRP PVGCEELVRE PGCGCCATCA
LGLGMPCGVY TPRCGSGMRC YPPRGVEKPL RTLMHGQGVC TELSEIEAIQ ESLQTSDKDE
SEHPNNSFNP CSAHDHRCLQ KHMAKVRDRS KMKVVGTPRE EPRPVPQGSC QSELHRALER
LAASQSRTHE DLFIIPIPNC DRNGNFHPKQ CHPALDGQRG KCWCVDRKTG VKLPGGLEPK
GELDCHQLAD SLQE
