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Insulin-like growth factor-binding protein 2 (IBP-2) (IGF-binding protein 2) (IGFBP-2) (BRL-BP)

 IBP2_RAT                Reviewed;         304 AA.
P12843; Q569C7;
01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
01-MAY-2007, sequence version 3.
12-SEP-2018, entry version 147.
RecName: Full=Insulin-like growth factor-binding protein 2;
Short=IBP-2;
Short=IGF-binding protein 2;
Short=IGFBP-2;
AltName: Full=BRL-BP;
Flags: Precursor;
Name=Igfbp2; Synonyms=Igfbp-2;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, INTERACTION WITH
IGF1 AND IGF2, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
PubMed=2538475;
Brown A.L., Chiariotti L., Orlowski C.C., Mehlman T., Burgers W.H.,
Ackerman E.J., Bruni C.B., Rechler M.M.;
"Nucleotide sequence and expression of a cDNA clone encoding a fetal
rat binding protein for insulin-like growth factors.";
J. Biol. Chem. 264:5148-5154(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL
STAGE.
TISSUE=Liver;
PubMed=2477691; DOI=10.1210/mend-3-7-1053;
Margot J.B., Binkert C., Mary J.-L., Landwehr J., Heinrich G.,
Schwander J.;
"A low molecular weight insulin-like growth factor binding protein
from rat: cDNA cloning and tissue distribution of its messenger RNA.";
Mol. Endocrinol. 3:1053-1060(1989).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Ovary;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
PROTEIN SEQUENCE OF 35-64, AND SUBCELLULAR LOCATION.
TISSUE=Serum;
PubMed=2480123; DOI=10.1016/0006-291X(89)91053-X;
Shimonaka M., Schroeder R., Shimasaki S., Ling N.;
"Identification of a novel binding protein for insulin-like growth
factors in adult rat serum.";
Biochem. Biophys. Res. Commun. 165:189-195(1989).
[5]
PROTEIN SEQUENCE OF 38-68, AND SUBCELLULAR LOCATION.
PubMed=2426267;
Mottola C., Macdonald R.G., Brackett J.L., Mole J.E., Anderson J.K.,
Czech M.P.;
"Purification and amino-terminal sequence of an insulin-like growth
factor-binding protein secreted by rat liver BRL-3A cells.";
J. Biol. Chem. 261:11180-11188(1986).
[6]
PROTEIN SEQUENCE OF 178-204, INTERACTION WITH IGF2, AND DOMAIN.
PubMed=2974285; DOI=10.1016/S0006-291X(88)80309-7;
Wang J.F., Hampton B., Mehlman T., Burgess W.H., Rechler M.M.;
"Isolation of a biologically active fragment from the carboxy terminus
of the fetal rat binding protein for insulin-like growth factors.";
Biochem. Biophys. Res. Commun. 157:718-726(1988).
-!- FUNCTION: Inhibits IGF-mediated growth and developmental rates (By
similarity). IGF-binding proteins prolong the half-life of the
IGFs and have been shown to either inhibit or stimulate the growth
promoting effects of the IGFs on cell culture. They alter the
interaction of IGFs with their cell surface receptors.
{ECO:0000250}.
-!- SUBUNIT: Binds IGF2 more than IGF1.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:2426267,
ECO:0000269|PubMed:2480123, ECO:0000269|PubMed:2538475}.
-!- TISSUE SPECIFICITY: In adults, expressed in brain, testes,
ovaries, and kidney. Expression in the adult liver is barely
detectable. {ECO:0000269|PubMed:2477691}.
-!- DEVELOPMENTAL STAGE: Predominantly expressed at fetal stages with
highest expression in fetal liver. Also expressed in fetal kidney,
intestine and lung, as well as muscle, heart and stomach.
{ECO:0000269|PubMed:2477691, ECO:0000269|PubMed:2538475}.
-!- DOMAIN: The C-terminus is required for IGF-binding and growth
inhibition. {ECO:0000269|PubMed:2974285}.
-!- PTM: O-glycosylated. {ECO:0000250}.
-----------------------------------------------------------------------
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EMBL; J04486; AAA40829.1; -; mRNA.
EMBL; M31672; AAA41381.1; -; mRNA.
EMBL; BC092570; AAH92570.1; -; mRNA.
PIR; A33274; A33274.
RefSeq; NP_037254.2; NM_013122.2.
UniGene; Rn.6813; -.
ProteinModelPortal; P12843; -.
SMR; P12843; -.
STRING; 10116.ENSRNOP00000023068; -.
MEROPS; I31.953; -.
iPTMnet; P12843; -.
PhosphoSitePlus; P12843; -.
PaxDb; P12843; -.
PRIDE; P12843; -.
Ensembl; ENSRNOT00000023068; ENSRNOP00000023068; ENSRNOG00000016957.
GeneID; 25662; -.
KEGG; rno:25662; -.
CTD; 3485; -.
RGD; 2873; Igfbp2.
eggNOG; ENOG410IHUR; Eukaryota.
eggNOG; ENOG4111GWQ; LUCA.
GeneTree; ENSGT00550000074457; -.
HOGENOM; HOG000253012; -.
HOVERGEN; HBG002631; -.
InParanoid; P12843; -.
OMA; DGTMNML; -.
OrthoDB; EOG091G0EIN; -.
PhylomeDB; P12843; -.
TreeFam; TF331211; -.
Reactome; R-RNO-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
PRO; PR:P12843; -.
Proteomes; UP000002494; Chromosome 9.
Bgee; ENSRNOG00000016957; Expressed in 10 organ(s), highest expression level in testis.
Genevisible; P12843; RN.
GO; GO:0016324; C:apical plasma membrane; IDA:RGD.
GO; GO:0031410; C:cytoplasmic vesicle; IDA:RGD.
GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
GO; GO:0005615; C:extracellular space; IDA:RGD.
GO; GO:0031994; F:insulin-like growth factor I binding; IDA:UniProtKB.
GO; GO:0031995; F:insulin-like growth factor II binding; IDA:RGD.
GO; GO:0007568; P:aging; IEP:RGD.
GO; GO:0032870; P:cellular response to hormone stimulus; IEP:RGD.
GO; GO:0007565; P:female pregnancy; IEP:RGD.
GO; GO:0007275; P:multicellular organism development; IEA:UniProtKB-KW.
GO; GO:0042104; P:positive regulation of activated T cell proliferation; ISS:UniProtKB.
GO; GO:0001558; P:regulation of cell growth; IEA:InterPro.
GO; GO:0043567; P:regulation of insulin-like growth factor receptor signaling pathway; ISS:UniProtKB.
GO; GO:0042493; P:response to drug; IEP:RGD.
GO; GO:0032355; P:response to estradiol; IEP:RGD.
GO; GO:0043627; P:response to estrogen; IEP:RGD.
GO; GO:0051384; P:response to glucocorticoid; IEP:RGD.
GO; GO:0010226; P:response to lithium ion; IEP:RGD.
GO; GO:0009612; P:response to mechanical stimulus; IEP:RGD.
GO; GO:0007584; P:response to nutrient; IEP:RGD.
GO; GO:0032526; P:response to retinoic acid; IEP:RGD.
GO; GO:0048545; P:response to steroid hormone; IEP:RGD.
GO; GO:0007165; P:signal transduction; IEP:RGD.
CDD; cd00191; TY; 1.
Gene3D; 4.10.800.10; -; 1.
InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
InterPro; IPR012210; IGFBP-2.
InterPro; IPR000867; IGFBP-like.
InterPro; IPR009168; IGFBP1-6.
InterPro; IPR022321; IGFBP_1-6_chordata.
InterPro; IPR017891; Insulin_GF-bd_Cys-rich_CS.
InterPro; IPR000716; Thyroglobulin_1.
InterPro; IPR036857; Thyroglobulin_1_sf.
PANTHER; PTHR11551; PTHR11551; 1.
Pfam; PF00219; IGFBP; 1.
Pfam; PF00086; Thyroglobulin_1; 1.
PRINTS; PR01976; IGFBPFAMILY.
PRINTS; PR01978; IGFBPFAMILY2.
SMART; SM00121; IB; 1.
SMART; SM00211; TY; 1.
SUPFAM; SSF57184; SSF57184; 1.
SUPFAM; SSF57610; SSF57610; 1.
PROSITE; PS00222; IGFBP_N_1; 1.
PROSITE; PS51323; IGFBP_N_2; 1.
PROSITE; PS00484; THYROGLOBULIN_1_1; 1.
PROSITE; PS51162; THYROGLOBULIN_1_2; 1.
1: Evidence at protein level;
Complete proteome; Developmental protein; Direct protein sequencing;
Disulfide bond; Glycoprotein; Growth factor binding;
Growth regulation; Reference proteome; Secreted; Signal.
SIGNAL 1 34 {ECO:0000269|PubMed:2480123}.
CHAIN 35 304 Insulin-like growth factor-binding
protein 2.
/FTId=PRO_0000014373.
DOMAIN 36 118 IGFBP N-terminal. {ECO:0000255|PROSITE-
ProRule:PRU00653}.
DOMAIN 203 285 Thyroglobulin type-1.
{ECO:0000255|PROSITE-ProRule:PRU00500}.
MOTIF 280 282 Cell attachment site.
DISULFID 206 240 {ECO:0000255|PROSITE-ProRule:PRU00500}.
DISULFID 251 262 {ECO:0000255|PROSITE-ProRule:PRU00500}.
DISULFID 264 285 {ECO:0000255|PROSITE-ProRule:PRU00500}.
CONFLICT 298 298 A -> V (in Ref. 1; AAA40829).
{ECO:0000305}.
SEQUENCE 304 AA; 32855 MW; 8558B7E2C9152B9F CRC64;
MLPRLGGPAL PLLLPSLLLL LLLGAGGCGP GVRAEVLFRC PPCTPERLAA CGPPPDAPCA
ELVREPGCGC CSVCARQEGE ACGVYIPRCA QTLRCYPNPG SELPLKALVT GAGTCEKRRV
GATPQQVADS EDDHSEGGLV ENHVDGTMNM LGGSSAGRKP PKSGMKELAV FREKVNEQHR
QMGKGAKHLS LEEPKKLRPP PARTPCQQEL DQVLERISTM RLPDDRGPLE HLYSLHIPNC
DKHGLYNLKQ CKMSLNGQRG ECWCVNPNTG KPIQGAPTIR GDPECHLFYN EQQENDGAHA
QRVQ


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