IBP2_RAT
ID IBP2_RAT Reviewed; 304 AA.
AC P12843; Q569C7;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 3.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Insulin-like growth factor-binding protein 2;
DE Short=IBP-2;
DE Short=IGF-binding protein 2;
DE Short=IGFBP-2;
DE AltName: Full=BRL-BP;
DE Flags: Precursor;
GN Name=Igfbp2; Synonyms=Igfbp-2;
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 [MRNA], PARTIAL PROTEIN SEQUENCE, INTERACTION WITH IGF1
RP AND IGF2, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=2538475; DOI=10.1016/s0021-9258(18)83711-5;
RA Brown A.L., Chiariotti L., Orlowski C.C., Mehlman T., Burgers W.H.,
RA Ackerman E.J., Bruni C.B., Rechler M.M.;
RT "Nucleotide sequence and expression of a cDNA clone encoding a fetal rat
RT binding protein for insulin-like growth factors.";
RL J. Biol. Chem. 264:5148-5154(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Liver;
RX PubMed=2477691; DOI=10.1210/mend-3-7-1053;
RA Margot J.B., Binkert C., Mary J.-L., Landwehr J., Heinrich G.,
RA Schwander J.;
RT "A low molecular weight insulin-like growth factor binding protein from
RT rat: cDNA cloning and tissue distribution of its messenger RNA.";
RL Mol. Endocrinol. 3:1053-1060(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
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 [4]
RP PROTEIN SEQUENCE OF 35-64, AND SUBCELLULAR LOCATION.
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 [5]
RP PROTEIN SEQUENCE OF 38-68, AND SUBCELLULAR LOCATION.
RX PubMed=2426267; DOI=10.1016/s0021-9258(18)67365-x;
RA Mottola C., Macdonald R.G., Brackett J.L., Mole J.E., Anderson J.K.,
RA Czech M.P.;
RT "Purification and amino-terminal sequence of an insulin-like growth factor-
RT binding protein secreted by rat liver BRL-3A cells.";
RL J. Biol. Chem. 261:11180-11188(1986).
RN [6]
RP PROTEIN SEQUENCE OF 178-204, INTERACTION WITH IGF2, AND DOMAIN.
RX PubMed=2974285; DOI=10.1016/s0006-291x(88)80309-7;
RA Wang J.F., Hampton B., Mehlman T., Burgess W.H., Rechler M.M.;
RT "Isolation of a biologically active fragment from the carboxy terminus of
RT the fetal rat binding protein for insulin-like growth factors.";
RL Biochem. Biophys. Res. Commun. 157:718-726(1988).
CC -!- FUNCTION: Inhibits IGF-mediated growth and developmental rates (By
CC similarity). 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. {ECO:0000250}.
CC -!- SUBUNIT: Binds IGF2 more than IGF1.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:2426267,
CC ECO:0000269|PubMed:2480123, ECO:0000269|PubMed:2538475}.
CC -!- TISSUE SPECIFICITY: In adults, expressed in brain, testes, ovaries, and
CC kidney. Expression in the adult liver is barely detectable.
CC {ECO:0000269|PubMed:2477691}.
CC -!- DEVELOPMENTAL STAGE: Predominantly expressed at fetal stages with
CC highest expression in fetal liver. Also expressed in fetal kidney,
CC intestine and lung, as well as muscle, heart and stomach.
CC {ECO:0000269|PubMed:2477691, ECO:0000269|PubMed:2538475}.
CC -!- DOMAIN: The C-terminus is required for IGF-binding and growth
CC inhibition. {ECO:0000269|PubMed:2974285}.
CC -!- PTM: O-glycosylated. {ECO:0000250}.
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DR EMBL; J04486; AAA40829.1; -; mRNA.
DR EMBL; M31672; AAA41381.1; -; mRNA.
DR EMBL; BC092570; AAH92570.1; -; mRNA.
DR PIR; A33274; A33274.
DR RefSeq; NP_037254.2; NM_013122.2.
DR AlphaFoldDB; P12843; -.
DR SMR; P12843; -.
DR STRING; 10116.ENSRNOP00000023068; -.
DR MEROPS; I31.953; -.
DR iPTMnet; P12843; -.
DR PhosphoSitePlus; P12843; -.
DR PaxDb; P12843; -.
DR PRIDE; P12843; -.
DR Ensembl; ENSRNOT00000023068; ENSRNOP00000023068; ENSRNOG00000016957.
DR GeneID; 25662; -.
DR KEGG; rno:25662; -.
DR CTD; 3485; -.
DR RGD; 2873; Igfbp2.
DR eggNOG; ENOG502QRWQ; Eukaryota.
DR GeneTree; ENSGT00940000158542; -.
DR HOGENOM; CLU_070833_3_0_1; -.
DR InParanoid; P12843; -.
DR OMA; AEPCAEM; -.
DR OrthoDB; 979270at2759; -.
DR PhylomeDB; P12843; -.
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 PRO; PR:P12843; -.
DR Proteomes; UP000002494; Chromosome 9.
DR Bgee; ENSRNOG00000016957; Expressed in stomach and 19 other tissues.
DR Genevisible; P12843; RN.
DR GO; GO:0016324; C:apical plasma membrane; IDA:RGD.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:RGD.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0005520; F:insulin-like growth factor binding; ISO:RGD.
DR GO; GO:0031994; F:insulin-like growth factor I binding; IDA:UniProtKB.
DR GO; GO:0031995; F:insulin-like growth factor II binding; IDA:RGD.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0032870; P:cellular response to hormone stimulus; IEP:RGD.
DR GO; GO:0007565; P:female pregnancy; IEP:RGD.
DR GO; GO:0042104; P:positive regulation of activated T cell proliferation; ISS:UniProtKB.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR GO; GO:0043567; P:regulation of insulin-like growth factor receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0032355; P:response to estradiol; IEP:RGD.
DR GO; GO:0043627; P:response to estrogen; IEP:RGD.
DR GO; GO:0051384; P:response to glucocorticoid; IEP:RGD.
DR GO; GO:0010226; P:response to lithium ion; IEP:RGD.
DR GO; GO:0009612; P:response to mechanical stimulus; IEP:RGD.
DR GO; GO:0007584; P:response to nutrient; IEP:RGD.
DR GO; GO:0032526; P:response to retinoic acid; IEP:RGD.
DR GO; GO:0048545; P:response to steroid hormone; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0007165; P:signal transduction; IEP:RGD.
DR CDD; cd00191; TY; 1.
DR Gene3D; 4.10.800.10; -; 1.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR012210; IGFBP-2.
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 Pfam; PF00219; IGFBP; 1.
DR Pfam; PF00086; Thyroglobulin_1; 1.
DR PRINTS; PR01976; IGFBPFAMILY.
DR PRINTS; PR01978; IGFBPFAMILY2.
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 Developmental protein; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Growth factor binding; Growth regulation; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..34
FT /evidence="ECO:0000269|PubMed:2480123"
FT CHAIN 35..304
FT /note="Insulin-like growth factor-binding protein 2"
FT /id="PRO_0000014373"
FT DOMAIN 36..118
FT /note="IGFBP N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT DOMAIN 203..285
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT MOTIF 280..282
FT /note="Cell attachment site"
FT DISULFID 206..240
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 251..262
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 264..285
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT CONFLICT 298
FT /note="A -> V (in Ref. 1; AAA40829)"
FT /evidence="ECO:0000305"
SQ 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
