IBP2_BOVIN
ID IBP2_BOVIN Reviewed; 317 AA.
AC P13384; O97599;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 2.
DT 03-AUG-2022, entry version 138.
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 Flags: Precursor;
GN Name=IGFBP2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
RX PubMed=1377702; DOI=10.1002/jcb.240480212;
RA Bourner M.J., Busby W.H. Jr., Siegel N.R., Krivi G.G., McCusker R.H.,
RA Clemmons D.R.;
RT "Cloning and sequence determination of bovine insulin-like growth factor
RT binding protein-2 (IGFBP-2): comparison of its structural and functional
RT properties with IGFBP-1.";
RL J. Cell. Biochem. 48:215-226(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 8-317.
RX PubMed=1697752; DOI=10.1677/jme.0.0050077;
RA Upton F.Z., Szabo L., Wallace J.C., Ballard F.J.;
RT "Characterization and cloning of a bovine insulin-like growth factor-
RT binding protein.";
RL J. Mol. Endocrinol. 5:77-84(1990).
RN [3]
RP PROTEIN SEQUENCE OF 34-86.
RX PubMed=2450535; DOI=10.1016/0006-291x(88)90580-3;
RA Szabo L., Mottershead D.G., Ballard F.J., Wallace J.C.;
RT "The bovine insulin-like growth factor (IGF) binding protein purified from
RT conditioned medium requires the N-terminal tripeptide in IGF-1 for
RT binding.";
RL Biochem. Biophys. Res. Commun. 151:207-214(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. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- DOMAIN: The C-terminus is required for IGF-binding and growth
CC inhibition. {ECO:0000250}.
CC -!- PTM: O-glycosylated. {ECO:0000250}.
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DR EMBL; AF074854; AAD04862.1; -; mRNA.
DR PIR; A60967; A60967.
DR RefSeq; NP_776980.1; NM_174555.1.
DR AlphaFoldDB; P13384; -.
DR BMRB; P13384; -.
DR SMR; P13384; -.
DR STRING; 9913.ENSBTAP00000007349; -.
DR MEROPS; I31.953; -.
DR PRIDE; P13384; -.
DR Ensembl; ENSBTAT00000007349; ENSBTAP00000007349; ENSBTAG00000005596.
DR GeneID; 282260; -.
DR KEGG; bta:282260; -.
DR CTD; 3485; -.
DR VEuPathDB; HostDB:ENSBTAG00000005596; -.
DR VGNC; VGNC:30084; IGFBP2.
DR GeneTree; ENSGT00940000158542; -.
DR InParanoid; P13384; -.
DR OMA; AEPCAEM; -.
DR OrthoDB; 979270at2759; -.
DR Proteomes; UP000009136; Chromosome 2.
DR Bgee; ENSBTAG00000005596; Expressed in anterior segment of eyeball and 103 other tissues.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:AgBase.
DR GO; GO:0031994; F:insulin-like growth factor I binding; ISS:UniProtKB.
DR GO; GO:0031995; F:insulin-like growth factor II binding; ISS:UniProtKB.
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:0032868; P:response to insulin; IDA:AgBase.
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 Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Growth factor binding; Growth regulation; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..33
FT /evidence="ECO:0000269|PubMed:2450535"
FT CHAIN 34..317
FT /note="Insulin-like growth factor-binding protein 2"
FT /id="PRO_0000014369"
FT DOMAIN 35..126
FT /note="IGFBP N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT DOMAIN 216..298
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT REGION 126..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 190..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 293..295
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT COMPBIAS 190..212
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 219..253
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 264..275
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 277..298
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT CONFLICT 32..33
FT /note="RA -> AS (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 46
FT /note="S -> C (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 60..61
FT /note="PA -> AP (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 82
FT /note="C -> F (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 114
FT /note="R -> H (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 128
FT /note="D -> S (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 134
FT /note="S -> T (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 313
FT /note="T -> N (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 317 AA; 34015 MW; 2B552BC61CA7E9CD CRC64;
MQPRLGGPAL LLLPPLLLLL LLGAGGGDCG ARAEVLFRCP PCTPESLAAC KPPPGAAAGP
AGDARVPCEL VREPGCGCCS VCARLEGERC GVYTPRCGQG LRCYPNPGSE LPLRALVHGE
GTCEKHGDAE YSASPEQVAD NGEEHSEGGL VENHVDGNVN LMGGGGGAGR KPLKSGMKEL
AVFREKVTEQ HRQMGKGGKH HLGLEEPKKL RPPPARTPCQ QELDQVLERI STMRLPDERG
PLEHLYSLHI PNCDKHGLYN LKQCKMSLNG QRGECWCVNP NTGKLIQGAP TIRGDPECHL
FYNEQQGARG VHTQRMQ
