ID IBP4_PIG Reviewed; 259 AA.
AC P24854; Q06AV6;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 2.
DT 08-NOV-2023, entry version 111.
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;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Liu G.Y.;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 23-38.
RX PubMed=1722398; DOI=10.1016/0006-291x(91)92056-p;
RA Coleman M.E., Pan Y.-C.E., Etherton T.D.;
RT "Identification and NH2-terminal amino acid sequence of three insulin-like
RT growth factor-binding proteins in porcine serum.";
RL Biochem. Biophys. Res. Commun. 181:1131-1136(1991).
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. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
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DR EMBL; DQ917619; ABI97164.1; -; mRNA.
DR PIR; JH0517; JH0517.
DR RefSeq; NP_001116601.1; NM_001123129.1.
DR AlphaFoldDB; P24854; -.
DR SMR; P24854; -.
DR STRING; 9823.ENSSSCP00000018516; -.
DR GlyCosmos; P24854; 1 site, No reported glycans.
DR PaxDb; 9823-ENSSSCP00000018516; -.
DR GeneID; 100144490; -.
DR KEGG; ssc:100144490; -.
DR CTD; 3487; -.
DR eggNOG; ENOG502QTC8; Eukaryota.
DR InParanoid; P24854; -.
DR OrthoDB; 5394492at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR Proteomes; UP000694570; Unplaced.
DR Proteomes; UP000694571; Unplaced.
DR Proteomes; UP000694720; Unplaced.
DR Proteomes; UP000694722; Unplaced.
DR Proteomes; UP000694723; Unplaced.
DR Proteomes; UP000694724; Unplaced.
DR Proteomes; UP000694725; Unplaced.
DR Proteomes; UP000694726; Unplaced.
DR Proteomes; UP000694727; Unplaced.
DR Proteomes; UP000694728; Unplaced.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
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:0043567; P:regulation of insulin-like growth factor receptor signaling pathway; IBA:GO_Central.
DR CDD; cd00191; TY; 1.
DR Gene3D; 4.10.40.20; -; 1.
DR Gene3D; 4.10.800.10; Thyroglobulin type-1; 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; INSULIN-LIKE GROWTH FACTOR BINDING PROTEIN; 1.
DR PANTHER; PTHR11551:SF7; INSULIN-LIKE GROWTH FACTOR-BINDING PROTEIN 4; 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; Growth factor receptor domain; 1.
DR SUPFAM; SSF57610; Thyroglobulin type-1 domain; 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..22
FT /evidence="ECO:0000269|PubMed:1722398"
FT CHAIN 23..259
FT /note="Insulin-like growth factor-binding protein 4"
FT /id="PRO_0000152773"
FT DOMAIN 24..104
FT /note="IGFBP N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT DOMAIN 172..250
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT REGION 115..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 256
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P22692"
FT CARBOHYD 126
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 28..54
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT DISULFID 31..56
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT DISULFID 39..57
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT DISULFID 45..60
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT DISULFID 68..81
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT DISULFID 75..101
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT DISULFID 132..139
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 175..205
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 216..227
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 229..250
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT CONFLICT 31
FT /note="C -> P (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 259 AA; 28230 MW; ED3EFB4F2D30CC76 CRC64;
MLPLCLVAAL LLSASGPRPS LGDEAIHCPP CSEEKLARCR PPVGCEELVR EPGCGCCATC
ALGKGMPCGV YTPRCGSGLR CYPPRGVEKP LHTLMHGQGL CMELAEIEAI QESLQPSDKD
EGDHPNNSFS PCSPQDRRCL QKHLAKIRDR STSGGKMKVI GAPREEARPV PQGSCQSELH
RALERLAASQ RRTHEDLYII PIPNCDRNGN FHPKQCHPAL DGQRGKCWCV DRKTGVKLPG
GLEPKGELDC HQLADSFRE
//
