ID   IBP4_SHEEP              Reviewed;         237 AA.
AC   Q28893;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   25-MAY-2022, entry version 98.
DE   RecName: Full=Insulin-like growth factor-binding protein 4;
DE            Short=IBP-4;
DE            Short=IGF-binding protein 4;
DE            Short=IGFBP-4;
GN   Name=IGFBP4;
OS   Ovis aries (Sheep).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Ovis.
OX   NCBI_TaxID=9940;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF N-TERMINUS, GLYCOSYLATION
RP   AT ASN-104, AND TISSUE SPECIFICITY.
RC   TISSUE=Liver;
RX   PubMed=7531449; DOI=10.1677/jme.0.0130219;
RA   Carr J.M., Grant P.A., Francis G.L., Owens J.A., Wallace J.C., Walton P.E.;
RT   "Isolation and characterization of ovine IGFBP-4: protein purification and
RT   cDNA sequence.";
RL   J. Mol. Endocrinol. 13:219-236(1994).
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.
CC   -!- TISSUE SPECIFICITY: Detected in adult ewe, liver > kidney > lung >>
CC       heart and also in several fetal tissues. {ECO:0000269|PubMed:7531449}.
CC   -!- PTM: There are two different molecular mass variants (29 kDa and 24 kDa
CC       forms). The 29 kDa form was shown to be N-glycosylated.
CC       {ECO:0000269|PubMed:7531449}.
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DR   EMBL; S77394; AAB33382.1; -; mRNA.
DR   PIR; I47031; I47031.
DR   AlphaFoldDB; Q28893; -.
DR   SMR; Q28893; -.
DR   STRING; 9940.ENSOARP00000015663; -.
DR   MEROPS; I31.952; -.
DR   iPTMnet; Q28893; -.
DR   eggNOG; ENOG502QTC8; Eukaryota.
DR   Proteomes; UP000002356; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005520; F:insulin-like growth factor binding; IEA:InterPro.
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.
FT   CHAIN           1..237
FT                   /note="Insulin-like growth factor-binding protein 4"
FT                   /id="PRO_0000152774"
FT   DOMAIN          2..82
FT                   /note="IGFBP N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT   DOMAIN          150..228
FT                   /note="Thyroglobulin type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT   MOD_RES         234
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P22692"
FT   CARBOHYD        104
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:7531449"
FT   DISULFID        6..32
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT   DISULFID        9..34
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT   DISULFID        17..38
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT   DISULFID        23..35
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT   DISULFID        46..59
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT   DISULFID        53..79
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT   DISULFID        110..117
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT   DISULFID        153..183
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT   DISULFID        194..205
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT   DISULFID        207..228
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
SQ   SEQUENCE   237 AA;  25869 MW;  EBC80D4C7667A226 CRC64;
     DEAIHCPPCS EEKLARCRPP VGCEELVREP GCGCCATCAL GKGMPCGVYT PDCGSGLRCH
     PPRGVEKPLH TLVHGQGVCM ELAEIEAIQE SLQPSDKDEG DHPNNSFSPC SAHDRKCLQK
     HLAKIRDRST SGGKMKVIGA PREEVRPVPQ GSCQSELHRA LERLAASQSR THEDLYIIPI
     PNCDRNGNFH PKQCHPALDG QRGKCWCVDR KTGVKLPGGL EPKGELDCHQ LADSFRE