IBP4_BOVIN
ID IBP4_BOVIN Reviewed; 258 AA.
AC Q05716; A5D7U8;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 151.
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 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].
RX PubMed=1282670; DOI=10.1210/mend.6.11.1282670;
RA Moser D.R., Lowe W.L. Jr., Dake B.L., Booth B.A., Boes M., Clemmons D.R.,
RA Bar R.S.;
RT "Endothelial cells express insulin-like growth factor-binding proteins 2 to
RT 6.";
RL Mol. Endocrinol. 6:1805-1814(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal lung;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
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; S52770; AAB24873.1; -; mRNA.
DR EMBL; BC140688; AAI40689.1; -; mRNA.
DR PIR; A45403; A45403.
DR RefSeq; NP_776982.1; NM_174557.4.
DR AlphaFoldDB; Q05716; -.
DR SMR; Q05716; -.
DR STRING; 9913.ENSBTAP00000011361; -.
DR MEROPS; I31.952; -.
DR PaxDb; Q05716; -.
DR PRIDE; Q05716; -.
DR Ensembl; ENSBTAT00000011361; ENSBTAP00000011361; ENSBTAG00000008611.
DR GeneID; 282262; -.
DR KEGG; bta:282262; -.
DR CTD; 3487; -.
DR VEuPathDB; HostDB:ENSBTAG00000008611; -.
DR VGNC; VGNC:30086; IGFBP4.
DR eggNOG; ENOG502QTC8; Eukaryota.
DR GeneTree; ENSGT00940000159647; -.
DR HOGENOM; CLU_070833_3_0_1; -.
DR InParanoid; Q05716; -.
DR OMA; KAPQGCA; -.
DR OrthoDB; 979270at2759; -.
DR TreeFam; TF331211; -.
DR Proteomes; UP000009136; Chromosome 19.
DR Bgee; ENSBTAG00000008611; Expressed in diaphragm and 104 other tissues.
DR ExpressionAtlas; Q05716; baseline and differential.
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; 4.10.800.10; -; 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 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Growth factor binding; Phosphoprotein;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000250"
FT CHAIN 22..258
FT /note="Insulin-like growth factor-binding protein 4"
FT /id="PRO_0000014381"
FT DOMAIN 23..103
FT /note="IGFBP N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT DOMAIN 171..249
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT MOD_RES 255
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P22692"
FT CARBOHYD 125
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 27..53
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 30..55
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 38..59
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 44..56
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 67..80
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 74..100
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 131..138
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 174..204
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 215..226
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 228..249
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
SQ SEQUENCE 258 AA; 27890 MW; A9FDB63B52F0AEF1 CRC64;
MLSLCLMAAL LLAAGPGPSL GDEAIHCPPC SEEKLARCRP PVGCEELVRE PGCGCCATCA
LGKGMPCGVY TPRCGSGLRC YPPRGVEKPL HTLVHGQGVC MELAEIEAIQ ESLQPSDKDE
GDHPNNSFSP CSAHDRKCLQ KHLAKIRDRS TSGGKMKVIG APREEARPVP QGSCQSELHR
ALERLAASQS RTHEDLYIIP IPNCDRNGNF HPKQCHPALD GQRGKCWCVD RKTGVKLPGG
LEPKGELDCH QLADSFRE
