ID   IBP5_BOVIN              Reviewed;         271 AA.
AC   Q05717; A6QPM8;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 2.
DT   03-AUG-2022, entry version 143.
DE   RecName: Full=Insulin-like growth factor-binding protein 5;
DE            Short=IBP-5;
DE            Short=IGF-binding protein 5;
DE            Short=IGFBP-5;
DE   Flags: Precursor;
GN   Name=IGFBP5;
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 [LARGE SCALE MRNA].
RA   Smith T.P.L., Roberts A.J., Echternkamp S.E., Chitko-McKown C.G.,
RA   Wray J.E., Keele J.W.;
RT   "A second set of bovine ESTs from pooled-tissue normalized libraries.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal lung;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 34-144.
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).
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   -!- SUBCELLULAR LOCATION: Secreted.
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DR   EMBL; DN511652; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; BC149394; AAI49395.1; -; mRNA.
DR   EMBL; S52657; AAB24874.1; -; mRNA.
DR   PIR; B45403; B45403.
DR   RefSeq; NP_001098797.1; NM_001105327.2.
DR   AlphaFoldDB; Q05717; -.
DR   SMR; Q05717; -.
DR   STRING; 9913.ENSBTAP00000009285; -.
DR   PaxDb; Q05717; -.
DR   PRIDE; Q05717; -.
DR   Ensembl; ENSBTAT00000078855; ENSBTAP00000061830; ENSBTAG00000054218.
DR   GeneID; 404185; -.
DR   KEGG; bta:404185; -.
DR   CTD; 3488; -.
DR   VEuPathDB; HostDB:ENSBTAG00000054218; -.
DR   VGNC; VGNC:30087; IGFBP5.
DR   eggNOG; ENOG502QUPK; Eukaryota.
DR   GeneTree; ENSGT00940000155890; -.
DR   HOGENOM; CLU_070833_1_1_1; -.
DR   InParanoid; Q05717; -.
DR   OMA; YTERCAL; -.
DR   OrthoDB; 979270at2759; -.
DR   TreeFam; TF331211; -.
DR   Reactome; R-BTA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR   Reactome; R-BTA-8957275; Post-translational protein phosphorylation.
DR   Proteomes; UP000009136; Chromosome 2.
DR   Bgee; ENSBTAG00000054218; Expressed in pigment epithelium of eye and 101 other tissues.
DR   GO; GO:0042567; C:insulin-like growth factor ternary complex; IEA:Ensembl.
DR   GO; GO:0031994; F:insulin-like growth factor I binding; IEA:Ensembl.
DR   GO; GO:0071320; P:cellular response to cAMP; IEA:Ensembl.
DR   GO; GO:0043569; P:negative regulation of insulin-like growth factor receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0014912; P:negative regulation of smooth muscle cell migration; IEA:Ensembl.
DR   GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; IEA:Ensembl.
DR   GO; GO:0017148; P:negative regulation of translation; IEA:Ensembl.
DR   GO; GO:1904754; P:positive regulation of vascular associated smooth muscle cell migration; IEA:Ensembl.
DR   GO; GO:1904707; P:positive regulation of vascular associated smooth muscle cell proliferation; IEA:Ensembl.
DR   GO; GO:0060416; P:response to growth hormone; IDA:AgBase.
DR   CDD; cd00191; TY; 1.
DR   Gene3D; 4.10.800.10; -; 1.
DR   InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR   InterPro; IPR012213; IGFBP-5.
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:SF4; PTHR11551:SF4; 1.
DR   Pfam; PF00219; IGFBP; 1.
DR   Pfam; PF00086; Thyroglobulin_1; 1.
DR   PRINTS; PR01976; IGFBPFAMILY.
DR   PRINTS; PR01981; IGFBPFAMILY5.
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; Growth factor binding; Phosphoprotein; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..271
FT                   /note="Insulin-like growth factor-binding protein 5"
FT                   /id="PRO_0000152775"
FT   DOMAIN          22..102
FT                   /note="IGFBP N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT   DOMAIN          188..262
FT                   /note="Thyroglobulin type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT   REGION          109..129
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        109..125
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         115
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P24593"
FT   DISULFID        44..58
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT   DISULFID        66..79
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT   DISULFID        191..218
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT   DISULFID        229..240
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT   DISULFID        242..262
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
SQ   SEQUENCE   271 AA;  30314 MW;  A4CD8756DD64133D CRC64;
     MVLTAVLLLL AACAGSAQGL GSFVHCEPCD EKALSMCPPS PLGCELVKEP GCGCCMTCAL
     AEGQSCGVYT ERCAQGLRCL PRQDEEKPLH ALLHGRGVCL NEKSYREQAK IERDSREHEE
     PTTSEMAEET YSPKIFRPKH TRISELKAEA VKKDRRKKLT QSKFVGGAEN TAHPRVISAP
     EMRQKSEQGP CRRHMEASLQ ELKASPRMVP RAVYLPNCDR KGFYKRKQCK PSRGRKRGIC
     WCVDKYGMKL PGMEYVDGDF QCHTFDSSNV E