ID   IBP5_PIG                Reviewed;         271 AA.
AC   Q28985;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   16-FEB-2004, sequence version 2.
DT   25-MAY-2022, entry version 120.
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   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 [MRNA].
RC   TISSUE=Skeletal muscle;
RX   PubMed=8573141; DOI=10.1006/bbrc.1996.0044;
RA   White M.E., Diao R., Hathaway M.R., Mickelson J., Dayton W.R.;
RT   "Molecular cloning and sequence analysis of the porcine insulin-like growth
RT   factor binding protein-5 complementary deoxyribonucleic acid.";
RL   Biochem. Biophys. Res. Commun. 218:248-253(1996).
RN   [2]
RP   SEQUENCE REVISION TO 49.
RA   White M.E., Diao R., Hathaway M.R., Mickelson J., Dayton W.R.;
RL   Submitted (SEP-2002) 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   -!- SUBCELLULAR LOCATION: Secreted.
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DR   EMBL; U41340; AAA87859.2; -; mRNA.
DR   PIR; JC4584; JC4584.
DR   RefSeq; NP_999264.1; NM_214099.1.
DR   AlphaFoldDB; Q28985; -.
DR   SMR; Q28985; -.
DR   STRING; 9823.ENSSSCP00000028711; -.
DR   MEROPS; I31.952; -.
DR   PaxDb; Q28985; -.
DR   Ensembl; ENSSSCT00040063800; ENSSSCP00040026945; ENSSSCG00040047315.
DR   GeneID; 397182; -.
DR   KEGG; ssc:397182; -.
DR   CTD; 3488; -.
DR   eggNOG; ENOG502QUPK; Eukaryota.
DR   InParanoid; Q28985; -.
DR   OrthoDB; 979270at2759; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005520; F:insulin-like growth factor binding; IEA:InterPro.
DR   GO; GO:0060416; P:response to growth hormone; ISS: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_0000014387"
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;  30337 MW;  7486EAF2BC7AF62D CRC64;
     MVLTAVLLLL AACAGPAQGL GSFVHCEPCD EKALSMCPPS PLGCELVKEP GCGCCMTCAL
     AEGQSCGVYT ERCAQGLRCL PRQDEEKPLH ALLHGRGVCL NEKSYREQAK IERDSREHEE
     PTTSEMAEET YSPKIFRPKH TRISELKAEA VKKDRRKKLT QSKFVGGAEN TAHPRVILAP
     EMRQESEQGP CRRHMEASLQ ELKASPRMVP RAVYLPNCDR KGFYKRKQCK PSRGRKRGIC
     WCVDKYGMKL PGMEYVDGDF QCHSFDSSNV E