IBP6_BOVIN
ID IBP6_BOVIN Reviewed; 237 AA.
AC Q05718; Q2YDN5; Q865L3;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 2.
DT 25-MAY-2022, entry version 125.
DE RecName: Full=Insulin-like growth factor-binding protein 6;
DE Short=IBP-6;
DE Short=IGF-binding protein 6;
DE Short=IGFBP-6;
DE Flags: Precursor;
GN Name=IGFBP6;
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].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 84-205.
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 110-191.
RX PubMed=14966674;
RA De Donato M., Gallagher D.S. Jr., Lehn C., Gill C., Taylor J.F.;
RT "Molecular cytogenetic assignment of genes to bovine chromosome 5.";
RL Genet. Mol. Res. 2:260-270(2003).
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. Activates the MAPK signaling pathway
CC and induces cell migration. {ECO:0000250|UniProtKB:P24592}.
CC -!- SUBUNIT: Interacts (via C-terminal domain) with PHB2.
CC {ECO:0000250|UniProtKB:P24592}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- PTM: O-glycosylated. {ECO:0000305}.
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DR EMBL; BC110141; AAI10142.1; -; mRNA.
DR EMBL; S52774; AAB24875.2; -; mRNA.
DR EMBL; AY197339; AAO45612.1; -; Genomic_DNA.
DR PIR; C45403; C45403.
DR PIR; T01404; T01404.
DR RefSeq; NP_001035585.1; NM_001040495.2.
DR AlphaFoldDB; Q05718; -.
DR SMR; Q05718; -.
DR STRING; 9913.ENSBTAP00000028615; -.
DR MEROPS; I31.952; -.
DR PaxDb; Q05718; -.
DR PRIDE; Q05718; -.
DR GeneID; 404186; -.
DR KEGG; bta:404186; -.
DR CTD; 3489; -.
DR eggNOG; ENOG502QV3Q; Eukaryota.
DR InParanoid; Q05718; -.
DR OrthoDB; 979270at2759; -.
DR Proteomes; UP000009136; 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:0016477; P:cell migration; ISS:UniProtKB.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; ISS:UniProtKB.
DR CDD; cd00191; TY; 1.
DR Gene3D; 4.10.800.10; -; 1.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR022326; IGFBP-6.
DR InterPro; IPR000867; IGFBP-like.
DR InterPro; IPR022321; IGFBP_1-6_chordata.
DR InterPro; IPR000716; Thyroglobulin_1.
DR InterPro; IPR036857; Thyroglobulin_1_sf.
DR PANTHER; PTHR11551:SF14; PTHR11551:SF14; 1.
DR Pfam; PF00086; Thyroglobulin_1; 1.
DR PRINTS; PR01976; IGFBPFAMILY.
DR PRINTS; PR01982; IGFBPFAMILY6.
DR SMART; SM00121; IB; 1.
DR SMART; SM00211; TY; 1.
DR SUPFAM; SSF57184; SSF57184; 1.
DR SUPFAM; SSF57610; SSF57610; 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; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..237
FT /note="Insulin-like growth factor-binding protein 6"
FT /id="PRO_0000152776"
FT DOMAIN 26..105
FT /note="IGFBP N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT DOMAIN 156..231
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT REGION 101..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 215..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..153
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..237
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 27..30
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 38..42
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 55..61
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 69..82
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 76..102
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 159..186
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 197..208
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 210..231
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT CONFLICT 188
FT /note="H -> Q (in Ref. 1; AAI10142)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 237 AA; 24967 MW; 3502EBDC21DE89AA CRC64;
MTPHRLLPPL LLTLLLAARP GGALARCPGC GQGVSAGCPG GCAEEEDGGP AAEGCAEAGG
CLRREGQQCG VYTPNCAPGL QCQPPEKEDL PLRALLQGRG RCGRARTPSG ENPKESKPQA
GTARSQDVNR RDQQRNSGTS TTPSRSNSGG VQDTEMGPCR KHLDSVLQQL QTEVFRGAHT
LYVPNCDHRG FYRKRQCRSS QGQRRGPCWC VERMGQPLPG SSEGGDGSSL CPTGSSG
