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Database: UniProt
Entry: A0A8C7MBW9_ONCKI
LinkDB: A0A8C7MBW9_ONCKI
Original site: A0A8C7MBW9_ONCKI 
ID   A0A8C7MBW9_ONCKI        Unreviewed;       280 AA.
AC   A0A8C7MBW9;
DT   19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2022, sequence version 1.
DT   28-JAN-2026, entry version 18.
DE   SubName: Full=Insulin-like growth factor binding protein 2b {ECO:0000313|Ensembl:ENSOKIP00005043300.1};
GN   Name=IGFBP2 {ECO:0000313|Ensembl:ENSOKIP00005043300.1};
GN   Synonyms=LOC109871277 {ECO:0000313|Ensembl:ENSOKIP00005043300.1};
OS   Oncorhynchus kisutch (Coho salmon) (Salmo kisutch).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Oncorhynchus.
OX   NCBI_TaxID=8019 {ECO:0000313|Ensembl:ENSOKIP00005043300.1, ECO:0000313|Proteomes:UP000694557};
RN   [1] {ECO:0000313|Ensembl:ENSOKIP00005043300.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (AUG-2025) to UniProtKB.
RN   [2] {ECO:0000313|Ensembl:ENSOKIP00005043300.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2025) to UniProtKB.
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. {ECO:0000256|ARBA:ARBA00003811}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00500}.
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DR   AlphaFoldDB; A0A8C7MBW9; -.
DR   Ensembl; ENSOKIT00005045629.1; ENSOKIP00005043300.1; ENSOKIG00005018263.1.
DR   GeneTree; ENSGT00940000158542; -.
DR   Proteomes; UP000694557; Unassembled WGS sequence.
DR   GO; GO:0005615; C:extracellular space; IEA:TreeGrafter.
DR   GO; GO:0031994; F:insulin-like growth factor I binding; IEA:UniProtKB-ARBA.
DR   GO; GO:0031995; F:insulin-like growth factor II binding; IEA:TreeGrafter.
DR   GO; GO:0048640; P:negative regulation of developmental growth; IEA:UniProtKB-ARBA.
DR   GO; GO:0043567; P:regulation of insulin-like growth factor receptor signaling pathway; IEA:TreeGrafter.
DR   CDD; cd00191; TY; 1.
DR   FunFam; 4.10.40.20:FF:000001; Insulin-like growth factor binding protein 5; 1.
DR   FunFam; 4.10.800.10:FF:000002; Insulin-like growth factor-binding protein 2; 1.
DR   Gene3D; 4.10.40.20; -; 1.
DR   Gene3D; 4.10.800.10; Thyroglobulin type-1; 1.
DR   InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR   InterPro; IPR012210; IGFBP-2.
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; INSULIN-LIKE GROWTH FACTOR BINDING PROTEIN; 1.
DR   PANTHER; PTHR11551:SF5; INSULIN-LIKE GROWTH FACTOR-BINDING PROTEIN 2; 1.
DR   Pfam; PF00219; IGFBP; 1.
DR   Pfam; PF00086; Thyroglobulin_1; 1.
DR   PRINTS; PR01976; IGFBPFAMILY.
DR   PRINTS; PR01978; IGFBPFAMILY2.
DR   SMART; SM00121; IB; 1.
DR   SMART; SM00211; TY; 1.
DR   SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR   SUPFAM; SSF57610; Thyroglobulin type-1 domain; 1.
DR   PROSITE; PS51323; IGFBP_N_2; 1.
DR   PROSITE; PS51162; THYROGLOBULIN_1_2; 1.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Growth factor binding {ECO:0000256|ARBA:ARBA00023183};
KW   Growth regulation {ECO:0000256|ARBA:ARBA00022604};
KW   Reference proteome {ECO:0000313|Proteomes:UP000694557};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..280
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5034484704"
FT   DOMAIN          25..106
FT                   /note="IGFBP N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51323"
FT   DOMAIN          174..256
FT                   /note="Thyroglobulin type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS51162"
FT   REGION          108..177
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        108..117
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   280 AA;  31335 MW;  0D91E4203589A085 CRC64;
     MVLYYGCSLL LLTFLALPGL LLGGVVFHCP SCAAERQAAC PKLATTCTEI VREPGCGCCP
     VCSRLEGEFC GIYTPRCSTG LHCYPTADSE LPLEQLVQGS GRCSHNLTQE HQDKSGSIEE
     LQGTEGPPQK KPTKDASPWM WSKQKALRQA QNELKTKMKT NTRPEEPRTQ RATQSHCQQE
     MDKVLEEISK MTFHDNREPL EDLYELNFPN CDRRGQYNLK QCHMSTHGQR GECWCVNPFT
     GVQITQSTRV RGDPKCSQYV EEQEMATGTL PTVVLPMAET
//
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