ID A0A3B3RIQ2_9TELE Unreviewed; 280 AA.
AC A0A3B3RIQ2;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Insulin like growth factor binding protein 3 {ECO:0000313|Ensembl:ENSPKIP00000018512.1};
GN Name=IGFBP3 {ECO:0000313|Ensembl:ENSPKIP00000018512.1};
OS Paramormyrops kingsleyae.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000018512.1, ECO:0000313|Proteomes:UP000261540};
RN [1] {ECO:0000313|Ensembl:ENSPKIP00000018512.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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; A0A3B3RIQ2; -.
DR Ensembl; ENSPKIT00000042976.1; ENSPKIP00000018512.1; ENSPKIG00000004049.1.
DR GeneTree; ENSGT00940000158092; -.
DR OrthoDB; 5394492at2759; -.
DR Proteomes; UP000261540; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005520; F:insulin-like growth factor binding; IEA:InterPro.
DR CDD; cd00191; TY; 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; 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; INSULIN-LIKE GROWTH FACTOR BINDING PROTEIN; 1.
DR PANTHER; PTHR11551:SF3; INSULIN-LIKE GROWTH FACTOR-BINDING PROTEIN 3; 1.
DR Pfam; PF00219; IGFBP; 1.
DR Pfam; PF00086; Thyroglobulin_1; 1.
DR PRINTS; PR01976; IGFBPFAMILY.
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; PS00222; IGFBP_N_1; 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 Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..280
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017252806"
FT DOMAIN 24..105
FT /note="IGFBP N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51323"
FT DOMAIN 199..274
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000259|PROSITE:PS51162"
FT REGION 107..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 280 AA; 30955 MW; AD0343FF1324281B CRC64;
MTRRLAALWL TAAALMRIAD AVGPVVQCGP CDPGALEQCK PLPANCVEKV REPGCGCCMT
CALAEGELCG VYTRRCGAGM TCQLQPGEAR QLQALLEGRG VCSKTALKKT PRLPPAGEQG
RPEHPGLTEE PSGSRAATPD PRIVTRVPEH RTPHHNPKAE VIRREQTKKT HSFKVQPVPE
YEHKEVHNFS VDFRRELEYG PCRTAMISIL KRLKASDTLN PRRLSIPNCD KKGFYKKKQC
RPSKGRKRGI CWCVDRYGQT LPGFDGSKKD GTQCQGLDNK
//