IGFBP_CUPSA
ID IGFBP_CUPSA Reviewed; 261 AA.
AC G4V4G1;
DT 19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 25-MAY-2022, entry version 29.
DE RecName: Full=Insulin-like growth factor-binding protein-related protein 1;
DE Short=IGFBP-rP1;
DE Flags: Precursor;
OS Cupiennius salei (American wandering spider).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae;
OC Araneomorphae; Entelegynae; Lycosoidea; Ctenidae; Cupiennius.
OX NCBI_TaxID=6928;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX PubMed=21888974; DOI=10.1016/j.ibmb.2011.08.003;
RA Kuhn-Nentwig L., Largiader C.R., Streitberger K., Chandru S., Baumann T.,
RA Kampfer U., Schaller J., Schurch S., Nentwig W.;
RT "Purification, cDNA structure and biological significance of a single
RT insulin-like growth factor-binding domain protein (SIBD-1) identified in
RT the hemocytes of the spider Cupiennius salei.";
RL Insect Biochem. Mol. Biol. 41:891-901(2011).
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
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DR EMBL; HE580155; CCD22034.1; -; mRNA.
DR AlphaFoldDB; G4V4G1; -.
DR SMR; G4V4G1; -.
DR ArachnoServer; AS001595; IGFBP-rP1-1-Cupiennius salei.
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:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0001558; P:regulation of cell growth; IEA:InterPro.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR000867; IGFBP-like.
DR InterPro; IPR011390; IGFBP_rP_mac25.
DR InterPro; IPR002350; Kazal_dom.
DR InterPro; IPR036058; Kazal_dom_sf.
DR PANTHER; PTHR14186; PTHR14186; 1.
DR Pfam; PF00219; IGFBP; 1.
DR Pfam; PF00050; Kazal_1; 1.
DR SMART; SM00121; IB; 1.
DR SMART; SM00409; IG; 1.
DR SMART; SM00408; IGc2; 1.
DR SMART; SM00280; KAZAL; 1.
DR SUPFAM; SSF100895; SSF100895; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR SUPFAM; SSF57184; SSF57184; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS51323; IGFBP_N_2; 1.
DR PROSITE; PS51465; KAZAL_2; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Immunoglobulin domain; Protease inhibitor;
KW Secreted; Serine protease inhibitor; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..261
FT /note="Insulin-like growth factor-binding protein-related
FT protein 1"
FT /id="PRO_0000425734"
FT DOMAIN 18..101
FT /note="IGFBP N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT DOMAIN 70..141
FT /note="Kazal-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DOMAIN 143..243
FT /note="Ig-like C2-type"
FT SITE 100..101
FT /note="Reactive bond"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT CARBOHYD 154
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 98..118
FT /evidence="ECO:0000250"
FT DISULFID 107..139
FT /evidence="ECO:0000250"
FT DISULFID 164..227
FT /evidence="ECO:0000250"
SQ SEQUENCE 261 AA; 28623 MW; 462256005E9FA3D8 CRC64;
MWIPLLLVAL VVPAIRCERK CGECNPEKCQ PPSEECLAGL VKDLCGCCYV CGRREGELCD
GDFLPIPYRN RGHGPCGEYL ECRPRTDLAP GDPPEAMCVC LKTETLCGSD GKTYQNECQL
TEARYKQRDG LRAMHRGPCK SAPKITSPPE EASNYTGGNI AMSCEATGWP IPVFEWRVDI
GDGNTIPLPS DDPKVSVQSR GGPSKYEVTS WLQLLSIQPK DDATYWCIAK NDEGESSAAA
RVVVLDFRGS QTSQKGRDND L
