ID   SIBD2_CUPSA             Reviewed;          99 AA.
AC   G4V4G0;
DT   19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT   14-DEC-2011, sequence version 1.
DT   25-MAY-2022, entry version 21.
DE   RecName: Full=Single insulin-like growth factor-binding domain protein-2;
DE            Short=SIBD-2;
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=Hemocyte;
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   -!- FUNCTION: Has a role in the innate immune system. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in hemocytes.
CC   -!- MISCELLANEOUS: Does not reveal bactericidal activities against E.coli
CC       and S.aureus. {ECO:0000250}.
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DR   EMBL; HE580154; CCD22033.1; -; mRNA.
DR   AlphaFoldDB; G4V4G0; -.
DR   SMR; G4V4G0; -.
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:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   GO; GO:0001558; P:regulation of cell growth; IEA:InterPro.
DR   InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR   InterPro; IPR000867; IGFBP-like.
DR   InterPro; IPR011390; IGFBP_rP_mac25.
DR   PANTHER; PTHR14186; PTHR14186; 1.
DR   SUPFAM; SSF57184; SSF57184; 1.
DR   PROSITE; PS51323; IGFBP_N_2; 1.
PE   1: Evidence at protein level;
KW   Disulfide bond; Glycoprotein; Immunity; Innate immunity; Secreted; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000250"
FT   CHAIN           19..99
FT                   /note="Single insulin-like growth factor-binding domain
FT                   protein-2"
FT                   /id="PRO_0000425733"
FT   DOMAIN          19..98
FT                   /note="IGFBP N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT   CARBOHYD        20
FT                   /note="O-linked (GalNAc...) serine"
FT   DISULFID        21..44
FT                   /evidence="ECO:0000250"
FT   DISULFID        24..46
FT                   /evidence="ECO:0000250"
FT   DISULFID        29..47
FT                   /evidence="ECO:0000250"
FT   DISULFID        35..50
FT                   /evidence="ECO:0000250"
FT   DISULFID        58..74
FT                   /evidence="ECO:0000250"
FT   DISULFID        68..95
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   99 AA;  10488 MW;  E6EC85501B8A4B48 CRC64;
     MESLFIFAFG MMLSSASALS CIPCVPEECE DPGPCEYGKV LDPCQCCLIC RKGPGEICGG
     PWNLQGVCAE GFACITLSGN PVMNLNGGGQ EVGRCRKKY