SIBD1_CUPSA
ID SIBD1_CUPSA Reviewed; 97 AA.
AC G4V4F9;
DT 19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 25-MAY-2022, entry version 27.
DE RecName: Full=Single insulin-like growth factor-binding domain protein-1;
DE Short=SIBD-1;
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], PROTEIN SEQUENCE OF 20-50, FUNCTION, TISSUE
RP SPECIFICITY, MASS SPECTROMETRY, AND GLYCOSYLATION AT THR-21.
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).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 20-97, AND GLYCOSYLATION AT
RP THR-21.
RX PubMed=22622866; DOI=10.1002/prot.24119;
RA Trachsel C., Widmer C., Kampfer U., Buhr C., Baumann T., Kuhn-Nentwig L.,
RA Schurch S., Schaller J., Baumann U.;
RT "Structural and biochemical characterization of native and recombinant
RT single insulin-like growth factor-binding domain protein (SIBD-1) from the
RT Central American hunting spider Cupiennius salei (Ctenidae).";
RL Proteins 80:2323-2329(2012).
CC -!- FUNCTION: Has a role in the innate immune system.
CC {ECO:0000269|PubMed:21888974}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed in hemocytes.
CC {ECO:0000269|PubMed:21888974}.
CC -!- MASS SPECTROMETRY: Mass=8676.08; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:21888974};
CC -!- MISCELLANEOUS: Does not reveal bactericidal activities against E.coli
CC and S.aureus. {ECO:0000305|PubMed:21888974}.
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DR EMBL; HE580153; CCD22032.1; -; mRNA.
DR PDB; 3ZXB; X-ray; 2.55 A; A/B/C/D=20-97.
DR PDB; 3ZXC; X-ray; 1.40 A; A/B=20-97.
DR PDBsum; 3ZXB; -.
DR PDBsum; 3ZXC; -.
DR AlphaFoldDB; G4V4F9; -.
DR SMR; G4V4F9; -.
DR iPTMnet; G4V4F9; -.
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 SMART; SM00121; IB; 1.
DR SUPFAM; SSF57184; SSF57184; 1.
DR PROSITE; PS51323; IGFBP_N_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Immunity; Innate immunity; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:21888974"
FT CHAIN 20..97
FT /note="Single insulin-like growth factor-binding domain
FT protein-1"
FT /id="PRO_0000425732"
FT DOMAIN 20..96
FT /note="IGFBP N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT CARBOHYD 21
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:21888974,
FT ECO:0000269|PubMed:22622866"
FT DISULFID 22..45
FT DISULFID 25..47
FT DISULFID 30..48
FT DISULFID 36..51
FT DISULFID 59..75
FT DISULFID 69..93
FT HELIX 27..29
FT /evidence="ECO:0007829|PDB:3ZXC"
FT STRAND 40..42
FT /evidence="ECO:0007829|PDB:3ZXC"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:3ZXB"
FT STRAND 48..51
FT /evidence="ECO:0007829|PDB:3ZXC"
FT STRAND 57..61
FT /evidence="ECO:0007829|PDB:3ZXC"
FT HELIX 62..64
FT /evidence="ECO:0007829|PDB:3ZXC"
FT STRAND 73..77
FT /evidence="ECO:0007829|PDB:3ZXC"
FT STRAND 90..95
FT /evidence="ECO:0007829|PDB:3ZXC"
SQ SEQUENCE 97 AA; 10219 MW; EE49AB8162199678 CRC64;
MKTLFVFAVG IMLSMRASAF TCPECRPELC GDPGYCEYGT TKDACDCCPV CFQGPGGYCG
GPEDVFGICA DGFACVPLVG ERDSQDPEIV GTCVKIP