ID   VA543_SCODE             Reviewed;         211 AA.
AC   P0DPU2;
DT   10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT   10-APR-2019, sequence version 1.
DT   25-MAY-2022, entry version 6.
DE   RecName: Full=Scoloptoxin SSD43 {ECO:0000303|PubMed:23148443};
DE   AltName: Full=Cysteine-rich venom protein {ECO:0000305};
DE            Short=CRVP {ECO:0000305};
DE   Flags: Precursor;
OS   Scolopendra dehaani (Thai centipede) (Scolopendra subspinipes dehaani).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Myriapoda; Chilopoda;
OC   Pleurostigmophora; Scolopendromorpha; Scolopendridae; Scolopendra.
OX   NCBI_TaxID=2609776;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 21-46, SUBCELLULAR
RP   LOCATION, MASS SPECTROMETRY, AND FUNCTION.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=23148443; DOI=10.1021/pr300881d;
RA   Liu Z.C., Zhang R., Zhao F., Chen Z.M., Liu H.W., Wang Y.J., Jiang P.,
RA   Zhang Y., Wu Y., Ding J.P., Lee W.H., Zhang Y.;
RT   "Venomic and transcriptomic analysis of centipede Scolopendra subspinipes
RT   dehaani.";
RL   J. Proteome Res. 11:6197-6212(2012).
CC   -!- FUNCTION: Shows trypsin inhibiting activity. The protein is highly
CC       thermally stable, since its incubation in boiling water during 10
CC       minutes does not reduce its activity. {ECO:0000269|PubMed:23148443}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23148443}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:23148443}.
CC   -!- PTM: Contains 3 disulfide bonds. {ECO:0000305}.
CC   -!- MASS SPECTROMETRY: Mass=21412.7; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:23148443};
CC   -!- SIMILARITY: Belongs to the CRISP family. Venom allergen 5-like
CC       subfamily. {ECO:0000305}.
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DR   EMBL; KC144061; -; NOT_ANNOTATED_CDS; mRNA.
DR   AlphaFoldDB; P0DPU2; -.
DR   SMR; P0DPU2; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.33.10; -; 1.
DR   InterPro; IPR014044; CAP_domain.
DR   InterPro; IPR035940; CAP_sf.
DR   InterPro; IPR001283; CRISP-related.
DR   InterPro; IPR002413; V5_allergen-like.
DR   PANTHER; PTHR10334; PTHR10334; 1.
DR   Pfam; PF00188; CAP; 1.
DR   PRINTS; PR00838; V5ALLERGEN.
DR   PRINTS; PR00837; V5TPXLIKE.
DR   SMART; SM00198; SCP; 1.
DR   SUPFAM; SSF55797; SSF55797; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Protease inhibitor; Secreted;
KW   Serine protease inhibitor; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000269|PubMed:23148443"
FT   CHAIN           21..211
FT                   /note="Scoloptoxin SSD43"
FT                   /evidence="ECO:0000269|PubMed:23148443"
FT                   /id="PRO_0000446845"
SQ   SEQUENCE   211 AA;  23624 MW;  624A5FB7C95AC53C CRC64;
     MNFVIYGVIV VLTSQLYVDG WGCQMSERGL DKKMKNKILK HHNELRQKVA NGQERGQPTA
     SNMKQLRWND ELAANAQRAA ERCIFQHTSD EGRKTTKYGV AGESMYAGTF SNPLKTAVDM
     WYEEVRDVNP SILDSYDYYP GAVIGHYIQL VWAETEAIGC GYAKSAADGE SYVFCHYAPH
     GLFPQQSVYK RGSPASACKK GQSSRYPGLC K