ID   SL3_ECHCS               Reviewed;         148 AA.
AC   Q6X5S8;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 55.
DE   RecName: Full=Snaclec 3;
DE   AltName: Full=C-type lectin 3;
DE            Short=CTL-3;
DE   Flags: Precursor; Fragment;
OS   Echis carinatus sochureki (Saw-scaled viper).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Viperinae; Echis.
OX   NCBI_TaxID=124223;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=14557069; DOI=10.1016/s0378-1119(03)00716-9;
RA   Harrison R.A., Oliver J., Hasson S.S., Bharati K., Theakston R.D.G.;
RT   "Novel sequences encoding venom C-type lectins are conserved in
RT   phylogenetically and geographically distinct Echis and Bitis viper
RT   species.";
RL   Gene 315:95-102(2003).
CC   -!- FUNCTION: Interferes with one step of hemostasis (modulation of
CC       platelet aggregation, or coagulation cascade, for example).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Heterodimer; disulfide-linked. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- MISCELLANEOUS: Shows greater sequence similarity to the beta than alpha
CC       subunits compared to other heterodimer snaclecs.
CC   -!- SIMILARITY: Belongs to the snaclec family. {ECO:0000305}.
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DR   EMBL; AY254332; AAQ01213.1; -; mRNA.
DR   AlphaFoldDB; Q6X5S8; -.
DR   SMR; Q6X5S8; -.
DR   MEROPS; I63.002; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.10.100.10; -; 1.
DR   InterPro; IPR001304; C-type_lectin-like.
DR   InterPro; IPR016186; C-type_lectin-like/link_sf.
DR   InterPro; IPR018378; C-type_lectin_CS.
DR   InterPro; IPR016187; CTDL_fold.
DR   Pfam; PF00059; Lectin_C; 1.
DR   SMART; SM00034; CLECT; 1.
DR   SUPFAM; SSF56436; SSF56436; 1.
DR   PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
DR   PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Hemostasis impairing toxin; Secreted; Signal; Toxin.
FT   SIGNAL          <1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..148
FT                   /note="Snaclec 3"
FT                   /id="PRO_0000355268"
FT   DOMAIN          34..145
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        27..38
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        55..144
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        100
FT                   /note="Interchain"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        121..136
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   NON_TER         1
SQ   SEQUENCE   148 AA;  16445 MW;  393DE118A9652017 CRC64;
     WGDSSSSASA CWSCSSPLSG TEAGVCCPLG WSGYDQNCYK AFEELMNWAD AEKFCTQQHK
     GSHLVSLHNI AEADFVVKKI VSVLKDGVIW MGLNDVWNEC NWGWTDGAQL DYKAWNVESN
     CFIFKTAENH WSRTDCSGTH SFVCKSPA