SL9_ECHCS
ID SL9_ECHCS Reviewed; 146 AA.
AC Q6X5S4;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 50.
DE RecName: Full=Snaclec 9;
DE AltName: Full=C-type lectin 9;
DE Short=CTL-9;
DE Flags: Precursor;
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; AY254336; AAQ01217.1; -; mRNA.
DR AlphaFoldDB; Q6X5S4; -.
DR SMR; Q6X5S4; -.
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..146
FT /note="Snaclec 9"
FT /id="PRO_0000355270"
FT DOMAIN 32..143
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 25..36
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 53..142
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 98
FT /note="Interchain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 119..134
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
SQ SEQUENCE 146 AA; 16733 MW; 7ECAE5368B91C6A0 CRC64;
MGRFIFISFG LLVVFLSLSG TEAECLPDWF HYEGHCYRVF DEPKTWADAE KFCSEQANGG
HLVSVHSKKE AGLVGVLAYQ TLESPIVWMG LSKIWNQCDW TWTNGAKLKY EAWAEESYCI
HITSKKKEWK SLPCRNYGHF VCKSPA