SL8_BITAR
ID SL8_BITAR Reviewed; 148 AA.
AC Q6X5T1;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 53.
DE RecName: Full=Snaclec 8;
DE AltName: Full=C-type lectin 8;
DE Short=CTL-8;
DE Flags: Precursor;
OS Bitis arietans (African puff adder).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Viperinae; Bitis.
OX NCBI_TaxID=8692;
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; AY254329; AAQ01210.1; -; mRNA.
DR AlphaFoldDB; Q6X5T1; -.
DR SMR; Q6X5T1; -.
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 8"
FT /id="PRO_0000355247"
FT DOMAIN 34..145
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 26
FT /note="Interchain"
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"
SQ SEQUENCE 148 AA; 16673 MW; C46256A79BF16328 CRC64;
MGRFIFVSFG LLVVFLSLSG TEAGVCCPLG WSGYDQNCYK AFEELMNWAD AEKFCTQQHK
GSHLVSLHNI AEADFVVKKI VSVLKDGVIW MGLNDVWNEC NWGWTDGAQL DYKAWNVESN
CFIFKTAENH WSRTDCSGTH SFVCKSPA