SL3_SISCA
ID SL3_SISCA Reviewed; 151 AA.
AC B0VXV2;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 25-MAY-2022, entry version 40.
DE RecName: Full=Snaclec 3;
DE AltName: Full=C-type lectin isoform 3;
DE Flags: Precursor;
OS Sistrurus catenatus edwardsii (Desert massasauga) (Crotalophorus
OS edwardsii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Sistrurus.
OX NCBI_TaxID=8762;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Venom gland;
RX PubMed=18096037; DOI=10.1186/1471-2199-8-115;
RA Pahari S., Mackessy S.P., Kini R.M.;
RT "The venom gland transcriptome of the Desert Massasauga rattlesnake
RT (Sistrurus catenatus edwardsii): towards an understanding of venom
RT composition among advanced snakes (Superfamily Colubroidea).";
RL BMC Mol. Biol. 8:115-115(2007).
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 alpha than beta
CC subunits compared to other heterodimer snaclecs.
CC -!- SIMILARITY: Belongs to the snaclec family. {ECO:0000305}.
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DR EMBL; DQ464258; ABG26987.1; -; mRNA.
DR AlphaFoldDB; B0VXV2; -.
DR SMR; B0VXV2; -.
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..151
FT /note="Snaclec 3"
FT /id="PRO_0000355291"
FT DOMAIN 32..150
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..149
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 102
FT /note="Interchain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 125..141
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
SQ SEQUENCE 151 AA; 16939 MW; 1238F903FF8663F2 CRC64;
MGRLVFVSFS LLVVFLSLSG TAADCPSGWS SYEGHCYKPF NEPKNWDDAE RFCLEQAKGG
HLVSIESSEE ADFVAQLVAN NVRRGISYIW IGLRVQGEEK QCSTKWSDGS SVNYENWIEA
LSKTCLGLEQ DTNHKWVNIY CGEINPFVCK A