SL7_DABSI
ID SL7_DABSI Reviewed; 150 AA.
AC Q4PRC6;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 25-MAY-2022, entry version 50.
DE RecName: Full=Snaclec 7;
DE AltName: Full=C-type lectin-like 7;
DE Flags: Precursor;
OS Daboia siamensis (Eastern Russel's viper) (Daboia russelii siamensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Viperinae; Daboia.
OX NCBI_TaxID=343250;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Zhong S., Jin Y., Li D., Wang W., Xiong Y.;
RT "Molecular cloning and sequence analysis of cDNAs encoding seven C-type
RT lectin-like protein subunits from Daboia russellii siamensis.";
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the snaclec family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DQ060420; AAY63876.1; -; mRNA.
DR AlphaFoldDB; Q4PRC6; -.
DR SMR; Q4PRC6; -.
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..150
FT /note="Snaclec 7"
FT /id="PRO_0000017541"
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"
SQ SEQUENCE 150 AA; 18067 MW; 9BBF8F607CB107C0 CRC64;
MGRFISISFG LLVVFLSLSG TGAKQDCLSD WSFYEGYCYK VFNEKKTWED AEKFCNEQVN
GGYLVSFRSS EEMDFVIRMT FPIFRFDFFW IGLRDFWRDC YWRWSDGVNL DYKAWSREPN
CFVSKTTDNQ WLRWNCNDPR YFVCKSRVSC