SL1_CRODU
ID SL1_CRODU Reviewed; 158 AA.
AC Q719L9;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 54.
DE RecName: Full=Snaclec crotocetin-1;
DE Short=CRC1;
DE Flags: Precursor;
OS Crotalus durissus terrificus (South American rattlesnake).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Crotalus.
OX NCBI_TaxID=8732;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RA Radis-Baptista G., Camargo A.C.M., Yamane T.;
RL Submitted (AUG-2002) 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 -!- 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; AF541883; AAQ11364.1; -; mRNA.
DR AlphaFoldDB; Q719L9; -.
DR SMR; Q719L9; -.
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:0000250"
FT CHAIN 24..158
FT /note="Snaclec crotocetin-1"
FT /id="PRO_0000355263"
FT DOMAIN 34..153
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..152
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 104
FT /note="Interchain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 127..144
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
SQ SEQUENCE 158 AA; 18199 MW; 9F43B3164691D1E9 CRC64;
MGRFIFVSFG LLVVFLSLSG TGADFDCPSG WSAYDQYCYR VIKQLKTWED AEWFCTKQAK
GAHLVSVESA GEADFVAQLV AENIKQNKYY VWIGLRIQNK GQQCSTKWSD GSSVNYENLL
KSYSKKCFGL KKETEFLQWY NTDCEEKNLF VCKFPPQR