ID   SL_DEIAC                Reviewed;         155 AA.
AC   Q8JIV8;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   25-MAY-2022, entry version 56.
DE   RecName: Full=Snaclec clone 2100755;
DE   AltName: Full=C-type lectin clone 2100755;
DE   Flags: Precursor;
OS   Deinagkistrodon acutus (Hundred-pace snake) (Agkistrodon acutus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Deinagkistrodon.
OX   NCBI_TaxID=36307;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Yu H., Xiang K., Wang Y., Liu J.;
RT   "Member of C-type lectin family from Deinagkistrodon acutus.";
RL   Submitted (MAR-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   -!- 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; AY091760; AAM22788.1; -; mRNA.
DR   AlphaFoldDB; Q8JIV8; -.
DR   SMR; Q8JIV8; -.
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..155
FT                   /note="Snaclec clone 2100755"
FT                   /id="PRO_0000355234"
FT   DOMAIN          32..145
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..144
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        98
FT                   /note="Interchain"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        119..136
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
SQ   SEQUENCE   155 AA;  17944 MW;  3E935FF53773AB94 CRC64;
     MGRFIFVSFG LLVVFLSLSG TAADCPSGWS SYDGHCYQVF SDLKNWDDAE SFCSGQHEGS
     RLASIHSREE EAFVGKMASR TLKYTSMWLG LNNPWKECKW EWSDDTRLDY KVWTRRPYCT
     VMVVKTDRIF WFNRGCEKSV SFVCKFKAYS EDAAE