ID   SLLC2_VIPAP             Reviewed;          13 AA.
AC   Q7LZ24;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   26-FEB-2020, entry version 32.
DE   RecName: Full=Snaclec coagulation factor X-activating enzyme light chain 2;
DE   AltName: Full=Factor X activator LC2;
DE   Flags: Fragment;
OS   Vipera aspis aspis (Aspic viper).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Viperinae; Vipera.
OX   NCBI_TaxID=194601;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Venom;
RX   PubMed=2282962; DOI=10.1016/0020-711x(90)90213-m;
RA   Komori Y., Nikai T., Sugihara H.;
RT   "Isolation and characterization of factor X activator from the venom of
RT   Vipera aspis aspis.";
RL   Int. J. Biochem. 22:1053-1060(1990).
CC   -!- FUNCTION: Regulatory subunit of coagulation factor X-activating enzyme,
CC       a zinc-protease enzyme that impairs hemostasis in envenomed animal.
CC       Activates coagulation factor X (F10) in a calcium-dependent manner
CC       probably by cleaving the Arg-Ile bond at position 234.
CC   -!- SUBUNIT: Heterotrimer; disulfide-linked. The heterotrimer consists of 1
CC       heavy chain (a metalloproteinase) and 2 light chains: LC1 and LC2 (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- PTM: N-glycosylated. {ECO:0000250}.
CC   -!- MISCELLANEOUS: Calcium is required for ligand binding.
CC   -!- MISCELLANEOUS: The molecular weight was determined to be 75 kDa with an
CC       isoelectric point of 4.6. Upon reduction, this activator migrated as
CC       two bands of 16 kDa and 14 kDa.
CC   -!- SIMILARITY: Belongs to the snaclec family. {ECO:0000305}.
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DR   PIR; A60379; A60379.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Blood coagulation cascade activating toxin; Calcium;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein;
KW   Hemostasis impairing toxin; Lectin; Metal-binding; Secreted; Toxin.
FT   CHAIN           1..>13
FT                   /note="Snaclec coagulation factor X-activating enzyme light
FT                   chain 2"
FT                   /id="PRO_0000408029"
FT   DOMAIN          11..>13
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   NON_TER         13
SQ   SEQUENCE   13 AA;  1435 MW;  9C9866844BA67865 CRC64;
     AFCCPSGWSA YDQ