ID   SL1C2_VIPAA             Reviewed;          11 AA.
AC   P0C8J3;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   26-FEB-2020, entry version 23.
DE   RecName: Full=Snaclec factor X-activator 1 light chain 2;
DE            Short=VAFXA-I LC2;
DE   Flags: Fragment;
GN   Name=LC2;
OS   Vipera ammodytes ammodytes (Western sand viper).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Viperinae; Vipera.
OX   NCBI_TaxID=8705;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Venom;
RX   PubMed=18760294; DOI=10.1016/j.toxicon.2008.07.015;
RA   Leonardi A., Fox J.W., Trampus-Bakija A., Krizaj I.;
RT   "Two coagulation factor X activators from Vipera a. ammodytes venom with
RT   potential to treat patients with dysfunctional factors IXa or VIIa.";
RL   Toxicon 52:628-637(2008).
CC   -!- FUNCTION: Regulatory subunit of the blood coagulation factor X-
CC       activating enzyme. Activates coagulation factor X (F10) in a calcium-
CC       dependent manner by cleaving the Arg-Ile bond at position 234. Weakly
CC       hydrolyzes insulin B chain, fibrinogen and some components of the
CC       extracellular matrix in vitro, but does not activate prothrombin or
CC       plasminogen.
CC   -!- SUBUNIT: Heterotrimer; disulfide-linked. The heterotrimer consists of 1
CC       heavy chain (a metalloproteinase) and 2 light chains: LC1 and LC2.
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   -!- SIMILARITY: Belongs to the snaclec family. {ECO:0000305}.
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DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; Metal-binding; Secreted; Toxin.
FT   CHAIN           1..>11
FT                   /note="Snaclec factor X-activator 1 light chain 2"
FT                   /id="PRO_0000355313"
FT   DOMAIN          10..>11
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   NON_TER         11
SQ   SEQUENCE   11 AA;  1273 MW;  2F487706F5BAB777 CRC64;
     LFDPPDSXPX Y