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SLLC1_MACLB
ID   SLLC1_MACLB             Reviewed;         146 AA.
AC   Q7T045;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   25-MAY-2022, entry version 67.
DE   RecName: Full=Snaclec coagulation factor X-activating enzyme light chain 1;
DE   AltName: Full=VL factor X activator light chain 1;
DE            Short=VLFXA light chain 1;
DE   Contains:
DE     RecName: Full=Snaclec coagulation factor X-activating enzyme light chain 1 alternate form;
DE   Flags: Precursor;
GN   Name=LC1;
OS   Macrovipera lebetina (Levantine viper) (Vipera lebetina).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Viperinae; Macrovipera.
OX   NCBI_TaxID=8709;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 24-43, AND SUBUNIT.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=15450849; DOI=10.1016/j.bbapap.2004.07.007;
RA   Siigur E., Aaspollu A., Trummal K., Tonismaegi K., Tammiste I.,
RA   Kalkkinen N., Siigur J.;
RT   "Factor X activator from Vipera lebetina venom is synthesized from
RT   different genes.";
RL   Biochim. Biophys. Acta 1702:41-51(2004).
RN   [2]
RP   FUNCTION, SUBUNIT, AND GLYCOSYLATION.
RC   TISSUE=Venom;
RX   PubMed=11731090; DOI=10.1016/s0304-4165(01)00206-9;
RA   Siigur E., Tonismagi K., Trummal K., Samel M., Vija H., Subbi J.,
RA   Siigur J.;
RT   "Factor X activator from Vipera lebetina snake venom, molecular
RT   characterization and substrate specificity.";
RL   Biochim. Biophys. Acta 1568:90-98(2001).
CC   -!- FUNCTION: Regulatory subunit of the blood coagulation factor X-
CC       activating enzyme. Activates coagulation factor X (F10) by cleaving the
CC       Arg-Ile bond at position 234, activates coagulation factor IX (F9) by
CC       cleaving the Arg-Val bond at position 226 and is also able to activate
CC       protein C (PROC). May serve as an exosite by which the enzyme
CC       recognizes and binds to the Gla domain of factor X (F10) in a calcium-
CC       dependent manner. {ECO:0000269|PubMed:11731090}.
CC   -!- SUBUNIT: Heterotrimer; disulfide-linked. The heterotrimer consists of 1
CC       heavy chain (a metalloproteinase) and 2 light chains: LC1 and LC2.
CC       {ECO:0000269|PubMed:11731090, ECO:0000269|PubMed:15450849}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- MISCELLANEOUS: Calcium is required for ligand binding. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the snaclec family. {ECO:0000305}.
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DR   EMBL; AY339163; AAQ17468.1; -; mRNA.
DR   AlphaFoldDB; Q7T045; -.
DR   SMR; Q7T045; -.
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.
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   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; Signal; Toxin.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000269|PubMed:15450849"
FT   CHAIN           24..146
FT                   /note="Snaclec coagulation factor X-activating enzyme light
FT                   chain 1"
FT                   /id="PRO_0000017533"
FT   CHAIN           25..146
FT                   /note="Snaclec coagulation factor X-activating enzyme light
FT                   chain 1 alternate form"
FT                   /id="PRO_0000017534"
FT   DOMAIN          34..145
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   CARBOHYD        47
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
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 (with C-104 in coagulation factor X-
FT                   activating enzyme light chain LC2)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        121..136
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
SQ   SEQUENCE   146 AA;  16581 MW;  96F3157F2EC0DC46 CRC64;
     MGRFISVSFG LLVVFLSLSG TGADFDCPSD WVSYDQHCYK AFNDLKNWTD AEKFCTEQNK
     GSHLVSLHSS EEEDFVVNLA SQSLQYPVAW IGLGNMWKEC RSEWSDGGNV KYKALAEESY
     CLLINTHKKG WRSMTCNNMA HVICKF
 
 
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