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 27-MAR-2024, entry version 70.
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 GlyCosmos; Q7T045; 1 site, No reported glycans.
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; Mannose-Binding Protein A, subunit A; 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 PANTHER; PTHR22803:SF124; C-TYPE LECTIN DOMAIN FAMILY 19 MEMBER A-RELATED; 1.
DR PANTHER; PTHR22803; MANNOSE, PHOSPHOLIPASE, LECTIN RECEPTOR RELATED; 1.
DR Pfam; PF00059; Lectin_C; 1.
DR SMART; SM00034; CLECT; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 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
//
