SLLC1_DABSI
ID SLLC1_DABSI Reviewed; 146 AA.
AC Q4PRD1; A9UKE3; Q7LZ72;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2013, sequence version 2.
DT 25-MAY-2022, entry version 72.
DE RecName: Full=Snaclec coagulation factor X-activating enzyme light chain 1;
DE AltName: Full=C-type lectin-like protein subunit 2;
DE AltName: Full=Coagulation factor X-activating enzyme gamma-chain;
DE AltName: Full=RVV-X light chain 1;
DE Flags: Precursor;
GN Name=LC1;
OS Daboia siamensis (Eastern Russel's viper) (Daboia russelii siamensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Viperinae; Daboia.
OX NCBI_TaxID=343250;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RA Zhong S., Jin Y., Li D., Wang W., Xiong Y.;
RT "Molecular cloning and sequence analysis of cDNAs encoding seven C-type
RT lectin-like protein subunits from Daboia russellii siamensis.";
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC TISSUE=Venom, and Venom gland;
RX PubMed=18616470; DOI=10.1111/j.1742-4658.2008.06540.x;
RA Chen H.S., Chen J.M., Lin C.W., Khoo K.H., Tsai I.H.;
RT "New insights into the functions and N-glycan structures of factor X
RT activator from Russell's viper venom.";
RL FEBS J. 275:3944-3958(2008).
RN [3]
RP PROTEIN SEQUENCE OF 24-146, CALCIUM-BINDING, ENZYME ACTIVITY, AND
RP GLYCOSYLATION.
RC TISSUE=Venom;
RX PubMed=1629211; DOI=10.1016/s0021-9258(19)49685-3;
RA Takeya H., Nishida S., Miyata T., Kawada S., Saisaka Y., Morita T.,
RA Iwanaga S.;
RT "Coagulation factor X activating enzyme from Russell's viper venom (RVV-X).
RT A novel metalloproteinase with disintegrin (platelet aggregation
RT inhibitor)-like and C-type lectin-like domains.";
RL J. Biol. Chem. 267:14109-14117(1992).
RN [4]
RP PROTEIN SEQUENCE OF 24-51, ENZYME ACTIVITY, SUBUNIT, AND GLYCOSYLATION AT
RP ASN-47.
RC TISSUE=Venom;
RX PubMed=8144654; DOI=10.1016/s0021-9258(17)34108-x;
RA Gowda D.C., Jackson C.M., Hensley P., Davidson E.A.;
RT "Factor X-activating glycoprotein of Russell's viper venom. Polypeptide
RT composition and characterization of the carbohydrate moieties.";
RL J. Biol. Chem. 269:10644-10650(1994).
RN [5]
RP ROLE OF GLYCOSYLATION.
RX PubMed=8639544; DOI=10.1021/bi953043e;
RA Gowda D.C., Jackson C.M., Kurzban G.P., McPhie P., Davidson E.A.;
RT "Core sugar residues of the N-linked oligosaccharides of Russell's viper
RT venom factor X-activator maintain functionally active polypeptide
RT structure.";
RL Biochemistry 35:5833-5837(1996).
RN [6]
RP REVIEW.
RX PubMed=11910189; DOI=10.1159/000048067;
RA Tans G., Rosing J.;
RT "Snake venom activators of factor X: an overview.";
RL Haemostasis 31:225-233(2001).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.91 ANGSTROMS) OF 25-146 IN COMPLEX WITH LC2,
RP SUBUNIT, GLYCOSYLATION AT ASN-47, AND DISULFIDE BONDS.
RX PubMed=18060879; DOI=10.1016/j.febslet.2007.11.062;
RA Takeda S., Igarashi T., Mori H.;
RT "Crystal structure of RVV-X: an example of evolutionary gain of specificity
RT by ADAM proteinases.";
RL FEBS Lett. 581:5859-5864(2007).
CC -!- FUNCTION: Regulatory subunit of the blood coagulation factor X- and IX-
CC activating enzyme. The enzyme activates coagulation factor X (F10) by
CC cleaving the Arg-Ile bond and is also able to activate coagulation
CC factor IX (F9) and protein S (PROS1) by specific cleavage of Arg-Ile
CC and Arg-Val bonds. May serve as an exosite by which the enzyme
CC recognizes and binds to the Gla domain of factor X (F10) and factor IX
CC (F9) in a calcium-dependent manner. {ECO:0000269|PubMed:18616470}.
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:18060879, ECO:0000269|PubMed:8144654}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- PTM: N-glycosylated; probably required for conformation. Removal of
CC easily accessible sugars does not change its functional capacity, but
CC removal of the core sugars with N-glycanase causes a virtually complete
CC loss of enzyme activity, apparently as a result of major conformational
CC changes in the molecule. Not O-glycosylated.
CC {ECO:0000269|PubMed:1629211, ECO:0000269|PubMed:18060879,
CC ECO:0000269|PubMed:8144654}.
CC -!- MISCELLANEOUS: Binding to prothrombin and protein C (PROC) is hardly
CC detectable. {ECO:0000305|PubMed:18616470}.
CC -!- SIMILARITY: Belongs to the snaclec family. {ECO:0000305}.
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DR EMBL; DQ060415; AAY63871.1; -; mRNA.
DR EMBL; AY734998; AAW69870.1; -; mRNA.
DR PIR; B42972; B42972.
DR PDB; 2E3X; X-ray; 2.91 A; C=25-146.
DR PDBsum; 2E3X; -.
DR AlphaFoldDB; Q4PRD1; -.
DR SMR; Q4PRD1; -.
DR iPTMnet; Q4PRD1; -.
DR BRENDA; 3.4.24.58; 6667.
DR EvolutionaryTrace; Q4PRD1; -.
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 3D-structure; 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:1629211,
FT ECO:0000269|PubMed:8144654"
FT CHAIN 24..146
FT /note="Snaclec coagulation factor X-activating enzyme light
FT chain 1"
FT /id="PRO_0000017532"
FT DOMAIN 34..145
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT CARBOHYD 47
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:18060879,
FT ECO:0000269|PubMed:8144654"
FT DISULFID 27..38
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT ECO:0000269|PubMed:18060879"
FT DISULFID 55..144
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT ECO:0000269|PubMed:18060879"
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 ECO:0000269|PubMed:18060879"
FT DISULFID 121..136
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT ECO:0000269|PubMed:18060879"
FT CONFLICT 11
FT /note="C -> W (in Ref. 1; AAY63871)"
FT /evidence="ECO:0000305"
FT CONFLICT 74
FT /note="E -> K (in Ref. 1; AAY63871)"
FT /evidence="ECO:0000305"
FT CONFLICT 130
FT /note="E -> V (in Ref. 1; AAY63871)"
FT /evidence="ECO:0000305"
FT STRAND 32..34
FT /evidence="ECO:0007829|PDB:2E3X"
FT STRAND 37..41
FT /evidence="ECO:0007829|PDB:2E3X"
FT HELIX 48..58
FT /evidence="ECO:0007829|PDB:2E3X"
FT HELIX 70..83
FT /evidence="ECO:0007829|PDB:2E3X"
FT STRAND 85..95
FT /evidence="ECO:0007829|PDB:2E3X"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:2E3X"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:2E3X"
FT STRAND 120..125
FT /evidence="ECO:0007829|PDB:2E3X"
FT TURN 126..128
FT /evidence="ECO:0007829|PDB:2E3X"
FT STRAND 131..135
FT /evidence="ECO:0007829|PDB:2E3X"
FT STRAND 143..145
FT /evidence="ECO:0007829|PDB:2E3X"
SQ SEQUENCE 146 AA; 16871 MW; A26EBD406B9F016E CRC64;
MGRFISVSFG CLVVFLSLSG TEAVLDCPSG WLSYEQHCYK GFNDLKNWTD AEKFCTEQKK
GSHLVSLHSR EEEEFVVNLI SENLEYPATW IGLGNMWKDC RMEWSDRGNV KYKALAEESY
CLIMITHEKE WKSMTCNFIA PVVCKF
