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Protein

Snaclec coagulation factor X-activating enzyme light chain 2

Gene

LC2

Organism
Daboia siamensis (Eastern Russel's viper) (Daboia russelii siamensis)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Regulatory subunit of the blood coagulation factor X- and IX-activating enzyme. The enzyme activates coagulation factor X (F10) by cleaving the Arg-Ile bond and is also able to activate coagulation factor IX (F9) and protein S (PROS1) by specific cleavage of Arg-Ile and Arg-Val bonds. May serve as an exosite by which the enzyme recognizes and binds to the Gla domain of factor X (F10) and factor IX (F9) in a calcium-dependent manner.1 Publication

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Blood coagulation cascade activating toxin, Hemostasis impairing toxin, Toxin

Keywords - Ligandi

Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Snaclec coagulation factor X-activating enzyme light chain 2
Alternative name(s):
C-type lectin-like protein subunit 1
Coagulation factor X-activating enzyme beta-chain
RVV-X light chain 2
Gene namesi
Name:LC2
OrganismiDaboia siamensis (Eastern Russel's viper) (Daboia russelii siamensis)
Taxonomic identifieri343250 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaViperidaeViperinaeDaboia

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 24242 PublicationsAdd
BLAST
Chaini25 – 158134Snaclec coagulation factor X-activating enzyme light chain 2PRO_0000017535Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi27 ↔ 38PROSITE-ProRule annotation1 Publication
Disulfide bondi55 ↔ 152PROSITE-ProRule annotation1 Publication
Glycosylationi82 – 821N-linked (GlcNAc...) (complex)1 Publication
Disulfide bondi104 – 104Interchain (with C-100 in coagulation factor X-activating enzyme light chain LC1)PROSITE-ProRule annotation1 Publication
Disulfide bondi127 ↔ 144PROSITE-ProRule annotation1 Publication
Disulfide bondi158 – 158Interchain (with C-391 in coagulation factor X-activating enzyme heavy chain)PROSITE-ProRule annotation1 Publication

Post-translational modificationi

N-glycosylated; probably required for conformation. Removal of easily accessible sugars does not change its functional capacity, but removal of the core sugars with N-glycanase causes a virtually complete loss of enzyme activity, apparently as a result of major conformational changes in the molecule. Not O-glycosylated.2 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein

Expressioni

Tissue specificityi

Expressed by the venom gland.

Interactioni

Subunit structurei

Heterotrimer; disulfide-linked. The heterotrimer consists of 1 heavy chain (a metalloproteinase) and 2 light chains: LC1 and LC2.2 Publications

Structurei

Secondary structure

1
158
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni28 – 303Combined sources
Beta strandi31 – 344Combined sources
Beta strandi37 – 4711Combined sources
Helixi48 – 558Combined sources
Turni58 – 614Combined sources
Helixi70 – 8112Combined sources
Beta strandi90 – 923Combined sources
Beta strandi95 – 973Combined sources
Turni102 – 1054Combined sources
Helixi121 – 1233Combined sources
Beta strandi127 – 1315Combined sources
Helixi132 – 1343Combined sources
Beta strandi139 – 1424Combined sources
Beta strandi146 – 1549Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2E3XX-ray2.91B25-158[»]
ProteinModelPortaliQ4PRD2.
SMRiQ4PRD2. Positions 26-158.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ4PRD2.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini34 – 153120C-type lectinPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the snaclec family.Curated
Contains 1 C-type lectin domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

HOVERGENiHBG004151.

Family and domain databases

Gene3Di3.10.100.10. 1 hit.
InterProiIPR001304. C-type_lectin.
IPR016186. C-type_lectin-like.
IPR018378. C-type_lectin_CS.
IPR016187. C-type_lectin_fold.
[Graphical view]
PfamiPF00059. Lectin_C. 1 hit.
[Graphical view]
SMARTiSM00034. CLECT. 1 hit.
[Graphical view]
SUPFAMiSSF56436. SSF56436. 1 hit.
PROSITEiPS00615. C_TYPE_LECTIN_1. 1 hit.
PS50041. C_TYPE_LECTIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q4PRD2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGRFISVSFG LLVVFLSLSG TGAGLDCPPD SSLYRYFCYR VFKEHKTWEA
60 70 80 90 100
AERFCMEHPN NGHLVSIESM EEAEFVAKLL SNTTGKFITH FWIGLMIKDK
110 120 130 140 150
EQECSSEWSD GSSVSYDKLG KQEFRKCFVL EKESGYRMWF NRNCEERYLF

VCKVPPEC
Length:158
Mass (Da):18,337
Last modified:July 19, 2005 - v1
Checksum:i931BCC243854FB85
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti26 – 261D → L AA sequence (PubMed:8144654).Curated
Sequence conflicti30 – 301D → P AA sequence (PubMed:8144654).Curated
Sequence conflicti33 – 331L → P AA sequence (PubMed:8144654).Curated
Sequence conflicti38 – 381C → F AA sequence (PubMed:8144654).Curated
Sequence conflicti40 – 401R → W AA sequence (PubMed:8144654).Curated
Sequence conflicti44 – 441E → L AA sequence (PubMed:8144654).Curated
Sequence conflicti122 – 1221Q → E in AAW69869 (PubMed:18616470).Curated
Sequence conflicti149 – 1491L → V in AAW69869 (PubMed:18616470).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ060414 mRNA. Translation: AAY63870.1.
AY734997 mRNA. Translation: AAW69869.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ060414 mRNA. Translation: AAY63870.1.
AY734997 mRNA. Translation: AAW69869.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2E3XX-ray2.91B25-158[»]
ProteinModelPortaliQ4PRD2.
SMRiQ4PRD2. Positions 26-158.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG004151.

Miscellaneous databases

EvolutionaryTraceiQ4PRD2.

Family and domain databases

Gene3Di3.10.100.10. 1 hit.
InterProiIPR001304. C-type_lectin.
IPR016186. C-type_lectin-like.
IPR018378. C-type_lectin_CS.
IPR016187. C-type_lectin_fold.
[Graphical view]
PfamiPF00059. Lectin_C. 1 hit.
[Graphical view]
SMARTiSM00034. CLECT. 1 hit.
[Graphical view]
SUPFAMiSSF56436. SSF56436. 1 hit.
PROSITEiPS00615. C_TYPE_LECTIN_1. 1 hit.
PS50041. C_TYPE_LECTIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSLLC2_DABSI
AccessioniPrimary (citable) accession number: Q4PRD2
Secondary accession number(s): A9UKE2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: July 19, 2005
Last modified: October 14, 2015
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Binding to prothrombin and protein C (PROC) is hardly detectable.1 Publication

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.