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Protein

Snaclec anticoagulant protein subunit A

Gene
N/A
Organism
Deinagkistrodon acutus (Hundred-pace snake) (Agkistrodon acutus)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Anticoagulant protein which binds to the gamma-carboxyglutamic acid-domain regions of factors IX and factor X in the presence of calcium with a 1 to 1 stoichiometry. Also inhibits platelet aggregation by binding to platelet glycoprotein Ibalpha (GP1BA) and functioning as a blocker of vWF. Is devoid of hemorrhagic and lethal activities. Possess antithrombotic and thrombolytic activities. Also hydrolyzes the Aalpha-chain of fibrinogen. Does not affect the Bbeta-chain and the gamma chain (By similarity).By similarity1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi64 – 641Calcium; via carbonyl oxygen
Metal bindingi66 – 661Calcium
Metal bindingi70 – 701Calcium
Metal bindingi151 – 1511Calcium

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Blood coagulation cascade inhibiting toxin, Hemostasis impairing toxin, Platelet aggregation inhibiting toxin, Toxin

Keywords - Ligandi

Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Snaclec anticoagulant protein subunit A
Short name:
AaACP-A
OrganismiDeinagkistrodon acutus (Hundred-pace snake) (Agkistrodon acutus)
Taxonomic identifieri36307 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaViperidaeCrotalinaeDeinagkistrodon

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323By similarityAdd
BLAST
Chaini24 – 152129Snaclec anticoagulant protein subunit APRO_5000049504Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi25 ↔ 36PROSITE-ProRule annotation1 Publication
Disulfide bondi53 ↔ 150PROSITE-ProRule annotation1 Publication
Disulfide bondi102 – 102Interchain (with C-98 in subunit B)PROSITE-ProRule annotation1 Publication
Disulfide bondi125 ↔ 142PROSITE-ProRule annotation1 Publication

Keywords - PTMi

Disulfide bond

Expressioni

Tissue specificityi

Expressed by the venom gland.

Interactioni

Subunit structurei

Heterodimer of subunits A and B; disulfide-linked.1 Publication

Structurei

Secondary structure

1
152
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi30 – 323Combined sources
Beta strandi35 – 4410Combined sources
Helixi46 – 5611Combined sources
Helixi68 – 8114Combined sources
Beta strandi85 – 873Combined sources
Beta strandi89 – 957Combined sources
Helixi119 – 1213Combined sources
Beta strandi125 – 1284Combined sources
Helixi130 – 1323Combined sources
Beta strandi136 – 1405Combined sources
Beta strandi146 – 1527Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Y17X-ray2.40A24-152[»]
ProteinModelPortaliQ9DEF9.
SMRiQ9DEF9. Positions 24-152.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9DEF9.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini24 – 152129C-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.

Q9DEF9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGRFIFVSFG LLVVYLSLSG TAADCSSSWS SYEGHCYKAF KQSKTWADAE
60 70 80 90 100
SFCTKQVNGG HLVSIESSGE ADFVAHLIAQ KIKSAKIHVW IGLRAQNKEK
110 120 130 140 150
QCSIEWSDGS SISYENWIEE ESKKCLGVHK ATGFRKWENF YCEQRDPFVC

EA
Length:152
Mass (Da):17,124
Last modified:March 1, 2001 - v1
Checksum:i5C59C0F503A4D223
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB036880 mRNA. Translation: BAA99281.1.
PIRiJC7134.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB036880 mRNA. Translation: BAA99281.1.
PIRiJC7134.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Y17X-ray2.40A24-152[»]
ProteinModelPortaliQ9DEF9.
SMRiQ9DEF9. Positions 24-152.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG004151.

Miscellaneous databases

EvolutionaryTraceiQ9DEF9.

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...

Publicationsi

  1. "Characterization, primary structure and molecular evolution of anticoagulant protein from Agkistrodon actus venom."
    Tani A., Ogawa T., Nose T., Nikandrov N.N., Deshimaru M., Chijiwa T., Chang C.C., Fukumaki Y., Ohno M.
    Toxicon 40:803-813(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
    Tissue: Venom and Venom gland.
  2. "Characterizations and crystal structures of two snake venom proteins with the activity of binding coagulation factor X from Agkistrodon acutus."
    Zhu Z., Liu S., Mo X., Yu X., Liang Z., Zang J., Zhao W., Teng M., Niu L.
    Submitted (NOV-2004) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 24-152, METAL-BINDING SITES, DISULFIDE BONDS.
    Tissue: Venom.

Entry informationi

Entry nameiSLAA_DEIAC
AccessioniPrimary (citable) accession number: Q9DEF9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: March 1, 2001
Last modified: December 9, 2015
This is version 69 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

Keywords - Technical termi

3D-structure

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.