UniProtKB - Q6YNQ0 (PA2A3_BUNCA)
Protein
Acidic phospholipase A2 beta-bungarotoxin A3 chain
Gene
N/A
Organism
Bungarus candidus (Malayan krait)
Status
Functioni
Beta bungarotoxin is a presynaptic neurotoxin. The A chain has phospholipase activity. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides (By similarity).By similarity
Catalytic activityi
- a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H+PROSITE-ProRule annotationEC:3.1.1.4PROSITE-ProRule annotation
Cofactori
Ca2+By similarityNote: Binds 1 Ca2+ ion.By similarity
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 45 | Calcium; via carbonyl oxygenBy similarity | 1 | |
Metal bindingi | 47 | Calcium; via carbonyl oxygenBy similarity | 1 | |
Metal bindingi | 49 | Calcium; via carbonyl oxygenBy similarity | 1 | |
Active sitei | 65 | By similarity | 1 | |
Metal bindingi | 66 | CalciumBy similarity | 1 | |
Active sitei | 111 | By similarity | 1 |
GO - Molecular functioni
- calcium ion binding Source: InterPro
- phospholipase A2 activity Source: UniProtKB-EC
- phospholipase A2 activity (consuming 1,2-dipalmitoylphosphatidylcholine) Source: UniProtKB-EC
- phospholipase A2 activity consuming 1,2-dioleoylphosphatidylethanolamine) Source: UniProtKB-EC
- toxin activity Source: UniProtKB-KW
GO - Biological processi
- arachidonic acid secretion Source: InterPro
- lipid catabolic process Source: UniProtKB-KW
- phospholipid metabolic process Source: InterPro
Keywordsi
Molecular function | Hydrolase, Neurotoxin, Presynaptic neurotoxin, Toxin |
Biological process | Lipid degradation, Lipid metabolism |
Ligand | Calcium, Metal-binding |
Names & Taxonomyi
Protein namesi | Recommended name: Acidic phospholipase A2 beta-bungarotoxin A3 chain (EC:3.1.1.4)Short name: Beta-BuTX A3 chain Short name: svPLA2 Alternative name(s): Phosphatidylcholine 2-acylhydrolase |
Organismi | Bungarus candidus (Malayan krait) |
Taxonomic identifieri | 92438 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Bifurcata › Unidentata › Episquamata › Toxicofera › Serpentes › Colubroidea › Elapidae › Bungarinae › Bungarus |
Subcellular locationi
Extracellular region or secreted
- Secreted By similarity
Extracellular region or secreted
- extracellular region Source: UniProtKB-SubCell
Other locations
- other organism presynaptic membrane Source: UniProtKB-KW
Keywords - Cellular componenti
SecretedPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | ‹1 – 9 | Sequence analysis | ›9 | |
PropeptideiPRO_0000271451 | 10 – 17 | By similarity | 8 | |
ChainiPRO_0000271452 | 18 – 137 | Acidic phospholipase A2 beta-bungarotoxin A3 chainAdd BLAST | 120 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Disulfide bondi | 32 | Interchain (with a B chain)By similarity | ||
Disulfide bondi | 44 ↔ 136 | By similarity | ||
Disulfide bondi | 46 ↔ 62 | By similarity | ||
Disulfide bondi | 61 ↔ 117 | By similarity | ||
Disulfide bondi | 68 ↔ 110 | By similarity | ||
Disulfide bondi | 78 ↔ 103 | By similarity | ||
Disulfide bondi | 96 ↔ 108 | By similarity |
Keywords - PTMi
Disulfide bondExpressioni
Tissue specificityi
Expressed by the venom gland.
Interactioni
Subunit structurei
Heterodimer; disulfide-linked. The A chain has phospholipase A2 activity and the B chain shows homology with the basic protease inhibitors (By similarity).By similarity
Structurei
3D structure databases
ProteinModelPortali | Q6YNQ0 |
SMRi | Q6YNQ0 |
ModBasei | Search... |
MobiDBi | Search... |
Family & Domainsi
Sequence similaritiesi
Keywords - Domaini
SignalPhylogenomic databases
HOVERGENi | HBG008137 |
Family and domain databases
CDDi | cd00125 PLA2c, 1 hit |
Gene3Di | 1.20.90.10, 1 hit |
InterProi | View protein in InterPro IPR001211 PLipase_A2 IPR033112 PLipase_A2_Asp_AS IPR016090 PLipase_A2_dom IPR036444 PLipase_A2_dom_sf IPR033113 PLipase_A2_His_AS |
PANTHERi | PTHR11716 PTHR11716, 1 hit |
Pfami | View protein in Pfam PF00068 Phospholip_A2_1, 1 hit |
PRINTSi | PR00389 PHPHLIPASEA2 |
SMARTi | View protein in SMART SM00085 PA2c, 1 hit |
SUPFAMi | SSF48619 SSF48619, 1 hit |
PROSITEi | View protein in PROSITE PS00119 PA2_ASP, 1 hit PS00118 PA2_HIS, 1 hit |
i Sequence
Sequence statusi: Fragment.
: The displayed sequence is further processed into a mature form. Sequence processingi
Q6YNQ0-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
AVCVSLLGAA NIPPHPLNLI NFMEMIRYTI PCEKTWGEYT NYGCYCGAGG
60 70 80 90 100
SGRPIDALDR CCYVHDNCYG DAANIRDCNP KTQSYSYKLT KRTIICYGAA
110 120 130
GTCARVVCDC DRTAALCFGD SEYIEGHKNI DTARFCQ
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Non-terminal residuei | 1 | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AY057882 mRNA Translation: AAL30064.1 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AY057882 mRNA Translation: AAL30064.1 |
3D structure databases
ProteinModelPortali | Q6YNQ0 |
SMRi | Q6YNQ0 |
ModBasei | Search... |
MobiDBi | Search... |
Protocols and materials databases
Structural Biology Knowledgebase | Search... |
Phylogenomic databases
HOVERGENi | HBG008137 |
Family and domain databases
CDDi | cd00125 PLA2c, 1 hit |
Gene3Di | 1.20.90.10, 1 hit |
InterProi | View protein in InterPro IPR001211 PLipase_A2 IPR033112 PLipase_A2_Asp_AS IPR016090 PLipase_A2_dom IPR036444 PLipase_A2_dom_sf IPR033113 PLipase_A2_His_AS |
PANTHERi | PTHR11716 PTHR11716, 1 hit |
Pfami | View protein in Pfam PF00068 Phospholip_A2_1, 1 hit |
PRINTSi | PR00389 PHPHLIPASEA2 |
SMARTi | View protein in SMART SM00085 PA2c, 1 hit |
SUPFAMi | SSF48619 SSF48619, 1 hit |
PROSITEi | View protein in PROSITE PS00119 PA2_ASP, 1 hit PS00118 PA2_HIS, 1 hit |
ProtoNeti | Search... |
Entry informationi
Entry namei | PA2A3_BUNCA | |
Accessioni | Q6YNQ0Primary (citable) accession number: Q6YNQ0 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | January 9, 2007 |
Last sequence update: | July 5, 2004 | |
Last modified: | December 5, 2018 | |
This is version 59 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program | |
Annotation program | Animal Toxin Annotation Program |