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Protein

Basic phospholipase A2 KPA2

Gene
N/A
Organism
Bungarus caeruleus (Indian krait)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Snake venom phospholipase A2 (PLA2) that shows anticoagulant and neurotoxic activities. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.

Catalytic activityi

Phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate.PROSITE-ProRule annotation

Cofactori

Ca2+1 PublicationNote: Binds 1 Ca2+ ion.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi53 – 531Calcium; via carbonyl oxygenCombined sources1 Publication
Metal bindingi55 – 551Calcium; via carbonyl oxygenCombined sources1 Publication
Metal bindingi57 – 571Calcium; via carbonyl oxygenCombined sources1 Publication
Active sitei73 – 7311 Publication
Metal bindingi74 – 741CalciumCombined sources1 Publication
Active sitei119 – 11911 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Blood coagulation cascade inhibiting toxin, Hemostasis impairing toxin, Hydrolase, Neurotoxin, Presynaptic neurotoxin, Toxin

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Keywords - Ligandi

Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Basic phospholipase A2 KPA2 (EC:3.1.1.4)
Short name:
svPLA2
Alternative name(s):
Phosphatidylcholine 2-acylhydrolase
OrganismiBungarus caeruleus (Indian krait)
Taxonomic identifieri132961 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaElapidaeBungarinaeBungarus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Sequence analysisAdd
BLAST
Propeptidei20 – 278By similarityPRO_0000022827
Chaini28 – 145118Basic phospholipase A2 KPA2PRO_0000022828Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi38 ↔ 97Combined sources1 Publication
Disulfide bondi52 ↔ 144Combined sources1 Publication
Disulfide bondi54 ↔ 70Combined sources1 Publication
Disulfide bondi69 ↔ 125Combined sources1 Publication
Disulfide bondi76 ↔ 118Combined sources1 Publication
Disulfide bondi86 ↔ 111Combined sources1 Publication
Disulfide bondi104 ↔ 116Combined sources1 Publication

Keywords - PTMi

Disulfide bond

Expressioni

Tissue specificityi

Expressed by the venom gland.

Interactioni

Subunit structurei

Monomer.1 Publication

Structurei

Secondary structure

1
145
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi29 – 3911Combined sources
Helixi44 – 474Combined sources
Turni51 – 533Combined sources
Beta strandi54 – 574Combined sources
Helixi65 – 8016Combined sources
Turni88 – 903Combined sources
Beta strandi95 – 984Combined sources
Beta strandi101 – 1044Combined sources
Helixi110 – 12819Combined sources
Helixi133 – 1353Combined sources
Turni139 – 1424Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DPYX-ray2.45A28-142[»]
1FE5X-ray2.45A28-145[»]
1PO8X-ray2.71A28-145[»]
ProteinModelPortaliQ9DF52.
SMRiQ9DF52. Positions 28-145.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9DF52.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

HOVERGENiHBG008137.

Family and domain databases

Gene3Di1.20.90.10. 1 hit.
InterProiIPR001211. PLipase_A2.
IPR033112. PLipase_A2_Asp_AS.
IPR016090. PLipase_A2_dom.
IPR033113. PLipase_A2_His_AS.
[Graphical view]
PANTHERiPTHR11716. PTHR11716. 1 hit.
PfamiPF00068. Phospholip_A2_1. 1 hit.
[Graphical view]
PRINTSiPR00389. PHPHLIPASEA2.
SMARTiSM00085. PA2c. 1 hit.
[Graphical view]
SUPFAMiSSF48619. SSF48619. 1 hit.
PROSITEiPS00119. PA2_ASP. 1 hit.
PS00118. PA2_HIS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9DF52-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MYPAHLLVLV AVCVSLLGAA NIPPQPLNLI QFKNMIQCAG TRPWTAYVNY
60 70 80 90 100
GCYCGKGGSG TPVDELDRCC YTHDNCYNEA EKIPGCNPNI KTYSYTCTEP
110 120 130 140
NLTCTDTADT CARFLCDCDR TAAICFASAP YNSNNVMISS STNCQ
Length:145
Mass (Da):15,765
Last modified:March 1, 2001 - v1
Checksum:i4CE49BD226AF3317
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF297663 mRNA. Translation: AAG13412.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF297663 mRNA. Translation: AAG13412.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DPYX-ray2.45A28-142[»]
1FE5X-ray2.45A28-145[»]
1PO8X-ray2.71A28-145[»]
ProteinModelPortaliQ9DF52.
SMRiQ9DF52. Positions 28-145.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG008137.

Miscellaneous databases

EvolutionaryTraceiQ9DF52.

Family and domain databases

Gene3Di1.20.90.10. 1 hit.
InterProiIPR001211. PLipase_A2.
IPR033112. PLipase_A2_Asp_AS.
IPR016090. PLipase_A2_dom.
IPR033113. PLipase_A2_His_AS.
[Graphical view]
PANTHERiPTHR11716. PTHR11716. 1 hit.
PfamiPF00068. Phospholip_A2_1. 1 hit.
[Graphical view]
PRINTSiPR00389. PHPHLIPASEA2.
SMARTiSM00085. PA2c. 1 hit.
[Graphical view]
SUPFAMiSSF48619. SSF48619. 1 hit.
PROSITEiPS00119. PA2_ASP. 1 hit.
PS00118. PA2_HIS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPA2B_BUNCE
AccessioniPrimary (citable) accession number: Q9DF52
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 6, 2002
Last sequence update: March 1, 2001
Last modified: May 11, 2016
This is version 90 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.