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Protein

Acidic phospholipase A2 2

Gene
N/A
Organism
Naja naja (Indian cobra)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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 per subunit.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi27 – 271Calcium; via carbonyl oxygenCombined sources1 Publication
Metal bindingi29 – 291Calcium; via carbonyl oxygenCombined sources1 Publication
Metal bindingi31 – 311Calcium; via carbonyl oxygenCombined sources1 Publication
Active sitei47 – 4711 Publication
Metal bindingi48 – 481CalciumCombined sources1 Publication
Active sitei93 – 9311 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BRENDAi3.1.1.4. 3557.

Chemistry

SwissLipidsiSLP:000000937.

Names & Taxonomyi

Protein namesi
Recommended name:
Acidic phospholipase A2 2 (EC:3.1.1.4)
Short name:
PLA22
Short name:
svPLA2
Alternative name(s):
Phosphatidylcholine 2-acylhydrolase
OrganismiNaja naja (Indian cobra)
Taxonomic identifieri35670 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaElapidaeElapinaeNaja

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL5584.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 119119Acidic phospholipase A2 2PRO_0000161669Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi11 ↔ 71Combined sources3 Publications
Disulfide bondi26 ↔ 118Combined sources3 Publications
Disulfide bondi28 ↔ 44Combined sources3 Publications
Disulfide bondi43 ↔ 99Combined sources3 Publications
Disulfide bondi50 ↔ 92Combined sources3 Publications
Disulfide bondi60 ↔ 85Combined sources3 Publications
Disulfide bondi78 ↔ 90Combined sources3 Publications

Keywords - PTMi

Disulfide bond

Expressioni

Tissue specificityi

Expressed by the venom gland.1 Publication

Interactioni

Subunit structurei

Homotrimer.3 Publications

Chemistry

BindingDBiP15445.

Structurei

Secondary structure

1
119
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi2 – 1211Combined sources
Helixi18 – 214Combined sources
Beta strandi22 – 243Combined sources
Turni25 – 273Combined sources
Beta strandi28 – 303Combined sources
Beta strandi32 – 343Combined sources
Helixi39 – 5416Combined sources
Helixi62 – 643Combined sources
Beta strandi69 – 724Combined sources
Beta strandi75 – 784Combined sources
Helixi84 – 10219Combined sources
Helixi107 – 1093Combined sources
Helixi114 – 1174Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A3DX-ray1.80A1-119[»]
1A3FX-ray2.65A/B/C1-119[»]
1OWSX-ray2.30A1-118[»]
B1-119[»]
1PSHX-ray2.30A/B/C1-119[»]
2WQ5X-ray1.65A1-119[»]
ProteinModelPortaliP15445.
SMRiP15445. Positions 1-119.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP15445.

Family & Domainsi

Sequence similaritiesi

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.

P15445-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
NLYQFKNMIK CTVPSRSWWD FADYGCYCGR GGSGTPVDDL DRCCQVHDNC
60 70 80 90 100
YNEAEKISGC WPYFKTYSYE CSQGTLTCKG DNNACAASVC DCDRLAAICF
110
AGAPYNDNNY NIDLKARCQ
Length:119
Mass (Da):13,346
Last modified:April 1, 1990 - v1
Checksum:iB725291AAB522966
GO

Sequence cautioni

The sequence CAA45372.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X63947 Genomic DNA. Translation: CAA45372.1. Different initiation.
PIRiS07528.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X63947 Genomic DNA. Translation: CAA45372.1. Different initiation.
PIRiS07528.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A3DX-ray1.80A1-119[»]
1A3FX-ray2.65A/B/C1-119[»]
1OWSX-ray2.30A1-118[»]
B1-119[»]
1PSHX-ray2.30A/B/C1-119[»]
2WQ5X-ray1.65A1-119[»]
ProteinModelPortaliP15445.
SMRiP15445. Positions 1-119.
ModBaseiSearch...
MobiDBiSearch...

Chemistry

BindingDBiP15445.
ChEMBLiCHEMBL5584.
SwissLipidsiSLP:000000937.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG008137.

Enzyme and pathway databases

BRENDAi3.1.1.4. 3557.

Miscellaneous databases

EvolutionaryTraceiP15445.

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...

Publicationsi

  1. "Amino acid sequence and circular dichroism of Indian cobra (Naja naja naja) venom acidic phospholipase A2."
    Davidson F.F., Dennis E.A.
    Biochim. Biophys. Acta 1037:7-15(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE, CIRCULAR DICHROISM.
    Tissue: Venom.
  2. "Phospholipase A2 from cobra (Naja naja naja) venom. Primary structure and subspecies variation."
    Shafqat J., Beg O.U., Joernvall H., Zaidi Z.H.
    Protein Seq. Data Anal. 2:451-452(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.
    Tissue: Venom.
  3. "Renaturation of cobra venom phospholipase A2 expressed from a synthetic gene in Escherichia coli."
    Kelley M.J., Crowl R.M., Dennis E.A.
    Biochim. Biophys. Acta 1118:107-115(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "Molecular diversity in venom proteins of the Russell's viper (Daboia russellii russellii) and the Indian cobra (Naja naja) in Sri Lanka."
    Suzuki M., Itoh T., Bandaranayake B.M.A.I.K., Ranasinghe J.G., Athauda S.B., Moriyama A.
    Biomed. Res. 31:71-81(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-20, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Tissue: Venom.
  5. "Crystal structure of phospholipase A2 from Indian cobra reveals a trimeric association."
    Fremont D.H., Anderson D.H., Wilson I.A., Dennis E.A., Xuong N.-H.
    Proc. Natl. Acad. Sci. U.S.A. 90:342-346(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH CALCIUM ION, COFACTOR, DISULFIDE BONDS, SUBUNIT.
    Tissue: Venom.
  6. "Structures of two novel crystal forms of Naja naja naja phospholipase A2 lacking Ca2+ reveal trimeric packing."
    Segelke B.W., Nguyen D., Chee R., Xuong N.H., Dennis E.A.
    J. Mol. Biol. 279:223-232(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), DISULFIDE BONDS, SUBUNIT.
    Tissue: Venom.
  7. "Nonantibiotic properties of tetracyclines: structural basis for inhibition of secretory phospholipase A2."
    Dalm D., Palm G.J., Aleksandrov A., Simonson T., Hinrichs W.
    J. Mol. Biol. 398:83-96(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) IN COMPLEX WITH AN INHIBITOR, DISULFIDE BONDS.

Entry informationi

Entry nameiPA2A2_NAJNA
AccessioniPrimary (citable) accession number: P15445
Secondary accession number(s): Q65ZF5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: May 11, 2016
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Is not neurotoxic.

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.