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Protein

Acidic phospholipase A2 3

Gene
N/A
Organism
Naja sagittifera (Andaman 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.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi34 – 341Calcium; via carbonyl oxygenCombined sources1 Publication
Metal bindingi36 – 361Calcium; via carbonyl oxygenCombined sources1 Publication
Metal bindingi38 – 381Calcium; via carbonyl oxygenCombined sources1 Publication
Active sitei54 – 5411 Publication
Metal bindingi55 – 551CalciumCombined sources1 Publication
Active sitei100 – 10011 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

Names & Taxonomyi

Protein namesi
Recommended name:
Acidic phospholipase A2 3 (EC:3.1.1.4)
Short name:
svPLA2
Alternative name(s):
Phosphatidylcholine 2-acylhydrolase
OrganismiNaja sagittifera (Andaman cobra)
Taxonomic identifieri195058 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaElapidaeElapinaeNaja

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei‹1 – 7›7PRO_0000022928
Chaini8 – 126119Acidic phospholipase A2 3PRO_0000022929Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi18 ↔ 78Combined sources1 Publication
Disulfide bondi33 ↔ 125Combined sources1 Publication
Disulfide bondi35 ↔ 51Combined sources1 Publication
Disulfide bondi50 ↔ 106Combined sources1 Publication
Disulfide bondi57 ↔ 99Combined sources1 Publication
Disulfide bondi67 ↔ 92Combined sources1 Publication
Disulfide bondi85 ↔ 97Combined sources1 Publication

Keywords - PTMi

Disulfide bond

Expressioni

Tissue specificityi

Expressed by the venom gland.

Structurei

Secondary structure

1
126
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi9 – 1911Combined sources
Helixi25 – 284Combined sources
Beta strandi29 – 313Combined sources
Turni32 – 343Combined sources
Beta strandi35 – 373Combined sources
Helixi46 – 6116Combined sources
Turni69 – 713Combined sources
Beta strandi76 – 794Combined sources
Beta strandi82 – 854Combined sources
Helixi91 – 10919Combined sources
Helixi114 – 1163Combined sources
Helixi121 – 1244Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LN8X-ray1.65A8-126[»]
1MF4X-ray1.90A8-126[»]
1OXRX-ray1.93A8-125[»]
1SZ8X-ray1.50A8-126[»]
1T37X-ray2.60A8-125[»]
1TD7X-ray2.50A8-126[»]
1YXLX-ray1.48A8-125[»]
1ZM6X-ray2.60A8-125[»]
3GCIX-ray2.04A8-126[»]
3JQ5X-ray2.03A8-126[»]
3JQLX-ray1.20A8-126[»]
3JTIX-ray1.80A8-126[»]
3NJUX-ray1.40A8-126[»]
3OSHX-ray1.50A8-126[»]
3Q4YX-ray2.30A8-126[»]
ProteinModelPortaliP60045.
SMRiP60045. Positions 8-126.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP60045.

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: Fragment.

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

P60045-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
SNRPMPLNLY QFKNMIQCTV PSRSWQDFAD YGCYCGKGGS GTPVDDLDRC
60 70 80 90 100
CQVHDNCYNE AENISGCRPY FKTYSYECTQ GTLTCKGDNN ACAASVCDCD
110 120
RLAAICFAGA PYNDANYNID LKARCN
Length:126
Mass (Da):13,969
Last modified:November 21, 2003 - v1
Checksum:iDA6CA9CB6A447EF3
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY433936 mRNA. Translation: AAR08048.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY433936 mRNA. Translation: AAR08048.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LN8X-ray1.65A8-126[»]
1MF4X-ray1.90A8-126[»]
1OXRX-ray1.93A8-125[»]
1SZ8X-ray1.50A8-126[»]
1T37X-ray2.60A8-125[»]
1TD7X-ray2.50A8-126[»]
1YXLX-ray1.48A8-125[»]
1ZM6X-ray2.60A8-125[»]
3GCIX-ray2.04A8-126[»]
3JQ5X-ray2.03A8-126[»]
3JQLX-ray1.20A8-126[»]
3JTIX-ray1.80A8-126[»]
3NJUX-ray1.40A8-126[»]
3OSHX-ray1.50A8-126[»]
3Q4YX-ray2.30A8-126[»]
ProteinModelPortaliP60045.
SMRiP60045. Positions 8-126.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG008137.

Miscellaneous databases

EvolutionaryTraceiP60045.

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. "Phospholipase A2 isoform 3 from Indian cobra."
    Paramasivam M., Hariprasad R.G., Saravanan K., Singh R.K., Sharma S., Singh T.P., Srinivasan A.
    Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Venom gland.
  2. "Design of specific peptide inhibitors for group I phospholipase A2: structure of a complex formed between phospholipase A2 from Naja naja sagittifera (group I) and a designed peptide inhibitor Val-Ala-Phe-Arg-Ser (VAFRS) at 1.9 A resolution reveals unique features."
    Singh R.K., Vikram P., Makker J., Jabeen T., Sharma S., Dey S., Kaur P., Srinivasan A., Singh T.P.
    Biochemistry 42:11701-11706(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 8-126 IN COMPLEX WITH A PEPTIDE INHIBITOR.
  3. "Aspirin induces its anti-inflammatory effects through its specific binding to phospholipase A2: crystal structure of the complex formed between phospholipase A2 and aspirin at 1.9 angstroms resolution."
    Singh R.K., Ethayathulla A.S., Jabeen T., Sharma S., Kaur P., Singh T.P.
    J. Drug. Target. 13:113-119(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) OF 8-125 IN COMPLEX WITH CALCIUM ION AND ACETYLSALICYLIC ACID, COFACTOR, DISULFIDE BONDS.

Entry informationi

Entry nameiPA2A3_NAJSG
AccessioniPrimary (citable) accession number: P60045
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 21, 2003
Last sequence update: November 21, 2003
Last modified: May 11, 2016
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
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.