Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Basic phospholipase A2 1

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 – 541By similarity
Metal bindingi55 – 551CalciumCombined sources1 Publication
Active sitei100 – 1001By similarity

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:
Basic phospholipase A2 1 (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_0000022924
Chaini8 – 126119Basic phospholipase A2 1PRO_0000022925Add
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.

Interactioni

Subunit structurei

Heterodimer formed between two homologous isoforms: isoform 1 and isoform 2.1 Publication

Structurei

Secondary structure

1
126
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi9 – 1911Combined sources
Helixi26 – 294Combined 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
1MH2X-ray2.70A8-126[»]
1MH7X-ray2.00A8-126[»]
1MH8X-ray1.86A8-126[»]
1S6BX-ray1.60A8-126[»]
1XXWX-ray2.70A8-125[»]
2RD4X-ray2.97A8-126[»]
ProteinModelPortaliP60043.
SMRiP60043. Positions 8-126.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP60043.

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.

P60043-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
SNRPMPLNTY QFKNMIQCTV PKRSWWDFAD YGCYCGRGGS GTPIDDLDRC
60 70 80 90 100
CQVHDNCYNS AREQGGCRPK QKTYSYECKA GTLSCSGSNN SCAATVCDCD
110 120
RLAAICFAGA PYNDNNYNID LKARCQ
Length:126
Mass (Da):14,003
Last modified:May 10, 2004 - v2
Checksum:i07D0BFA119F6A8B2
GO

Experimental Info

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY422775 mRNA. Translation: AAR00253.2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY422775 mRNA. Translation: AAR00253.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MH2X-ray2.70A8-126[»]
1MH7X-ray2.00A8-126[»]
1MH8X-ray1.86A8-126[»]
1S6BX-ray1.60A8-126[»]
1XXWX-ray2.70A8-125[»]
2RD4X-ray2.97A8-126[»]
ProteinModelPortaliP60043.
SMRiP60043. Positions 8-126.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG008137.

Miscellaneous databases

EvolutionaryTraceiP60043.

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 from Indian cobra."
    Paramasivam M., Saravanan K., Hariprasad R.G., Jabeen T., Sharma S., Singh T.P., Srinivasan A.
    Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Venom gland.
  2. "Crystal structure of a calcium-induced dimer of two isoforms of cobra phospholipase A2 at 1.6 A resolution."
    Jabeen T., Sharma S., Singh N., Singh R.K., Kaur P., Perbandt M., Betzel C., Srinivasan A., Singh T.P.
    Proteins 59:856-863(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 8-126 IN COMPLEX WITH ISOFORM 2 AND CALCIUM ION, COFACTOR, DISULFIDE BONDS.

Entry informationi

Entry nameiPA2B1_NAJSG
AccessioniPrimary (citable) accession number: P60043
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 21, 2003
Last sequence update: May 10, 2004
Last modified: May 11, 2016
This is version 75 of the entry and version 2 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.