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Reviewed, UniProtKB/Swiss-Prot P00598 (PA21_NAJAT)

Last modified June 16, 2009. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Phospholipase A2 1
    EC=3.1.1.4
Alternative name(s):
    Muscarinic protein
      Short name=MP
    Phosphatidylcholine 2-acylhydrolase
OrganismNaja atra (Chinese cobra)
Taxonomic identifier8656 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataScleroglossaSerpentesColubroideaElapidaeElapinaeNaja

Protein attributes

Sequence length146 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

PA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. In guinea-pig ileum, this protein produces an onset and dose-dependent contraction. Has a high affinity for muscarinic acetylcholine receptors mAChRs and has the ability to activate them. Ref.3

Catalytic activity

Phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate.

Cofactor

Binds 1 calcium ion per subunit.

Subunit structure

Homodimer.

Subcellular location

Secreted.

Tissue specificity

Expressed by the venom gland.

Sequence similarities

Belongs to the phospholipase A2 family. Group I subfamily.

Mass spectrometry

Molecular mass is 13260 Da from positions 28 - 146. Ref.3

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Propeptide22 – 276
PRO_0000022916
Chain28 – 146119Phospholipase A2 1
PRO_0000022917

Sites

Active site741
Active site1201
Metal binding541Calcium; via carbonyl oxygen
Metal binding561Calcium; via carbonyl oxygen
Metal binding581Calcium; via carbonyl oxygen
Metal binding751Calcium

Amino acid modifications

Disulfide bond38 ↔ 98
Disulfide bond53 ↔ 145
Disulfide bond55 ↔ 71
Disulfide bond70 ↔ 126
Disulfide bond77 ↔ 119
Disulfide bond87 ↔ 112
Disulfide bond105 ↔ 117

Experimental info

Sequence conflict111 – 1122AC → CA AA sequence Ref.2
Sequence conflict134 – 1363NNN → DND AA sequence Ref.2
Sequence conflict1401D → N AA sequence Ref.2
Sequence conflict1461Q → QE AA sequence Ref.2

Secondary structure

...................... 146
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00598-1 [UniParc].

Last modified February 1, 1994. Version 2.
Checksum: 862EDF47654BFF93

FASTA14616,013
        10         20         30         40         50         60 
MTPAHLLILA AVCVSPLGAS SNRPMPLNLY QFKNMIQCTV PSRSWWDFAD YGCYCGRGGS 

        70         80         90        100        110        120 
GTPVDDLDRC CQVHDNCYNE AEKISGCWPY FKTYSYECSQ GTLTCKGGNN ACAAAVCDCD 

       130        140 
RLAAICFAGA PYNNNNYNID LKARCQ 

« Hide

References

[1]"Sequence analysis and expression of phospholipase A2 from Taiwan cobra."
Pan F.M., Yeh M.S., Chang W.C., Hung C.C., Chiou S.H.
Biochem. Biophys. Res. Commun. 199:969-976(1994) [PubMed: 7510963] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Venom gland.
[2]"Complete amino acid sequence of a phospholipase A2 from the venom of Naja naja atra (Taiwan cobra)."
Tsai I.-H., Wu S.-H., Lo T.-B.
Toxicon 19:141-152(1981) [PubMed: 7222082] [Abstract]
Cited for: PROTEIN SEQUENCE OF 28-146.
Tissue: Venom.
[3]"A snake venom phospholipase A(2) with high affinity for muscarinic acetylcholine receptors acts on guinea pig ileum."
Huang L.-F., Zheng J.-B., Xu Y., Song H.-T., Yu C.-X.
Toxicon 51:1008-1016(2008) [PubMed: 18281071] [Abstract]
Cited for: PROTEIN SEQUENCE OF 28-43, FUNCTION, MASS SPECTROMETRY.
Tissue: Venom.
[4]"Crystal structure of cobra-venom phospholipase A2 in a complex with a transition-state analogue."
White S.P., Scott D.L., Otwinowski Z., Gelb M.H., Sigler P.B.
Science 250:1560-1563(1990) [PubMed: 2274787] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[5]"Interfacial catalysis: the mechanism of phospholipase A2."
Scott D.L., White S.P., Otwinowski Z., Yuan W., Gelb M.H., Sigler P.B.
Science 250:1541-1546(1990) [PubMed: 2274785] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).

Cross-references

Sequence databases

X73225 mRNA. Translation: CAA51694.1.
PIRPSNJAF. JC2137.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1POAX-ray1.50A28-145[»]
1POBX-ray2.00A/B28-145[»]
ModBaseSearch...

Phylogenomic databases

HOVERGENP00598.

Enzyme and pathway databases

BRENDA3.1.1.4. 279483.

Family and domain databases

InterProIPR016090. Phospholipase_A2.
IPR013090. Phospholipase_A2_AS.
IPR001211. Phospholipase_A2_euk.
[Graphical view]
Gene3DG3DSA:1.20.90.10. Phospholipase_A2. 1 hit.
PANTHERPTHR11716. Phospholipase_A2. 1 hit.
PfamPF00068. Phospholip_A2_1. 1 hit.
[Graphical view]
PRINTSPR00389. PHPHLIPASEA2.
ProDomPD000303. PhospholipaseA2. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00085. PA2c. 1 hit.
[Graphical view]
PROSITEPS00119. PA2_ASP. 1 hit.
PS00118. PA2_HIS. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePA21_NAJAT
AccessionPrimary (citable) accession number: P00598
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: February 1, 1994
Last modified: June 16, 2009
This is version 89 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents