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Reviewed, UniProtKB/Swiss-Prot P24293 (PA21B_ERIMA)

Last modified June 16, 2009. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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 isozyme PLA-1
    EC=3.1.1.4
Alternative name(s):
    Phosphatidylcholine 2-acylhydrolase
OrganismEristocophis macmahoni (Leaf-nosed viper)
Taxonomic identifier8702 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataScleroglossaSerpentesColubroideaViperidaeViperinaeEristocophis

Protein attributes

Sequence length121 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

PA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.

Catalytic activity

Phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate.

Cofactor

Binds 1 calcium ion per subunit By similarity.

Subcellular location

Secreted.

Tissue specificity

Expressed by the venom gland.

Sequence similarities

Belongs to the phospholipase A2 family. Group II subfamily.

Ontologies

Keywords
   Biological processLipid degradation
   Cellular componentSecreted
   LigandCalcium
Metal-binding
   Molecular functionHydrolase
   PTMDisulfide bond
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processlipid catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

phospholipid metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functioncalcium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

phospholipase A2 activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 121121Phospholipase A2 isozyme PLA-1
PRO_0000161645

Sites

Active site471 By similarity
Active site891 By similarity
Metal binding271Calcium; via carbonyl oxygen By similarity
Metal binding291Calcium; via carbonyl oxygen By similarity
Metal binding311Calcium; via carbonyl oxygen By similarity
Metal binding481Calcium By similarity

Amino acid modifications

Disulfide bond26 ↔ 115 By similarity
Disulfide bond28 ↔ 44 By similarity
Disulfide bond43 ↔ 95 By similarity
Disulfide bond49 ↔ 121 By similarity
Disulfide bond50 ↔ 88 By similarity
Disulfide bond57 ↔ 81 By similarity
Disulfide bond75 ↔ 86 By similarity

Sequences

Sequence LengthMass (Da)Tools
P24293-1 [UniParc].

Last modified March 1, 1992. Version 1.
Checksum: F5BAA64676954B5E

FASTA12113,533
        10         20         30         40         50         60 
NLYQFGKMIF KMTGKSALLS YSDYGCYCGW GGKGKPLDAT DRCCFVHDCC YGRVNGCNPK 

        70         80         90        100        110        120 
LSTYSYSFQN GDIVCGDDNA CLRAVCECDR VAAICFGENL NTYDRKYKDY PSSQCTETEQ 


C 

« Hide

References

[1]"Purification and characterization of two highly different group II phospholipase A2 isozymes from a single viperid (Eristocophis macmahoni) venom."
Siddiqi A.R., Zaidi Z.H., Joernvall H.
Eur. J. Biochem. 201:675-679(1991) [PubMed: 1935962] [Abstract]
Cited for: PROTEIN SEQUENCE.
Tissue: Venom.

Cross-references

Sequence databases

PIRS17860.

3D structure databases

HSSPHSSP built from PDB template 1VIP based on UniProtKB P81458.
ModBaseSearch...

Phylogenomic databases

HOVERGENP24293.

Enzyme and pathway databases

BRENDA3.1.1.4. 279510.

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 namePA21B_ERIMA
AccessionPrimary (citable) accession number: P24293
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: March 1, 1992
Last modified: June 16, 2009
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

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