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Reviewed, UniProtKB/Swiss-Prot P00611 (PA21B_LATSE)

Last modified January 19, 2010. Version 78. 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 1
    EC=3.1.1.4
Alternative name(s):
    Phospholipase A2 isozyme I
    Phosphatidylcholine 2-acylhydrolase
    GL5-1
OrganismLaticauda semifasciata (Broad-banded blue sea snake) (Erabu sea snake)
Taxonomic identifier8631 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataScleroglossaSerpentesColubroideaElapidaeLaticaudinaeLaticauda

Protein attributes

Sequence length145 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.

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.

Ontologies

Keywords
   Biological processLipid degradation
   Cellular componentSecreted
   DomainSignal
   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

Signal peptide1 – 2121 Potential
Propeptide22 – 276
PRO_0000022896
Chain28 – 145118Phospholipase A2 isozyme 1
PRO_0000022897

Sites

Active site751 By similarity
Active site1191 By similarity
Metal binding551Calcium; via carbonyl oxygen By similarity
Metal binding571Calcium; via carbonyl oxygen By similarity
Metal binding591Calcium; via carbonyl oxygen By similarity
Metal binding761Calcium By similarity
Site911Specific activity reduced 20-fold by modification

Amino acid modifications

Disulfide bond38 ↔ 98 By similarity
Disulfide bond54 ↔ 144 By similarity
Disulfide bond56 ↔ 72 By similarity
Disulfide bond71 ↔ 125 By similarity
Disulfide bond78 ↔ 118 By similarity
Disulfide bond87 ↔ 111 By similarity
Disulfide bond105 ↔ 116 By similarity

Experimental info

Sequence conflict39 – 402VN → NV AA sequence Ref.2
Sequence conflict771D → N AA sequence Ref.2

Sequences

Sequence LengthMass (Da)Tools
P00611-1 [UniParc].

Last modified November 1, 2002. Version 3.
Checksum: 1F84DF6F7BC5348F

FASTA14515,900
        10         20         30         40         50         60 
MYPAHLLVLL AVCVSLLGAT AIPPLPLNLV QFSNLIQCVN KGSRASYHYA DYGCYCGAGG 

        70         80         90        100        110        120 
SGTPVDELDR CCKIHDDCYG EAEKMGCYPK WTLYTYDCST EEPNCSTKTG CQGFVCACDL 

       130        140 
EAAKCFARSP YNNKNYNIDT SKRCK 

« Hide

References

[1]"A comparative analysis of invaded sequences from group IA phospholipase A(2) genes provides evidence about the divergence period of genes groups and snake families."
Fujimi T.J., Tsuchiya T., Tamiya T.
Toxicon 40:873-884(2002) [PubMed: 12076640] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Liver.
[2]"Amino acid sequences of three phospholipases A I, III and IV from the venom of the sea snake Laticauda semifasciata."
Nishida S., Kim H.S., Tamiya N.
Biochem. J. 207:589-594(1982) [PubMed: 7165712] [Abstract]
Cited for: PROTEIN SEQUENCE OF 28-145.
Tissue: Venom.
[3]"Correction of amino acid sequence of phospholipase A2 I from the venom of Laticauda semifasciata (Erabu sea snake)."
Takasaki C., Kuramochi H., Shimazu T., Tamiya N.
Toxicon 26:747-749(1988) [PubMed: 3188064] [Abstract]
Cited for: SEQUENCE REVISION TO 97-107.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB062440 Genomic DNA. Translation: BAB72247.1.
PIRPSLT1E. A94325.

3D structure databases

SMRP00611. Positions 28-145.
ModBaseSearch...

Phylogenomic databases

HOVERGENP00611.

Enzyme and pathway databases

BRENDA3.1.1.4. 96002.

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.
SMARTSM00085. PA2c. 1 hit.
[Graphical view]
PROSITEPS00119. PA2_ASP. 1 hit.
PS00118. PA2_HIS. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePA21B_LATSE
AccessionPrimary (citable) accession number: P00611
Secondary accession number(s): Q9I848
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: November 1, 2002
Last modified: January 19, 2010
This is version 78 of the entry and version 3 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