Skip Header

 
Contribute Send feedback
Read comments (1) or add your own

Reviewed, UniProtKB/Swiss-Prot P06596 (PA21B_CANFA)

Last modified June 16, 2009. Version 79. 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
    EC=3.1.1.4
Alternative name(s):
    Phosphatidylcholine 2-acylhydrolase
    Group IB phospholipase A2
Gene names
Name: PLA2G1B
OrganismCanis familiaris (Dog)
Taxonomic identifier9615 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis

Protein attributes

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

Sequence similarities

Belongs to the phospholipase A2 family.

Ontologies

Keywords
   Biological processLipid degradation
   Cellular componentSecreted
   DomainSignal
   LigandCalcium
Metal-binding
   Molecular functionHydrolase
   PTMDisulfide bond
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 – 1515
Propeptide16 – 227
PRO_0000022733
Chain23 – 146124Phospholipase A2
PRO_0000022734

Sites

Active site701 By similarity
Active site1211 By similarity
Metal binding501Calcium; via carbonyl oxygen By similarity
Metal binding521Calcium; via carbonyl oxygen By similarity
Metal binding541Calcium; via carbonyl oxygen By similarity
Metal binding711Calcium By similarity

Amino acid modifications

Disulfide bond33 ↔ 99 By similarity
Disulfide bond49 ↔ 146 By similarity
Disulfide bond51 ↔ 67 By similarity
Disulfide bond66 ↔ 127 By similarity
Disulfide bond73 ↔ 120 By similarity
Disulfide bond83 ↔ 113 By similarity
Disulfide bond106 ↔ 118 By similarity

Sequences

Sequence LengthMass (Da)Tools
P06596-1 [UniParc].

Last modified January 1, 1988. Version 1.
Checksum: F6258ED9527F3692

FASTA14616,236
        10         20         30         40         50         60 
MKFLVLAALL TVAAAEGGIS PRAVWQFRNM IKCTIPESDP LKDYNDYGCY CGLGGSGTPV 

        70         80         90        100        110        120 
DELDKCCQTH DHCYSEAKKL DSCKFLLDNP YTKIYSYSCS GSEITCSSKN KDCQAFICNC 

       130        140 
DRSAAICFSK APYNKEHKNL DTKKYC 

« Hide

References

[1]"Dog and rat pancreatic phospholipases A2: complete amino acid sequences deduced from complementary DNAs."
Ohara O., Tamaki M., Nakamura E., Tsuruta Y., Fujii Y., Shin M., Teraoka H., Okamoto M.
J. Biochem. 99:733-739(1986) [PubMed: 3754861] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Isolation and sequence of the canine pancreatic phospholipase A2 gene."
Kerfelec B., Laforge K.S., Vasiloudes P., Puigserver A., Scheele G.A.
Eur. J. Biochem. 190:299-304(1990) [PubMed: 2142076] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Primary structures of canine pancreatic lipase and phospholipase A2 messenger RNAs."
Kerfelec B., Laforge K.S., Puigserver A., Scheele G.A.
Pancreas 1:430-437(1986) [PubMed: 3562437] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

D00035 mRNA. Translation: BAA00023.1.
M35301 mRNA. Translation: AAA30883.1.
PIRPSDG. S11316.
RefSeqNP_001003320.1.
UniGeneCfa.40293

3D structure databases

HSSPHSSP built from PDB template 1HN4 based on UniProtKB P00592.
ModBaseSearch...

Genome annotation databases

EnsemblENSCAFG00000010263. Canis familiaris. [Contig view]
GeneID404011.
KEGGcfa:404011.

Phylogenomic databases

HOVERGENP06596.
OMAP06596. AKKLDSC.

Enzyme and pathway databases

BRENDA3.1.1.4. 463.

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_CANFA
AccessionPrimary (citable) accession number: P06596
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 1, 1988
Last modified: June 16, 2009
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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