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Protein Page:
PLA2G2D (human)

Overview
PLA2G2D PA2 catalyzes the calcium-dependent hydrolysis of the 2- acyl groups in 3-sn-phosphoglycerides. L-alpha-1-palmitoyl-2- linoleoyl phosphatidylethanolamine is more efficiently hydrolyzed than the other phospholipids examined. Belongs to the phospholipase A2 family. Note: This description may include information from UniProtKB.
Protein type: Lipid Metabolism - alpha-linolenic acid; Secreted, signal peptide; Lipid Metabolism - ether lipid; Lipid Metabolism - linoleic acid; Lipid Metabolism - arachidonic acid; Secreted; Phospholipase; EC 3.1.1.4; Lipid Metabolism - glycerophospholipid
Chromosomal Location of Human Ortholog: 1p36.12
Cellular Component: extracellular region
Molecular Function: calcium ion binding; heparan sulfate proteoglycan binding; heparin binding; phospholipase A2 activity
Biological Process: CD4-positive, CD25-positive, alpha-beta regulatory T cell differentiation; inflammatory response; lipid catabolic process; negative regulation of T cell proliferation; phosphatidic acid biosynthetic process; phospholipid metabolic process
Reference #:  Q9UNK4 (UniProtKB)
Alt. Names/Synonyms: GIID sPLA2; Group IID secretory phospholipase A2; PA2GD; Phosphatidylcholine 2-acylhydrolase 2D; phospholipase A2, group IID; PLA2G2D; PLA2IID; secretory phospholipase A2s; Secretory-type PLA, stroma-associated homolog; sPLA2-IID; sPLA2S; SPLASH
Gene Symbols: PLA2G2D
Molecular weight: 16,546 Da
Basal Isoelectric point: 8.6  Predict pI for various phosphorylation states
Select Structure to View Below

PLA2G2D

Protein Structure Not Found.


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Modification Sites and Domains  

Modification Sites in Parent Protein, Orthologs, and Isoforms  
 

Show Multiple Sequence Alignment


 LTP 

LTP: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 HTP 

HTP: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 1 Y41‑p GKMPILSyWPYGCHC
0 1 Y82‑p KTQGCSIyKDyyRYN
0 1 Y85‑p GCSIyKDyyRYNFSQ
0 1 Y86‑p CSIyKDyyRYNFSQG
0 1 Y126‑p LKRNLDTyQKRLRFY
  mouse

 
Y40 GKKAFFSYWPYGCHC
L81 KIDGCKSLTDNYKYS
N84 GCKSLTDNYKYSISQ
Y85 CKSLTDNYKYSISQG
Y125 LKQNLDSYNKRLRYY
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