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521  structures 389  species 0  interactions 2413  sequences 30  architectures

Family: Phospholip_A2_1 (PF00068)

Summary: Phospholipase A2

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This is the Wikipedia entry entitled "Phospholipase A2". More...

Phospholipase A2 Edit Wikipedia article

phospholipase A2
Phospholipase Cleavage Sites. Note that an enzyme that displays both PLA1 and PLA2 activities is called a Phospholipase B
EC number3.1.1.4
CAS number9001-84-7
IntEnzIntEnz view
ExPASyNiceZyme view
MetaCycmetabolic pathway
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Phospholipase A2
Bee venom phospholipase A2 sPLA2. Middle plane of the lipid bilayer - black dots. Boundary of the hydrocarbon core region - red dots (extracellular side). Layer of lipid phosphates - yellow dots.
OPM superfamily82
OPM protein1g4i

Phospholipases A2 (PLA2s) EC are enzymes that cleave fatty acid in position two of phospholipids, hydrolyzing the bond between the second fatty acid “tail” and the glycerol molecule. This particular phospholipase specifically recognizes the sn-2 acyl bond of phospholipids and catalytically hydrolyzes the bond, releasing arachidonic acid and lysophosphatidic acid. Upon downstream modification by cyclooxygenases or lipoxygenases, arachidonic acid is modified into active compounds called eicosanoids. Eicosanoids include prostaglandins and leukotrienes, which are categorized as anti-inflammatory and inflammatory mediators.[1]

PLA2 enzymes are commonly found in mammalian tissues as well as arachnid, insect, and snake venom.[2] Venom from both snakes and insects is largely composed of melittin, which is a stimulant of PLA2. Due to the increased presence and activity of PLA2 resulting from a snake or insect bite, arachidonic acid is released from the phospholipid membrane disproportionately. As a result, inflammation and pain occur at the site.[3] There are also prokaryotic A2 phospholipases.

Additional types of phospholipases include phospholipase A1, phospholipase B, phospholipase C, and phospholipase D.[4]


Phospholipases A2 include several unrelated protein families with common enzymatic activity. Two most notable families are secreted and cytosolic phospholipases A2. Other families include Ca2+ independent PLA2 (iPLA2) and lipoprotein-associated PLA2s (lp-PLA2), also known as platelet activating factor acetylhydrolase (PAF-AH).

Secreted phospholipases A2 (sPLA2)

The extracellular forms of phospholipases A2 have been isolated from different venoms (snake, bee, and wasp), from virtually every studied mammalian tissue (including pancreas and kidney) as well as from bacteria. They require Ca2+ for activity.

Pancreatic sPLA2 serve for the initial digestion of phospholipid compounds in dietary fat. Venom phospholipases help to immobilize prey by promoting cell lysis.

In mice, group III sPLA2 are involved in sperm maturation,[5] and group X are thought to be involved in sperm capacitation.[6]

sPLA2 has been shown to promote inflammation in mammals by catalyzing the first step of the arachidonic acid pathway by breaking down phospholipids, resulting in the formation of fatty acids including arachidonic acid. This arachidonic acid is then metabolized to form several inflammatory and thrombogenic molecules. Excess levels of sPLA2 is thought to contribute to several inflammatory diseases, and has been shown to promote vascular inflammation correlating with coronary events in coronary artery disease and acute coronary syndrome,[7] and possibly leading to acute respiratory distress syndrome[8] and progression of tonsillitis.[9]

In children, excess levels of sPLA2 have been associated with inflammation thought to exacerbate asthma[10] and ocular surface inflammation (dry eye).[11]

Increased sPLA2 activity is observed in the cerebrospinal fluid of humans with Alzheimer's disease and multiple sclerosis, and may serve as a marker of increases in permeability of the blood-cerebrospinal fluid barrier.[12]

There are atypical members of the phospholipase A2 family, such as PLA2G12B, that have no phospholipase activity with typical phospholipase substrate.[13] The lack of enzymatic activity of PLA2G12B indicates that it may have unique function distinctive from other sPLA2s. It has been shown that in PLA2G12B null mice VLDL levels were greatly reduced, suggesting it could have an effect in lipoprotein secretion[14][15]

Cytosolic phospholipases A2 (cPLA2)

The intracellular, group IV PLA2 are also Ca-dependent, but they have a different 3D structure and are significantly larger than secreted PLA2 (more than 700 residues). They include a C2 domain and a large catalytic domain.

These phospholipases are involved in cell signaling processes, such as inflammatory response. They release arachidonic acid from membrane phospholipids. Arachidonic acid is both a signaling molecule and the precursor for the synthesis of other signaling molecules termed eicosanoids. These include leukotrienes and prostaglandins. Some eicosanoids are synthesized from diacylglycerol, released from the lipid bilayer by phospholipase C (see below).

Phospholipases A2 can be classified based on sequence homology.[16]

Lipoprotein-associated PLA2s (lp-PLA2)

Increased levels of lp-PLA2 are associated with cardiac disease, and may contribute to atherosclerosis.[17] Although, the role of LP-PLA2 in atherosclerosis may depend on its carrier in plasma, and several lines of evidence suggest that HDL-associated Lp-PLA2 may substantially contribute to the HDL antiatherogenic activities.[18]


The suggested catalytic mechanism of pancreatic sPLA2 is initiated by a His-48/Asp-99/calcium complex within the active site. The calcium ion polarizes the sn-2 carbonyl oxygen while also coordinating with a catalytic water molecule, w5. His-48 improves the nucleophilicity of the catalytic water via a bridging second water molecule, w6. It has been suggested that two water molecules are necessary to traverse the distance between the catalytic histidine and the ester. The basicity of His-48 is thought to be enhanced through hydrogen bonding with Asp-99. An asparagine substitution for His-48 maintains wild-type activity, as the amide functional group on asparagine can also function to lower the pKa, or acid dissociation constant, of the bridging water molecule. The rate limiting state is characterized as the degradation of the tetrahedral intermediate composed of a calcium coordinated oxyanion. The role of calcium can also be duplicated by other relatively small cations like cobalt and nickel.[19] Before becoming active in digestion, the proform of PLA2 is activated by Trypsin.

Close-up rendering of PLA2 active site with phosphate enzyme inhibitor. Calcium ion (pink) coordinates with phosphate (light blue). Phosphate mimics tetrahedral intermediate blocking substrate access to active site. His-48, Asp-99, and 2 water molecules are also shown.[20]
Mechanism of hydrolysis catalyzed by PLA2

PLA2 can also be characterized as having a channel featuring a hydrophobic wall in which hydrophobic amino acid residues such as Phe, Leu, and Tyr serve to bind the substrate. Another component of PLA2 is the seven disulfide bridges that are influential in regulation and stable protein folding.[19]

Biological Effects

PLA2 action can release histamine from rat peritoneal mast cells. [21] It also causes histamine release in human basophils. [22]


Due to the importance of PLA2 in inflammatory responses, regulation of the enzyme is essential. PLA2 is regulated by phosphorylation and calcium concentrations. PLA2 is phosphorylated by a MAPK at Serine-505. When phosphorylation is coupled with an influx of calcium ions, PLA2 becomes stimulated and can translocate to the membrane to begin catalysis.[23]

Phosphorylation of PLA2 may be a result of ligand binding to receptors, including:

In the case of an inflammation, the application of glucocorticoids up-regulate (mediated at the gene level) the production of the protein lipocortin which will inhibit PLA2 and reduce the inflammatory response.

Relevance in neurological disorders

In normal brain cells, PLA2 regulation accounts for a balance between arachidonic acid's conversion into proinflammatory mediators and its reincorporation into the membrane. In the absence of strict regulation of PLA2 activity, a disproportionate amount of proinflammatory mediators are produced. The resulting induced oxidative stress and neuroinflammation is analogous to neurological diseases such as Alzheimer's disease, epilepsy, multiple sclerosis, ischemia. Lysophospholipids are another class of molecules released from the membrane that are upstream predecessors of platelet activating factors (PAF). Abnormal levels of potent PAF are also associated with neurological damage. An optimal enzyme inhibitor would specifically target PLA2 activity on neural cell membranes already under oxidative stress and potent inflammation. Thus, specific inhibitors of brain PLA2 could be a pharmaceutical approach to treatment of several disorders associated with neural trauma.[25]

Increase in phospholipase A2 activity is an acute-phase reaction that rises during inflammation, which is also seen to be exponentially higher in low back disc herniations compared to rheumatoid arthritis.[citation needed] It is a mixture of inflammation and substance P that are responsible for pain.[citation needed]

Increased phospholipase A2 has also been associated with neuropsychiatric disorders such as schizophrenia and pervasive developmental disorders (such as autism), though the mechanisms involved are not known.[26]


Human phospholipase A2 isozymes include:

In addition, the following human proteins contain the phospholipase A2 domain:

See also


  1. ^ Dennis EA (May 1994). "Diversity of group types, regulation, and function of phospholipase A2". The Journal of Biological Chemistry. 269 (18): 13057–60. PMID 8175726.
  2. ^ Nicolas JP, Lin Y, Lambeau G, Ghomashchi F, Lazdunski M, Gelb MH (Mar 1997). "Localization of structural elements of bee venom phospholipase A2 involved in N-type receptor binding and neurotoxicity". The Journal of Biological Chemistry. 272 (11): 7173–81. doi:10.1074/jbc.272.11.7173. PMID 9054413.
  3. ^ Argiolas A, Pisano JJ (Nov 1983). "Facilitation of phospholipase A2 activity by mastoparans, a new class of mast cell degranulating peptides from wasp venom". The Journal of Biological Chemistry. 258 (22): 13697–702. PMID 6643447.
  4. ^ Cox, Michael; Nelson, David R.; Lehninger, Albert L (2005). Lehninger principles of biochemistry (4th ed.). San Francisco: W.H. Freeman. ISBN 0-7167-4339-6.
  5. ^ Sato H, Taketomi Y, Isogai Y, Miki Y, Yamamoto K, Masuda S, Hosono T, Arata S, Ishikawa Y, Ishii T, Kobayashi T, Nakanishi H, Ikeda K, Taguchi R, Hara S, Kudo I, Murakami M (May 2010). "Group III secreted phospholipase A2 regulates epididymal sperm maturation and fertility in mice". The Journal of Clinical Investigation. 120 (5): 1400–14. doi:10.1172/JCI40493. PMC 2860917. PMID 20424323.
  6. ^ Escoffier J, Jemel I, Tanemoto A, Taketomi Y, Payre C, Coatrieux C, Sato H, Yamamoto K, Masuda S, Pernet-Gallay K, Pierre V, Hara S, Murakami M, De Waard M, Lambeau G, Arnoult C (May 2010). "Group X phospholipase A2 is released during sperm acrosome reaction and controls fertility outcome in mice". The Journal of Clinical Investigation. 120 (5): 1415–28. doi:10.1172/JCI40494. PMC 2860919. PMID 20424324.
  7. ^ Mallat Z, Lambeau G, Tedgui A (Nov 2010). "Lipoprotein-associated and secreted phospholipases Aâ‚‚ in cardiovascular disease: roles as biological effectors and biomarkers". Circulation. 122 (21): 2183–200. doi:10.1161/CIRCULATIONAHA.110.936393. PMID 21098459.
  8. ^ De Luca D, Minucci A, Cogo P, Capoluongo ED, Conti G, Pietrini D, Carnielli VP, Piastra M (Jan 2011). "Secretory phospholipase Aâ‚‚ pathway during pediatric acute respiratory distress syndrome: a preliminary study". Pediatric Critical Care Medicine. 12 (1): e20–4. doi:10.1097/PCC.0b013e3181dbe95e. PMID 20351613.
  9. ^ Ezzeddini R, Darabi M, Ghasemi B, Jabbari Moghaddam Y, Jabbari Y, Abdollahi S, Rashtchizadeh N, Gharahdaghi A, Darabi M, Ansarin M, Shaaker M, Samadi A, Karamravan J (Apr 2012). "Circulating phospholipase-A2 activity in obstructive sleep apnea and recurrent tonsillitis". International Journal of Pediatric Otorhinolaryngology. 76 (4): 471–4. doi:10.1016/j.ijporl.2011.12.026. PMID 22297210.
  10. ^ Henderson WR, Oslund RC, Bollinger JG, Ye X, Tien YT, Xue J, Gelb MH (Aug 2011). "Blockade of human group X secreted phospholipase A2 (GX-sPLA2)-induced airway inflammation and hyperresponsiveness in a mouse asthma model by a selective GX-sPLA2 inhibitor". The Journal of Biological Chemistry. 286 (32): 28049–55. doi:10.1074/jbc.M111.235812. PMC 3151050. PMID 21652694.
  11. ^ Wei Y, Epstein SP, Fukuoka S, Birmingham NP, Li XM, Asbell PA (Jun 2011). "sPLA2-IIa amplifies ocular surface inflammation in the experimental dry eye (DE) BALB/c mouse model". Investigative Ophthalmology & Visual Science. 52 (7): 4780–8. doi:10.1167/iovs.10-6350. PMC 3175946. PMID 21519031.
  12. ^ Chalbot S; Zetterberg H; Blennow K; Fladby T; Andreasen N; Grundke-Iqbal I; Iqbal K (January 2011). "Blood-cerebrospinal fluid barrier permeability in Alzheimer's disease". Journal of Alzheimer's Disease. 25 (3): 505–15. doi:10.3233/JAD-2011-101959. PMC 3139450. PMID 21471645.
  13. ^ Aleksandra Aljakna; Seungbum Choi; Holly Savage; Rachael Hageman Blair; Tongjun Gu; Karen L. Svenson; Gary A. Churchill; Matt Hibbs; Ron Korstanje (August 2012). "Pla2g12b and Hpn Are Genes Identified by Mouse ENU Mutagenesis That Affect HDL Cholesterol". PLOS ONE. 7 (8): e43139. doi:10.1371/journal.pone.0043139. PMC 3422231. PMID 22912808.
  14. ^ Guan M, Qu L, Tan W, Chen L, Wong CW (Feb 2011). "Hepatocyte Nuclear Factor-4 Alpha Regulates Liver Triglyceride Metabolism in Part Through Secreted Phospholipase A2 GXIIB". Hepatology. 53 (2): 458–466. doi:10.1002/hep.24066. PMID 21274867.
  15. ^ Li X, Jiang H, Qu L, Yao W, Cai H, Chen L, Peng T (Jan 2014). "Hepatocyte nuclear factor 4α and downstream secreted phospholipase A2 GXIIB regulate production of infectious hepatitis C virus". J Virol. 88 (1): 612–627. doi:10.1128/JVI.02068-13. PMC 3911757. PMID 24173221.
  16. ^ Six DA, Dennis EA (Oct 2000). "The expanding superfamily of phospholipase A(2) enzymes: classification and characterization". Biochimica et Biophysica Acta. 1488 (1–2): 1–19. doi:10.1016/S1388-1981(00)00105-0. PMID 11080672.
  17. ^ Wilensky RL, Shi Y, Mohler ER, Hamamdzic D, Burgert ME, Li J, Postle A, Fenning RS, Bollinger JG, Hoffman BE, Pelchovitz DJ, Yang J, Mirabile RC, Webb CL, Zhang L, Zhang P, Gelb MH, Walker MC, Zalewski A, Macphee CH (Oct 2008). "Inhibition of lipoprotein-associated phospholipase A2 reduces complex coronary atherosclerotic plaque development". Nature Medicine. 14 (10): 1059–66. doi:10.1038/nm.1870. PMC 2885134. PMID 18806801.
  18. ^ The role of lipoprotein-associated phospholipase A2 in atherosclerosis may depend on its lipoprotein carrier in plasma. Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids Volume 1791, Issue 5, May 2009, Pages 327-338 PMID 19272461 DOI: 10.1016/j.bbalip.2009.02.015
  19. ^ a b Berg OG, Gelb MH, Tsai MD, Jain MK (Sep 2001). "Interfacial enzymology: the secreted phospholipase A(2)-paradigm". Chemical Reviews. 101 (9): 2613–54. doi:10.1021/cr990139w. PMID 11749391. See page 2640
  20. ^ PDB: 1FXF​; Pan YH, Epstein TM, Jain MK, Bahnson BJ (January 2001). "Five coplanar anion binding sites on one face of phospholipase A2: relationship to interface binding". Biochemistry. 40 (3): 609–17. doi:10.1021/bi002514g. PMID 11170377.
  21. ^ Choi SH1, Sakamoto T, Fukutomi O, Inagaki N, Matsuura N, Nagai H, Koda A. "Pharmacological study of phospholipase A2-induced histamine release from rat peritoneal mast cells". J Pharmacobiodyn. 1989 Sep;12(9):517-22.
  22. ^ Morita Y, Aida N, Miyamoto T. "Role of phospholipase A2 activation in histamine release from human basophils". Allergy. 1983 Aug;38(6):413-8.
  23. ^ Leslie CC (Jul 1997). "Properties and regulation of cytosolic phospholipase A2". The Journal of Biological Chemistry. 272 (27): 16709–12. doi:10.1074/jbc.272.27.16709. PMID 9201969.
  24. ^ a b c d e Walter F. Boron (2003). Medical Physiology: A Cellular And Molecular Approaoch. Elsevier/Saunders. p. 103. ISBN 1-4160-2328-3.
  25. ^ Farooqui AA, Ong WY, Horrocks LA (Sep 2006). "Inhibitors of brain phospholipase A2 activity: their neuropharmacological effects and therapeutic importance for the treatment of neurologic disorders". Pharmacological Reviews. 58 (3): 591–620. doi:10.1124/pr.58.3.7. PMID 16968951.
  26. ^ Bell JG, MacKinlay EE, Dick JR, MacDonald DJ, Boyle RM, Glen AC (Oct 2004). "Essential fatty acids and phospholipase A2 in autistic spectrum disorders". Prostaglandins, Leukotrienes, and Essential Fatty Acids. 71 (4): 201–4. doi:10.1016/j.plefa.2004.03.008. PMID 15301788.

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This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

Phospholipase A2 Provide feedback

Phospholipase A2 releases fatty acids from the second carbon group of glycerol. Perhaps the best known members are secreted snake venoms, but also found in secreted pancreatic and membrane-associated forms. Structure is all-alpha, with two core disulfide-linked helices and a calcium-binding loop. This alignment represents the major family of PLA2s. A second minor family, defined by the honeybee venom PLA2 PDB:1POC and related sequences from Gila monsters (Heloderma), is not recognised. This minor family conserves the core helix pair but is substantially different elsewhere. The PROSITE pattern PA2_HIS, specific to the first core helix, recognises both families.

Internal database links

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR016090

Proteins containing this domain include eukaryotic phospholipase A2 enzymes (PLA2; EC ), small lipolytic enzymes that releases fatty acids from the second carbon group of glycerol, usually in a metal-dependent reaction, to generate lysophospholipid (LysoPL) and a free fatty acid (FA) [ PUBMED:11872155 ]. The resulting products are either dietary or used in synthetic pathways for leukotrienes and prostaglandins. Often, arachidonic acid is released as a free fatty acid and acts as second messenger in signaling networks [ PUBMED:10331081 ]. These enzymes enable the of fatty acids and lysophospholipid by hydrolysing the 2-ester bond of 1,2-diacyl-3-sn-phosphoglycerides. In eukaryotes, PLA2 plays a pivotal role in the biosynthesis of prostaglandin and other mediators of inflammation. These enzymes are either secreted or cytosolic; the latter are either Ca dependent or Ca independent. Secreted PLA2s have also been found to specifically bind to a variety of soluble and membrane proteins in mammals, including receptors [ PUBMED:11293116 ]. As a toxin, PLA2 is a potent presynaptic neurotoxin which blocks nerve terminals by binding to the nerve membrane and hydrolyzing stable membrane lipids [ PUBMED:11212293 ]. The products of the hydrolysis (LysoPL and FA) cannot form bilayers leading to a change in membrane conformation and ultimately to a block in the release of neurotransmitters [ PUBMED:16805767 , PUBMED:10838563 , PUBMED:16339444 ].

The phospholipase domain adopts an alpha-helical secondary structure, consisting of five alpha-helices and two helical segments. PLA2 may form dimers or oligomers [ PUBMED:11080675 , PUBMED:11897785 , PUBMED:12161451 ].

Gene Ontology

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Domain organisation

Below is a listing of the unique domain organisations or architectures in which this domain is found. More...

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Pfam Clan

This family is a member of clan PLA2 (CL0629), which has the following description:

The clan contains the following 5 members:

Phospholip_A2_1 Phospholip_A2_2 Phospholip_A2_3 Phospholip_A2_4 PLA2G12


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Curation and family details

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Curation View help on the curation process

Seed source: Overington and HMM_iterative_training
Previous IDs: phoslip;
Type: Domain
Sequence Ontology: SO:0000417
Author: Eddy SR
Number in seed: 117
Number in full: 2413
Average length of the domain: 104.90 aa
Average identity of full alignment: 35 %
Average coverage of the sequence by the domain: 57.93 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 57096847 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 32.1 32.1
Trusted cut-off 32.2 32.1
Noise cut-off 32.0 32.0
Model length: 109
Family (HMM) version: 21
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Species distribution

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Archea Archea Eukaryota Eukaryota
Bacteria Bacteria Other sequences Other sequences
Viruses Viruses Unclassified Unclassified
Viroids Viroids Unclassified sequence Unclassified sequence


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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Phospholip_A2_1 domain has been found. There are 521 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein sequence.

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AlphaFold Structure Predictions

The list of proteins below match this family and have AlphaFold predicted structures. Click on the protein accession to view the predicted structure.

Protein Predicted structure External Information
A9C458 View 3D Structure Click here
D3Z9Z1 View 3D Structure Click here
D3Z9Z1 View 3D Structure Click here
D3ZLB5 View 3D Structure Click here
D4AAK4 View 3D Structure Click here
F1QH90 View 3D Structure Click here
F1QH90 View 3D Structure Click here
O15496 View 3D Structure Click here
O16654 View 3D Structure Click here
P04054 View 3D Structure Click here
P04055 View 3D Structure Click here
P14423 View 3D Structure Click here
P14555 View 3D Structure Click here
P31482 View 3D Structure Click here
P39877 View 3D Structure Click here
P39878 View 3D Structure Click here
P48076 View 3D Structure Click here
P51433 View 3D Structure Click here
P97391 View 3D Structure Click here
Q02509 View 3D Structure Click here
Q02509 View 3D Structure Click here
Q17790 View 3D Structure Click here
Q3V5J7 View 3D Structure Click here
Q5BK35 View 3D Structure Click here
Q5R387 View 3D Structure Click here
Q6DHQ7 View 3D Structure Click here
Q8IML0 View 3D Structure Click here
Q9BZM2 View 3D Structure Click here
Q9NZK7 View 3D Structure Click here
Q9QUL3 View 3D Structure Click here
Q9QXX3 View 3D Structure Click here
Q9QZT3 View 3D Structure Click here
Q9QZT4 View 3D Structure Click here
Q9UNK4 View 3D Structure Click here
Q9WVF6 View 3D Structure Click here
Q9Z0L3 View 3D Structure Click here
Q9Z0L3 View 3D Structure Click here
Q9Z0Y2 View 3D Structure Click here