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Protein

Acidic phospholipase A2

Gene
N/A
Organism
Ophiophagus hannah (King cobra) (Naja hannah)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.By similarity

Catalytic activityi

Phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate.PROSITE-ProRule annotation

Cofactori

Ca2+By similarityNote: Binds 1 Ca2+ ion.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi55Calcium; via carbonyl oxygenBy similarity1
Metal bindingi57Calcium; via carbonyl oxygenBy similarity1
Metal bindingi59Calcium; via carbonyl oxygenBy similarity1
Active sitei75By similarity1
Metal bindingi76CalciumBy similarity1
Active sitei126By similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHydrolase, Toxin
Biological processLipid degradation, Lipid metabolism
LigandCalcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Acidic phospholipase A2 (EC:3.1.1.4)
Short name:
svPLA2
Alternative name(s):
Phosphatidylcholine 2-acylhydrolase
OrganismiOphiophagus hannah (King cobra) (Naja hannah)
Taxonomic identifieri8665 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaElapidaeElapinaeOphiophagus

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 21Sequence analysisAdd BLAST21
PropeptideiPRO_000002294622 – 27Sequence analysis6
ChainiPRO_000002294728 – 152Acidic phospholipase A2Add BLAST125

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi38 ↔ 104By similarity
Disulfide bondi54 ↔ 151By similarity
Disulfide bondi56 ↔ 72By similarity
Disulfide bondi71 ↔ 132By similarity
Disulfide bondi78 ↔ 125By similarity
Disulfide bondi88 ↔ 118By similarity
Disulfide bondi111 ↔ 123By similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

TopDownProteomicsiQ9DF56.

Expressioni

Tissue specificityi

Expressed by the venom gland.

Structurei

3D structure databases

ProteinModelPortaliQ9DF56.
SMRiQ9DF56.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

HOVERGENiHBG008137.

Family and domain databases

CDDicd00125. PLA2c. 1 hit.
Gene3Di1.20.90.10. 1 hit.
InterProiView protein in InterPro
IPR001211. PLipase_A2.
IPR033112. PLipase_A2_Asp_AS.
IPR016090. PLipase_A2_dom.
IPR036444. PLipase_A2_dom_sf.
IPR033113. PLipase_A2_His_AS.
PANTHERiPTHR11716. PTHR11716. 1 hit.
PfamiView protein in Pfam
PF00068. Phospholip_A2_1. 1 hit.
PRINTSiPR00389. PHPHLIPASEA2.
SMARTiView protein in SMART
SM00085. PA2c. 1 hit.
SUPFAMiSSF48619. SSF48619. 1 hit.
PROSITEiView protein in PROSITE
PS00119. PA2_ASP. 1 hit.
PS00118. PA2_HIS. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9DF56-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNPAHLLVLS AVCVSLLGAS SIPPQPLNLL QFNYMIQCTI PGSRPFLDYM
60 70 80 90 100
DYGCYCGTGV AGHPVDELDR CCQTHDLCYS KAEEQPKCSS LLNSPLMKKY
110 120 130 140 150
SYTCSGGTLT CNDDNDECGA FICNCDRAAR ICFAGAPYNK ENKELDIATR

CQ
Length:152
Mass (Da):16,641
Last modified:March 1, 2001 - v1
Checksum:iFC5663FD02583650
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF297034 mRNA. Translation: AAG17443.1.

Similar proteinsi

Entry informationi

Entry nameiPA2A_OPHHA
AccessioniPrimary (citable) accession number: Q9DF56
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 28, 2002
Last sequence update: March 1, 2001
Last modified: November 22, 2017
This is version 78 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
Annotation programAnimal Toxin Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families