Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Acidic phospholipase A2

Gene
N/A
Organism
Gloydius blomhoffii (Mamushi) (Agkistrodon halys blomhoffi)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Cofactori

Ca2+Note: Binds 1 Ca2+ ion.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi27 – 271Calcium; via carbonyl oxygen
Metal bindingi29 – 291Calcium; via carbonyl oxygen
Metal bindingi30 – 301Calcium; via carbonyl oxygen
Active sitei47 – 471
Metal bindingi48 – 481Calcium
Active sitei89 – 891

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. phospholipase A2 activity Source: UniProtKB-EC

GO - Biological processi

  1. lipid catabolic process Source: UniProtKB-KW
  2. phospholipid metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Keywords - Ligandi

Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Acidic phospholipase A2 (EC:3.1.1.4)
Short name:
PA2-II
Short name:
svPLA2
Alternative name(s):
Phosphatidylcholine 2-acylhydrolase
OrganismiGloydius blomhoffii (Mamushi) (Agkistrodon halys blomhoffi)
Taxonomic identifieri242054 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaViperidaeCrotalinaeGloydius

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 122122Acidic phospholipase A2PRO_0000161596Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi26 ↔ 115
Disulfide bondi28 ↔ 44
Disulfide bondi43 ↔ 95
Disulfide bondi49 ↔ 122
Disulfide bondi50 ↔ 88
Disulfide bondi57 ↔ 81
Disulfide bondi75 ↔ 86

Keywords - PTMi

Disulfide bond

Expressioni

Tissue specificityi

Expressed by the venom gland.

Interactioni

Subunit structurei

Monomer.

Structurei

3D structure databases

ProteinModelPortaliP20249.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

HOVERGENiHBG008137.

Family and domain databases

Gene3Di1.20.90.10. 1 hit.
InterProiIPR001211. PLipase_A2.
IPR013090. PLipase_A2_AS.
IPR016090. PLipase_A2_dom.
[Graphical view]
PANTHERiPTHR11716. PTHR11716. 1 hit.
PfamiPF00068. Phospholip_A2_1. 1 hit.
[Graphical view]
PRINTSiPR00389. PHPHLIPASEA2.
SMARTiSM00085. PA2c. 1 hit.
[Graphical view]
SUPFAMiSSF48619. SSF48619. 1 hit.
PROSITEiPS00119. PA2_ASP. 1 hit.
PS00118. PA2_HIS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P20249-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
SLMQFETLIM KIAGRSGIWY YGSYGCYCGA GGQGRPQDAS DRCCFVHDCC
60 70 80 90 100
YGKVTGCDPK LDVYTYTEEN GAIVCGGDDP CKKQICECDK DAAICFRDNI
110 120
DTYDNKYWFF PAKNCQEESE PC
Length:122
Mass (Da):13,664
Last modified:February 1, 1991 - v1
Checksum:i9728BC3E27CC5474
GO

Cross-referencesi

3D structure databases

ProteinModelPortaliP20249.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG008137.

Family and domain databases

Gene3Di1.20.90.10. 1 hit.
InterProiIPR001211. PLipase_A2.
IPR013090. PLipase_A2_AS.
IPR016090. PLipase_A2_dom.
[Graphical view]
PANTHERiPTHR11716. PTHR11716. 1 hit.
PfamiPF00068. Phospholip_A2_1. 1 hit.
[Graphical view]
PRINTSiPR00389. PHPHLIPASEA2.
SMARTiSM00085. PA2c. 1 hit.
[Graphical view]
SUPFAMiSSF48619. SSF48619. 1 hit.
PROSITEiPS00119. PA2_ASP. 1 hit.
PS00118. PA2_HIS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Revised amino acid sequence, crystallization, and preliminary X-ray diffraction analysis of acidic phospholipase A2 from the venom of Agkistrodon halys blomhoffii."
    Tomoo K., Ohishi H., Ishida T., Inoue M., Ikeda K., Aoki Y., Samejima Y.
    J. Biol. Chem. 264:3636-3638(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.
    Tissue: Venom.
  2. "Complete amino acid sequence of phospholipase A2-II isolated from Agkistrodon halys blomhoffii venom."
    Samejima Y., Iwanaga S., Suzuki T.
    FEBS Lett. 47:348-351(1974) [PubMed] [Europe PMC] [Abstract]
    Cited for: PRELIMINARY PROTEIN SEQUENCE.
    Tissue: Venom.
  3. "Structure of acidic phospholipase A2 for the venom of Agkistrodon halys blomhoffii at 2.8-A resolution."
    Tomoo K., Ohishi H., Doi M., Ishida T., Inoue M., Ikeda K., Hata Y., Samejima Y.
    Biochem. Biophys. Res. Commun. 184:137-143(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).

Entry informationi

Entry nameiPA2A_GLOBL
AccessioniPrimary (citable) accession number: P20249
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: January 7, 2015
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Is not neurotoxic.

Keywords - Technical termi

Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.