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Protein

Group 10 secretory phospholipase A2

Gene

Pla2g10

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

PA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. Has a powerful potency for releasing arachidonic acid from cell membrane phospholipids (By similarity).By similarity

Catalytic activityi

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

Cofactori

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi54 – 541Calcium; via carbonyl oxygenBy similarity
Metal bindingi56 – 561Calcium; via carbonyl oxygenBy similarity
Metal bindingi58 – 581Calcium; via carbonyl oxygenBy similarity
Active sitei74 – 741By similarity
Metal bindingi75 – 751CalciumBy similarity
Active sitei119 – 1191By similarity

GO - Molecular functioni

  • calcium ion binding Source: InterPro
  • phospholipase A2 activity Source: RGD

GO - Biological processi

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:
Group 10 secretory phospholipase A2 (EC:3.1.1.4)
Alternative name(s):
Group X secretory phospholipase A2
Short name:
GX sPLA2
Short name:
sPLA2-X
Phosphatidylcholine 2-acylhydrolase 10
Gene namesi
Name:Pla2g10
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi61935. Pla2g10.

Subcellular locationi

GO - Cellular componenti

  • extracellular region Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717By similarityAdd
BLAST
Propeptidei18 – 2811By similarityPRO_0000022768Add
BLAST
Chaini29 – 151123Group 10 secretory phospholipase A2PRO_0000022769Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi39 ↔ 97By similarity
Disulfide bondi53 ↔ 143By similarity
Disulfide bondi55 ↔ 71By similarity
Disulfide bondi70 ↔ 125By similarity
Disulfide bondi76 ↔ 150By similarity
Disulfide bondi77 ↔ 118By similarity
Disulfide bondi86 ↔ 111By similarity
Disulfide bondi104 ↔ 116By similarity

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond

Proteomic databases

PaxDbiQ9QZT3.
PRIDEiQ9QZT3.

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000004237.

Structurei

3D structure databases

ProteinModelPortaliQ9QZT3.
SMRiQ9QZT3. Positions 29-151.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the phospholipase A2 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG4087. Eukaryota.
ENOG411283D. LUCA.
HOGENOMiHOG000231749.
HOVERGENiHBG008137.
InParanoidiQ9QZT3.
KOiK01047.
PhylomeDBiQ9QZT3.

Family and domain databases

Gene3Di1.20.90.10. 1 hit.
InterProiIPR001211. PLipase_A2.
IPR033112. PLipase_A2_Asp_AS.
IPR016090. PLipase_A2_dom.
IPR033113. PLipase_A2_His_AS.
[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.

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

Q9QZT3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLLLLLLLLL GPGSCLSEAT RRSHVYKRGL LELAGTLDCV GPRSPMAYMN
60 70 80 90 100
YGCYCGLGGH GEPRDAIDWC CYYHDCCYSQ AQDAGCSPKL YRYPWKCMDH
110 120 130 140 150
RILCGPAENK CQELLCRCDE TLAYCLADTE YHLKYLFFPS VLCEKDSPKC

N
Length:151
Mass (Da):17,088
Last modified:May 1, 2000 - v1
Checksum:i2581E1520A455089
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF166100 mRNA. Translation: AAF04501.1.
RefSeqiNP_058872.1. NM_017176.2.
UniGeneiRn.6828.

Genome annotation databases

GeneIDi29359.
KEGGirno:29359.
UCSCiRGD:61935. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF166100 mRNA. Translation: AAF04501.1.
RefSeqiNP_058872.1. NM_017176.2.
UniGeneiRn.6828.

3D structure databases

ProteinModelPortaliQ9QZT3.
SMRiQ9QZT3. Positions 29-151.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000004237.

Proteomic databases

PaxDbiQ9QZT3.
PRIDEiQ9QZT3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi29359.
KEGGirno:29359.
UCSCiRGD:61935. rat.

Organism-specific databases

CTDi8399.
RGDi61935. Pla2g10.

Phylogenomic databases

eggNOGiKOG4087. Eukaryota.
ENOG411283D. LUCA.
HOGENOMiHOG000231749.
HOVERGENiHBG008137.
InParanoidiQ9QZT3.
KOiK01047.
PhylomeDBiQ9QZT3.

Miscellaneous databases

NextBioi608878.
PROiQ9QZT3.

Family and domain databases

Gene3Di1.20.90.10. 1 hit.
InterProiIPR001211. PLipase_A2.
IPR033112. PLipase_A2_Asp_AS.
IPR016090. PLipase_A2_dom.
IPR033113. PLipase_A2_His_AS.
[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. "On the diversity of secreted phospholipases A2. Cloning, tissue distribution, and functional expression of two novel mouse group II enzymes."
    Valentin E., Ghomashchi F., Gelb M.H., Lazdunski M., Lambeau G.
    J. Biol. Chem. 274:31195-31202(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Entry informationi

Entry nameiPA2GX_RAT
AccessioniPrimary (citable) accession number: Q9QZT3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 11, 2002
Last sequence update: May 1, 2000
Last modified: May 11, 2016
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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 one 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.