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UniProtKB - P48650 (PA2HS_ECHCA)
Protein
Basic phospholipase A2 homolog ecarpholin S
Gene
N/A
Organism
Echis carinatus (Saw-scaled viper)
Status
Functioni
Snake venom phospholipase A2 homolog that lacks enzymatic activity. Shows high myotoxin activities and displays edema-inducing activities (PubMed:18586854).
1 PublicationCaution
Has been reported as being enzymatically active and calcium-dependently inducing platelet aggregation (PubMed:8921006). This activity appears to be unlikely in light of the lack of activity of both recombinant AtnL (S49) and bothropstoxin-1 (K49), especially keeping in mind the possibility of contamination of the purified protein with catalytically active sPLA2s. The fact that the high level of enzymatic activity reported was determined on PC substrates and that it was in the range of the human group IIA enzyme, which in fact displays a very low activity on PC-rich substrates, casts further doubt on the reported activity of ecarpholin S (PubMed:17927217).2 Publications
Does not bind calcium as one of the calcium-binding sites is lost (Asp->Ser in position 48, which corresponds to 'Ser-49' in the current nomenclature).Curated
Activity regulationi
Suramin inhibits the myotoxic activity (PubMed:18586854).1 Publication
GO - Molecular functioni
- calcium ion binding Source: InterPro
- phospholipase A2 activity Source: InterPro
GO - Biological processi
- arachidonic acid secretion Source: InterPro
- lipid catabolic process Source: InterPro
- phospholipid metabolic process Source: InterPro
Names & Taxonomyi
Protein namesi | Recommended name: Basic phospholipase A2 homolog ecarpholin S2 PublicationsShort name: Ecs-S491 Publication Short name: svPLA2 homolog |
Organismi | Echis carinatus (Saw-scaled viper) |
Taxonomic identifieri | 40353 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Bifurcata › Unidentata › Episquamata › Toxicofera › Serpentes › Colubroidea › Viperidae › Viperinae › Echis |
Subcellular locationi
Extracellular region or secreted
- Secreted 1 Publication
Extracellular region or secreted
- extracellular region Source: UniProtKB-SubCell
Keywords - Cellular componenti
SecretedPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000161643 | 1 – 122 | Basic phospholipase A2 homolog ecarpholin SAdd BLAST | 122 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Disulfide bondi | 26 ↔ 115 | Combined sources1 Publication | ||
Disulfide bondi | 28 ↔ 44 | Combined sources1 Publication | ||
Disulfide bondi | 43 ↔ 95 | Combined sources1 Publication | ||
Disulfide bondi | 49 ↔ 122 | Combined sources1 Publication | ||
Disulfide bondi | 50 ↔ 88 | Combined sources1 Publication | ||
Disulfide bondi | 57 ↔ 81 | Combined sources1 Publication | ||
Disulfide bondi | 75 ↔ 86 | Combined sources1 Publication |
Keywords - PTMi
Disulfide bondExpressioni
Tissue specificityi
Expressed by the venom gland.1 Publication
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P48650 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P48650 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 105 – 117 | Important for membrane-damaging activities in eukaryotes and bacteria; heparin-bindingBy similarityAdd BLAST | 13 |
Sequence similaritiesi
Family and domain databases
CDDi | cd00125, PLA2c, 1 hit |
Gene3Di | 1.20.90.10, 1 hit |
InterProi | View 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 |
PANTHERi | PTHR11716, PTHR11716, 1 hit |
Pfami | View protein in Pfam PF00068, Phospholip_A2_1, 1 hit |
PRINTSi | PR00389, PHPHLIPASEA2 |
SMARTi | View protein in SMART SM00085, PA2c, 1 hit |
SUPFAMi | SSF48619, SSF48619, 1 hit |
PROSITEi | View protein in PROSITE PS00119, PA2_ASP, 1 hit PS00118, PA2_HIS, 1 hit |
i Sequence
Sequence statusi: Complete.
P48650-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
SVVELGKMII QETGKSPFPS YTSYGCFCGG GERGPPLDAT DRCCLAHSCC
60 70 80 90 100
YDTLPDCSPK TDRYKYKREN GEIICENSTS CKKRICECDK AVAVCLRKNL
110 120
NTYNKKYTYY PNFWCKGDIE KC
Mass spectrometryi
Molecular mass is 13805±2.7 Da. Determined by ESI. 1 Publication
Similar proteinsi
Cross-referencesi
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
2QHD | X-ray | 1.95 | A/B | 1-122 | [»] | |
2QHE | X-ray | 2.00 | A | 1-122 | [»] | |
3BJW | X-ray | 2.30 | A/B/C/D/E/F/G/H | 1-122 | [»] | |
SMRi | P48650 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P48650 |
Family and domain databases
CDDi | cd00125, PLA2c, 1 hit |
Gene3Di | 1.20.90.10, 1 hit |
InterProi | View 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 |
PANTHERi | PTHR11716, PTHR11716, 1 hit |
Pfami | View protein in Pfam PF00068, Phospholip_A2_1, 1 hit |
PRINTSi | PR00389, PHPHLIPASEA2 |
SMARTi | View protein in SMART SM00085, PA2c, 1 hit |
SUPFAMi | SSF48619, SSF48619, 1 hit |
PROSITEi | View protein in PROSITE PS00119, PA2_ASP, 1 hit PS00118, PA2_HIS, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | PA2HS_ECHCA | |
Accessioni | P48650Primary (citable) accession number: P48650 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | November 1, 1997 |
Last sequence update: | November 1, 1997 | |
Last modified: | June 2, 2021 | |
This is version 102 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencingDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families