UniProtKB - A0A1L4BJ46 (HEMI1_HEMLE)
Protein
Phospholipase A2 hemilipin
Gene
N/A
Organism
Hemiscorpius lepturus (Scorpion)
Status
Functioni
Scorpion venom phospholipase A2 (PLA2) that shows high hydrolytic activities towards lecithin and acts as an effective blocker of all angiogenesis key steps in vivo and in vitro (PubMed:26335363). It has no effect on apoptosis and does not display hemolytic, inflammatory or neurotoxic effects (PubMed:26335363). PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.1 Publication
Catalytic activityi
- a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H+1 PublicationEC:3.1.1.41 Publication
Cofactori
Ca2+1 PublicationNote: Binds 1 Ca2+ ion.1 Publication
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 115 | Calcium; via carbonyl oxygenBy similarity | 1 | |
Metal bindingi | 117 | Calcium; via carbonyl oxygenBy similarity | 1 | |
Metal bindingi | 119 | Calcium; via carbonyl oxygenBy similarity | 1 | |
Active sitei | 140 | PROSITE-ProRule annotation | 1 | |
Metal bindingi | 141 | CalciumBy similarity | 1 |
GO - Molecular functioni
- metal ion binding Source: UniProtKB-KW
- phospholipase A2 activity Source: UniProtKB-EC
- phospholipase A2 activity (consuming 1,2-dipalmitoylphosphatidylcholine) Source: UniProtKB-EC
- phospholipase A2 activity consuming 1,2-dioleoylphosphatidylethanolamine) Source: UniProtKB-EC
GO - Biological processi
- arachidonic acid secretion Source: InterPro
- lipid catabolic process Source: UniProtKB-KW
- phospholipid metabolic process Source: InterPro
Keywordsi
Molecular function | Hydrolase |
Biological process | Lipid degradation, Lipid metabolism |
Ligand | Calcium, Metal-binding |
Names & Taxonomyi
Protein namesi | Recommended name: Phospholipase A2 hemilipin1 Publication (EC:3.1.1.41 Publication)Alternative name(s): Phosphatidylcholine 2-acylhydrolase Phospholipase A(2)PROSITE-ProRule annotation Cleaved into the following 2 chains: Phospholipase A2 large subunit1 Publication Phospholipase A2 small subunit1 Publication |
Organismi | Hemiscorpius lepturus (Scorpion) |
Taxonomic identifieri | 520031 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Ecdysozoa › Arthropoda › Chelicerata › Arachnida › Scorpiones › Iurida › Scorpionoidea › Hemiscorpiidae › |
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 |
---|---|---|---|---|
Signal peptidei | 1 – 18 | Sequence analysisAdd BLAST | 18 | |
PropeptideiPRO_0000447333 | 19 – 105 | CuratedAdd BLAST | 87 | |
ChainiPRO_5012227965 | 106 – 213 | Phospholipase A2 large subunit1 PublicationAdd BLAST | 108 | |
PropeptideiPRO_0000447334 | 214 – 217 | Curated | 4 | |
PeptideiPRO_0000447335 | 218 – 232 | Phospholipase A2 small subunit1 PublicationAdd BLAST | 15 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Disulfide bondi | 116 ↔ 137 | By similarity | ||
Glycosylationi | 124 | N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation | 1 | |
Disulfide bondi | 136 ↔ 175 | By similarity | ||
Disulfide bondi | 143 ↔ 168 | By similarity | ||
Glycosylationi | 157 | N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation | 1 | |
Disulfide bondi | 166 ↔ 206 | By similarity | ||
Disulfide bondi | 211 ↔ 219 | Interchain (between large and small chains)By similarity |
Keywords - PTMi
Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, ZymogenExpressioni
Tissue specificityi
Expressed by the venom gland.1 Publication
Interactioni
Subunit structurei
Heterodimer composed of a small subunit and a large subunit; disulfid-linked.
1 PublicationFamily & Domainsi
Sequence similaritiesi
Keywords - Domaini
SignalFamily and domain databases
Gene3Di | 1.20.90.10, 1 hit |
InterProi | View protein in InterPro IPR016090, PLipase_A2_dom IPR036444, PLipase_A2_dom_sf IPR033113, PLipase_A2_His_AS |
Pfami | View protein in Pfam PF05826, Phospholip_A2_2, 1 hit |
SUPFAMi | SSF48619, SSF48619, 1 hit |
PROSITEi | View protein in PROSITE PS00118, PA2_HIS, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
A0A1L4BJ46-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MTFLILTILA TVTPSLYSHV VQRELRVNFE PLAGQRDSWP VARAAMVTFD
60 70 80 90 100
ARSEKAREFS ECRMINSMHE LSRELMDSPE HTVKRASKEE MDDLVQRCSG
110 120 130 140 150
SAEGRSWFIW PDTKWCGPGT DAKNESDLGP LEADKCCRTH DHCDYIGAGE
160 170 180 190 200
TKYGLTNKSF FTKLNCKCEA AFDQCLKESI DRAEGSAKSS MEGLHSFYFN
210 220 230
TYSPECYEVK CSRKRDAECT NGIAIWKDSY KS
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 118 | P → V AA sequence (PubMed:26335363).Curated | 1 | |
Sequence conflicti | 123 – 124 | KN → AS AA sequence (PubMed:26335363).Curated | 2 |
Mass spectrometryi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | KX924472 mRNA Translation: API81335.1 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | KX924472 mRNA Translation: API81335.1 |
3D structure databases
SMRi | A0A1L4BJ46 |
ModBasei | Search... |
Family and domain databases
Gene3Di | 1.20.90.10, 1 hit |
InterProi | View protein in InterPro IPR016090, PLipase_A2_dom IPR036444, PLipase_A2_dom_sf IPR033113, PLipase_A2_His_AS |
Pfami | View protein in Pfam PF05826, Phospholip_A2_2, 1 hit |
SUPFAMi | SSF48619, SSF48619, 1 hit |
PROSITEi | View protein in PROSITE PS00118, PA2_HIS, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | HEMI1_HEMLE | |
Accessioni | A0A1L4BJ46Primary (citable) accession number: A0A1L4BJ46 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | June 5, 2019 |
Last sequence update: | March 15, 2017 | |
Last modified: | February 26, 2020 | |
This is version 9 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) |
Miscellaneousi
Keywords - Technical termi
Direct protein sequencingDocuments
- SIMILARITY comments
Index of protein domains and families