HEMI1_HEMLE
ID HEMI1_HEMLE Reviewed; 232 AA.
AC A0A1L4BJ46;
DT 05-JUN-2019, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 1.
DT 03-AUG-2022, entry version 12.
DE RecName: Full=Phospholipase A2 hemilipin {ECO:0000303|PubMed:26335363};
DE EC=3.1.1.4 {ECO:0000269|PubMed:26335363};
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE AltName: Full=Phospholipase A(2) {ECO:0000255|PROSITE-ProRule:PRU10035};
DE Contains:
DE RecName: Full=Phospholipase A2 large subunit {ECO:0000303|PubMed:26335363};
DE Contains:
DE RecName: Full=Phospholipase A2 small subunit {ECO:0000303|PubMed:26335363};
DE Flags: Precursor;
OS Hemiscorpius lepturus (Scorpion).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC Scorpiones; Iurida; Scorpionoidea; Hemiscorpiidae.
OX NCBI_TaxID=520031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX PubMed=27914888; DOI=10.1016/j.toxicon.2016.11.261;
RA Kazemi-Lomedasht F., Khalaj V., Bagheri K.P., Behdani M., Shahbazzadeh D.;
RT "The first report on transcriptome analysis of the venom gland of Iranian
RT scorpion, Hemiscorpius lepturus.";
RL Toxicon 125:123-130(2016).
RN [2]
RP PROTEIN SEQUENCE OF 106-129 AND 218-227, FUNCTION, SUBCELLULAR LOCATION,
RP MASS SPECTROMETRY, SUBUNIT, CATALYTIC ACTIVITY, AND COFACTOR.
RC TISSUE=Venom;
RX PubMed=26335363; DOI=10.1016/j.toxicon.2015.08.022;
RA Jridi I., Catacchio I., Majdoub H., Shahbazeddah D., El Ayeb M.,
RA Frassanito M.A., Ribatti D., Vacca A., Borchani L.;
RT "Hemilipin, a novel Hemiscorpius lepturus venom heterodimeric phospholipase
RT A2, which inhibits angiogenesis in vitro and in vivo.";
RL Toxicon 105:34-44(2015).
CC -!- FUNCTION: Scorpion venom phospholipase A2 (PLA2) that shows high
CC hydrolytic activities towards lecithin and acts as an effective blocker
CC of all angiogenesis key steps in vivo and in vitro (PubMed:26335363).
CC It has no effect on apoptosis and does not display hemolytic,
CC inflammatory or neurotoxic effects (PubMed:26335363). PLA2 catalyzes
CC the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-
CC phosphoglycerides. {ECO:0000269|PubMed:26335363}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-
CC glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868,
CC ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4;
CC Evidence={ECO:0000269|PubMed:26335363};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:26335363};
CC Note=Binds 1 Ca(2+) ion. {ECO:0000269|PubMed:26335363};
CC -!- SUBUNIT: Heterodimer composed of a small subunit and a large subunit;
CC disulfid-linked. {ECO:0000269|PubMed:26335363}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:26335363}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:26335363}.
CC -!- MASS SPECTROMETRY: [Phospholipase A2 large subunit]: Mass=13293.65;
CC Method=MALDI; Evidence={ECO:0000269|PubMed:26335363};
CC -!- MASS SPECTROMETRY: [Phospholipase A2 small subunit]: Mass=2008.05;
CC Method=MALDI; Evidence={ECO:0000269|PubMed:26335363};
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group III
CC subfamily. {ECO:0000305}.
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DR EMBL; KX924472; API81335.1; -; mRNA.
DR AlphaFoldDB; A0A1L4BJ46; -.
DR SMR; A0A1L4BJ46; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004623; F:phospholipase A2 activity; IEA:UniProtKB-EC.
DR GO; GO:0050482; P:arachidonic acid secretion; IEA:InterPro.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006644; P:phospholipid metabolic process; IEA:InterPro.
DR Gene3D; 1.20.90.10; -; 1.
DR InterPro; IPR016090; PLipase_A2_dom.
DR InterPro; IPR036444; PLipase_A2_dom_sf.
DR InterPro; IPR033113; PLipase_A2_His_AS.
DR Pfam; PF05826; Phospholip_A2_2; 1.
DR SUPFAM; SSF48619; SSF48619; 1.
DR PROSITE; PS00118; PA2_HIS; 1.
PE 1: Evidence at protein level;
KW Calcium; Cleavage on pair of basic residues; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Hydrolase; Lipid degradation;
KW Lipid metabolism; Metal-binding; Secreted; Signal; Zymogen.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT PROPEP 19..105
FT /evidence="ECO:0000305"
FT /id="PRO_0000447333"
FT CHAIN 106..213
FT /note="Phospholipase A2 large subunit"
FT /evidence="ECO:0000305|PubMed:26335363"
FT /id="PRO_5012227965"
FT PROPEP 214..217
FT /evidence="ECO:0000305"
FT /id="PRO_0000447334"
FT PEPTIDE 218..232
FT /note="Phospholipase A2 small subunit"
FT /evidence="ECO:0000305|PubMed:26335363"
FT /id="PRO_0000447335"
FT ACT_SITE 140
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10035"
FT BINDING 115
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P00630"
FT BINDING 117
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P00630"
FT BINDING 119
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P00630"
FT BINDING 141
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P00630"
FT CARBOHYD 124
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 157
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 116..137
FT /evidence="ECO:0000250|UniProtKB:Q6T178"
FT DISULFID 136..175
FT /evidence="ECO:0000250|UniProtKB:Q6T178"
FT DISULFID 143..168
FT /evidence="ECO:0000250|UniProtKB:Q6T178"
FT DISULFID 166..206
FT /evidence="ECO:0000250|UniProtKB:Q6T178"
FT DISULFID 211..219
FT /note="Interchain (between large and small chains)"
FT /evidence="ECO:0000250|UniProtKB:Q6T178"
FT CONFLICT 118
FT /note="P -> V (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 123..124
FT /note="KN -> AS (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 232 AA; 26339 MW; D4D24BCACE6989B2 CRC64;
MTFLILTILA TVTPSLYSHV VQRELRVNFE PLAGQRDSWP VARAAMVTFD ARSEKAREFS
ECRMINSMHE LSRELMDSPE HTVKRASKEE MDDLVQRCSG SAEGRSWFIW PDTKWCGPGT
DAKNESDLGP LEADKCCRTH DHCDYIGAGE TKYGLTNKSF FTKLNCKCEA AFDQCLKESI
DRAEGSAKSS MEGLHSFYFN TYSPECYEVK CSRKRDAECT NGIAIWKDSY KS
