HEMI2_HEMLE
ID HEMI2_HEMLE Reviewed; 36 AA.
AC P0DSN5;
DT 05-JUN-2019, integrated into UniProtKB/Swiss-Prot.
DT 05-JUN-2019, sequence version 1.
DT 25-MAY-2022, entry version 5.
DE RecName: Full=Phospholipase A2 hemilipin-2 {ECO:0000303|PubMed:27940138};
DE EC=3.1.1.4 {ECO:0000269|PubMed:27940138};
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE AltName: Full=Phospholipase A(2) {ECO:0000255|PROSITE-ProRule:PRU10035};
DE Contains:
DE RecName: Full=Hemilipin-2 large subunit {ECO:0000303|PubMed:27940138};
DE Contains:
DE RecName: Full=Hemilipin-2 small subunit {ECO:0000303|PubMed:27940138};
DE Flags: Fragments;
OS Hemiscorpius lepturus (Scorpion).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC Scorpiones; Iurida; Scorpionoidea; Hemiscorpiidae.
OX NCBI_TaxID=520031;
RN [1]
RP PROTEIN SEQUENCE, SUBCELLULAR LOCATION, FUNCTION, SUBUNIT, MASS
RP SPECTROMETRY, CATALYTIC ACTIVITY, AND COFACTOR.
RC TISSUE=Venom;
RX PubMed=27940138; DOI=10.1016/j.toxicon.2016.12.001;
RA Jridi I., Catacchio I., Majdoub H., Shahbazzadeh D., El Ayeb M.,
RA Frassanito M.A., Solimando A.G., Ribatti D., Vacca A., Borchani L.;
RT "The small subunit of Hemilipin2, a new heterodimeric phospholipase A2 from
RT Hemiscorpius lepturus scorpion venom, mediates the antiangiogenic effect of
RT the whole protein.";
RL Toxicon 126:38-46(2017).
CC -!- FUNCTION: Scorpion venom phospholipase A2 (PLA2) that impacts
CC angiogenesis in vitro and in vivo without showing any cytotoxic or
CC apoptotic signs (PubMed:27940138). The antiangiogenic effect is
CC independent from the catalytic activity and seems to be held by its
CC small subunit (PubMed:27940138). PLA2 catalyzes the calcium-dependent
CC hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
CC {ECO:0000269|PubMed:27940138}.
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:27940138};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:27940138};
CC Note=Binds 1 Ca(2+) ion. {ECO:0000269|PubMed:27940138};
CC -!- SUBUNIT: Heterodimer composed of a small subunit and a large subunit;
CC disulfid-linked. {ECO:0000269|PubMed:27940138}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:27940138}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:27940138}.
CC -!- MASS SPECTROMETRY: [Hemilipin-2 large subunit]: Mass=12866.63;
CC Method=MALDI; Evidence={ECO:0000269|PubMed:27940138};
CC -!- MASS SPECTROMETRY: [Hemilipin-2 small subunit]: Mass=2461.27;
CC Method=MALDI; Evidence={ECO:0000269|PubMed:27940138};
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group III
CC subfamily. {ECO:0000305}.
CC -!- CAUTION: The large subunit has no homology with other group III PA2
CC family members, but the small subunit does.
CC {ECO:0000305|PubMed:27940138}.
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DR AlphaFoldDB; P0DSN5; -.
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:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Calcium; Cleavage on pair of basic residues; Direct protein sequencing;
KW Disulfide bond; Hydrolase; Lipid degradation; Lipid metabolism;
KW Metal-binding; Secreted; Zymogen.
FT CHAIN 1..>24
FT /note="Hemilipin-2 large subunit"
FT /evidence="ECO:0000269|PubMed:27940138"
FT /id="PRO_0000447336"
FT PEPTIDE 25..>36
FT /note="Hemilipin-2 small subunit"
FT /evidence="ECO:0000269|PubMed:27940138"
FT /id="PRO_0000447337"
FT DISULFID 16..?
FT /evidence="ECO:0000250|UniProtKB:Q6T178"
FT DISULFID ?..28
FT /note="Interchain (between large and small chains)"
FT /evidence="ECO:0000250|UniProtKB:Q6T178"
FT NON_CONS 24..25
FT /evidence="ECO:0000305"
FT NON_TER 36
FT /evidence="ECO:0000305"
SQ SEQUENCE 36 AA; 3880 MW; 23626E62A778E911 CRC64;
DSLSEDNWKF VVSSSCETIL EILDIGGCAK GVAEYT
