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A1IB1_LOXHI
ID   A1IB1_LOXHI             Reviewed;         273 AA.
AC   C0JAR9;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 39.
DE   RecName: Full=Dermonecrotic toxin LhSicTox-alphaIA2bi {ECO:0000303|PubMed:19042943};
DE            EC=4.6.1.- {ECO:0000250|UniProtKB:Q4ZFU2};
DE   AltName: Full=Phospholipase D;
DE            Short=PLD;
DE   AltName: Full=Sphingomyelin phosphodiesterase D;
DE            Short=SMD;
DE            Short=SMase D;
DE            Short=Sphingomyelinase D;
DE   Flags: Fragment;
OS   Loxosceles hirsuta (Recluse spider).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae;
OC   Araneomorphae; Haplogynae; Scytodoidea; Sicariidae; Loxosceles.
OX   NCBI_TaxID=571525;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND NOMENCLATURE.
RC   TISSUE=Venom gland;
RX   PubMed=19042943; DOI=10.1093/molbev/msn274;
RA   Binford G.J., Bodner M.R., Cordes M.H., Baldwin K.L., Rynerson M.R.,
RA   Burns S.N., Zobel-Thropp P.A.;
RT   "Molecular evolution, functional variation, and proposed nomenclature of
RT   the gene family that includes sphingomyelinase D in sicariid spider
RT   venoms.";
RL   Mol. Biol. Evol. 26:547-566(2009).
CC   -!- FUNCTION: Dermonecrotic toxins cleave the phosphodiester linkage
CC       between the phosphate and headgroup of certain phospholipids
CC       (sphingolipid and lysolipid substrates), forming an alcohol (often
CC       choline) and a cyclic phosphate (By similarity). This toxin acts on
CC       sphingomyelin (SM) (By similarity). It may also act on ceramide
CC       phosphoethanolamine (CPE), lysophosphatidylcholine (LPC) and
CC       lysophosphatidylethanolamine (LPE), but not on lysophosphatidylserine
CC       (LPS), and lysophosphatidylglycerol (LPG) (By similarity). It acts by
CC       transphosphatidylation, releasing exclusively cyclic phosphate products
CC       as second products (By similarity). Induces dermonecrosis, hemolysis,
CC       increased vascular permeability, edema, inflammatory response, and
CC       platelet aggregation (By similarity).
CC       {ECO:0000250|UniProtKB:A0A0D4WTV1, ECO:0000250|UniProtKB:P0CE80}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an N-(acyl)-sphingosylphosphocholine = an N-(acyl)-sphingosyl-
CC         1,3-cyclic phosphate + choline; Xref=Rhea:RHEA:60652,
CC         ChEBI:CHEBI:15354, ChEBI:CHEBI:64583, ChEBI:CHEBI:143892;
CC         Evidence={ECO:0000250|UniProtKB:A0A0D4WTV1};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an N-(acyl)-sphingosylphosphoethanolamine = an N-(acyl)-
CC         sphingosyl-1,3-cyclic phosphate + ethanolamine; Xref=Rhea:RHEA:60648,
CC         ChEBI:CHEBI:57603, ChEBI:CHEBI:143891, ChEBI:CHEBI:143892;
CC         Evidence={ECO:0000250|UniProtKB:A0A0D4WTV1};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1-acyl-sn-glycero-3-phosphocholine = a 1-acyl-sn-glycero-
CC         2,3-cyclic phosphate + choline; Xref=Rhea:RHEA:60700,
CC         ChEBI:CHEBI:15354, ChEBI:CHEBI:58168, ChEBI:CHEBI:143947;
CC         Evidence={ECO:0000250|UniProtKB:A0A0D4WTV1};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1-acyl-sn-glycero-3-phosphoethanolamine = a 1-acyl-sn-
CC         glycero-2,3-cyclic phosphate + ethanolamine; Xref=Rhea:RHEA:60704,
CC         ChEBI:CHEBI:57603, ChEBI:CHEBI:64381, ChEBI:CHEBI:143947;
CC         Evidence={ECO:0000250|UniProtKB:A0A0D4WTV1};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:Q8I914};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:Q8I914};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:19042943}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:19042943}.
CC   -!- SIMILARITY: Belongs to the arthropod phospholipase D family. Class II
CC       subfamily. {ECO:0000305}.
CC   -!- CAUTION: The most common activity assay for dermonecrotic toxins
CC       detects enzymatic activity by monitoring choline release from
CC       substrate. Liberation of choline from sphingomyelin (SM) or
CC       lysophosphatidylcholine (LPC) is commonly assumed to result from
CC       substrate hydrolysis, giving either ceramide-1-phosphate (C1P) or
CC       lysophosphatidic acid (LPA), respectively, as a second product.
CC       However, two studies from Lajoie and colleagues (2013 and 2015) report
CC       the observation of exclusive formation of cyclic phosphate products as
CC       second products, resulting from intramolecular transphosphatidylation.
CC       Cyclic phosphates have vastly different biological properties from
CC       their monoester counterparts, and they may be relevant to the pathology
CC       of brown spider envenomation. {ECO:0000250|UniProtKB:A0A0D4WTV1,
CC       ECO:0000250|UniProtKB:A0A0D4WV12, ECO:0000250|UniProtKB:Q4ZFU2}.
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DR   EMBL; FJ171354; ACN48850.1; -; mRNA.
DR   AlphaFoldDB; C0JAR9; -.
DR   SMR; C0JAR9; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008081; F:phosphoric diester hydrolase activity; IEA:InterPro.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.190; -; 1.
DR   InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR   SUPFAM; SSF51695; SSF51695; 1.
PE   2: Evidence at transcript level;
KW   Cytolysis; Dermonecrotic toxin; Disulfide bond; Hemolysis;
KW   Lipid degradation; Lipid metabolism; Lyase; Magnesium; Metal-binding;
KW   Secreted; Toxin.
FT   CHAIN           <1..273
FT                   /note="Dermonecrotic toxin LhSicTox-alphaIA2bi"
FT                   /id="PRO_0000392757"
FT   ACT_SITE        41
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q8I914"
FT   BINDING         25
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q8I914"
FT   BINDING         27
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q8I914"
FT   BINDING         85
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q8I914"
FT   DISULFID        45..51
FT                   /evidence="ECO:0000250|UniProtKB:P0CE80"
FT   DISULFID        47..190
FT                   /evidence="ECO:0000250|UniProtKB:P0CE80"
FT   NON_TER         1
SQ   SEQUENCE   273 AA;  30472 MW;  2685C42850C9F625 CRC64;
     WIMGYMVNAI YQIDEFVNLG ANSIETDVSF DDNANPEYTY HGIPCDCGRS CLKWENYNDF
     LKGLRSATTP GNSKYQSKLI LVVFDLKTGS LYDNQASEAG KKLAKNLLKH YWNNGNNGGR
     AYIVLSIPDL NHYPLIKGFT DTLKQEGHPE LLEKVGYDFS GNDAIGDVAK AYKKAGVSGH
     VWQSDGITNC LLRGLSRVKD AVANRDSGKG YINKVYYWTV DKRATTRDAL DAGVDGVMTN
     YPDVIADVMN EAAYKNKVRL ATYEDSPWVT FKK
 
 
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