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A1IB2_LOXIN
ID   A1IB2_LOXIN             Reviewed;         302 AA.
AC   B2KKV7;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   03-AUG-2022, entry version 45.
DE   RecName: Full=Dermonecrotic toxin LiSicTox-alphaIA2bii;
DE            EC=4.6.1.- {ECO:0000250|UniProtKB:Q4ZFU2};
DE   AltName: Full=Loxtox i2;
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: Precursor; Fragment;
OS   Loxosceles intermedia (Brown spider).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae;
OC   Araneomorphae; Haplogynae; Scytodoidea; Sicariidae; Loxosceles.
OX   NCBI_TaxID=58218;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=17825864; DOI=10.1016/j.toxicon.2007.07.001;
RA   Kalapothakis E., Chatzaki M., Goncalves-Dornelas H., de Castro C.S.,
RA   Silvestre F.G., Laborne F.V., de Moura J.F., Veiga S.S.,
RA   Chavez-Olortegui C., Granier C., Barbaro K.C.;
RT   "The Loxtox protein family in Loxosceles intermedia (Mello-Leitao) venom.";
RL   Toxicon 50:938-946(2007).
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:17825864}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:17825864}.
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; EF535251; ABU43330.1; -; mRNA.
DR   AlphaFoldDB; B2KKV7; -.
DR   SMR; B2KKV7; -.
DR   ArachnoServer; AS000693; Sphingomyelinase D (LiSicTox-alphaIA2bii).
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; Glycoprotein; Hemolysis;
KW   Lipid degradation; Lipid metabolism; Lyase; Magnesium; Metal-binding;
KW   Secreted; Signal; Toxin; Zymogen.
FT   SIGNAL          <1..14
FT                   /evidence="ECO:0000255"
FT   PROPEP          15..22
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000380635"
FT   CHAIN           23..302
FT                   /note="Dermonecrotic toxin LiSicTox-alphaIA2bii"
FT                   /id="PRO_0000380636"
FT   ACT_SITE        34
FT                   /evidence="ECO:0000250|UniProtKB:Q8I914"
FT   ACT_SITE        70
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q8I914"
FT   BINDING         54
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q8I914"
FT   BINDING         56
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q8I914"
FT   BINDING         114
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q8I914"
FT   CARBOHYD        279
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        74..80
FT                   /evidence="ECO:0000250|UniProtKB:P0CE80"
FT   DISULFID        76..219
FT                   /evidence="ECO:0000250|UniProtKB:P0CE80"
FT   NON_TER         1
SQ   SEQUENCE   302 AA;  33627 MW;  871758A6434036F4 CRC64;
     IALILVCWSV LSQAAQTDVE GRADKRRPIW IMGHMVNAIA QIDEFVNLGA NSIETDVSFD
     DNANPEYTYH GVPCDCGRSC LKWENFNDFL KGLRSATTPG NAKYQAKLIL VVFDLKTGSL
     YDNQANEAGK KLAKNLLKHY WNNGNNGGRA YIVLSIPDLN HYPLIKGFKD QLTHDGHPEL
     MDKVGHDFSG NDAIGDVGNA YKKAGISGHV WQSDGITNCL LRGLDRVKQA IANRDSGNGF
     INKVYYWTVD KRATTRDALD AGVDGVMTNY PDVITDVLNE SAYKNKFRVA SYEDNPWETF
     KK
 
 
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