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A1KA1_LOXAR
ID   A1KA1_LOXAR             Reviewed;         306 AA.
AC   Q4ZFU1;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=Dermonecrotic toxin LarSicTox-alphaIB1ai;
DE            EC=4.6.1.- {ECO:0000250|UniProtKB:Q4ZFU2};
DE   AltName: Full=Phospholipase D;
DE            Short=PLD;
DE   AltName: Full=Sphingomyelin phosphodiesterase D 3;
DE            Short=SMD 3;
DE            Short=SMase D 3;
DE            Short=Sphingomyelinase D 3;
DE   Flags: Precursor; Fragment;
OS   Loxosceles arizonica (Arizona brown spider).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae;
OC   Araneomorphae; Haplogynae; Scytodoidea; Sicariidae; Loxosceles.
OX   NCBI_TaxID=196454;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=15777950; DOI=10.1016/j.toxicon.2004.11.011;
RA   Binford G.J., Cordes M.H.J., Wells M.A.;
RT   "Sphingomyelinase D from venoms of Loxosceles spiders: evolutionary
RT   insights from cDNA sequences and gene structure.";
RL   Toxicon 45:547-560(2005).
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:15777950}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:15777950}.
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; AY699704; AAW22998.1; -; mRNA.
DR   AlphaFoldDB; Q4ZFU1; -.
DR   SMR; Q4ZFU1; -.
DR   ArachnoServer; AS000142; SicTox-LazalphaIB1ai.
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..1
FT                   /evidence="ECO:0000255"
FT   PROPEP          2..27
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000279551"
FT   CHAIN           28..306
FT                   /note="Dermonecrotic toxin LarSicTox-alphaIB1ai"
FT                   /id="PRO_0000279552"
FT   ACT_SITE        38
FT                   /evidence="ECO:0000250|UniProtKB:Q8I914"
FT   ACT_SITE        74
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q8I914"
FT   BINDING         58
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q8I914"
FT   BINDING         60
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q8I914"
FT   BINDING         118
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q8I914"
FT   CARBOHYD        283
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        78..84
FT                   /evidence="ECO:0000250|UniProtKB:P0CE80"
FT   DISULFID        80..223
FT                   /evidence="ECO:0000250|UniProtKB:P0CE80"
FT   NON_TER         1
SQ   SEQUENCE   306 AA;  34132 MW;  FA3668B8246CA6D3 CRC64;
     VRATEKFASM YFFCHSPQSA ETDVAERGNK RPVWIMGHMV NAIAQIDEFV NLGANSIETD
     VSFDSSANPE YTYHGVPCDC GRTCTKWEHF NEFLKGLRKA TTPGDSKYHE KLVLVVFDLK
     TGRLYDNQAS DAGKKLAKSL LQNYWNNGNN GGRAYIVLSI PNLAHYKLIA GFKEALTSEG
     HPELMDKVGY DFSGNDDIGD VANAYKKAGV TGHVWQSDGI TNCLLRGLDR VGKAVANRDS
     SNGYINKVYY WTVDKRQSTR DALDAGVDGI MTNYPDVIAD VLNESAYKAK FRIASYDDNP
     WETYKN
 
 
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