PA2BT_PROMU
ID PA2BT_PROMU Reviewed; 138 AA.
AC Q90W39;
DT 28-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Basic phospholipase A2 trimucrotoxin;
DE Short=svPLA2;
DE EC=3.1.1.4;
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE AltName: Full=TMV-D49-PLA2;
DE Flags: Precursor;
OS Protobothrops mucrosquamatus (Taiwan habu) (Trimeresurus mucrosquamatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Protobothrops.
OX NCBI_TaxID=103944;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, SUBUNIT,
RP AND TOXIC DOSE.
RC TISSUE=Venom, and Venom gland;
RX PubMed=7487947; DOI=10.1042/bj3110895;
RA Tsai I.-H., Lu P.J., Wang Y.-M., Ho C.L., Liaw L.L.;
RT "Molecular cloning and characterization of a neurotoxic phospholipase A2
RT from the venom of Taiwan habu (Trimeresurus mucrosquamatus).";
RL Biochem. J. 311:895-900(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Venom, and Venom gland;
RA Guo Y.-W., Liu H.-W., Chang T.-Y., Chen C.-T., Li C.-J.;
RT "Cloning, functional expression, and characterization of an edema-producing
RT Asp-49 phospholipase A2 from Trimeresurus mucrosquamatus.";
RL Toxin Rev. 28:271-280(2009).
RN [3]
RP PROTEIN SEQUENCE OF 17-39, FUNCTION, AND MASS SPECTROMETRY.
RC TISSUE=Venom;
RX PubMed=15032748; DOI=10.1042/bj20040125;
RA Chen Y.-H., Wang Y.-M., Hseu M.-J., Tsai I.-H.;
RT "Molecular evolution and structure-function relationships of crotoxin-like
RT and asparagine-6-containing phospholipases A2 in pit viper venoms.";
RL Biochem. J. 381:25-34(2004).
RN [4]
RP MUTAGENESIS OF ASN-22 AND 22-ASN--MET-24.
RX PubMed=9792175; DOI=10.1016/s0041-0101(98)00151-2;
RA Tsai I.-H., Wang Y.-M.;
RT "Effect of site directed mutagenesis on the activity of recombinant
RT trimucrotoxin, a neurotoxic phospholipase from Trimeresurus mucrosquamatus
RT venom.";
RL Toxicon 36:1591-1597(1998).
CC -!- FUNCTION: Snake venom phospholipase A2 (PLA2) that displays edema-
CC inducing activities, as well as presynaptic neurotoxicity and low
CC myotoxicity. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-
CC acyl groups in 3-sn-phosphoglycerides. {ECO:0000269|PubMed:15032748,
CC ECO:0000269|PubMed:7487947, ECO:0000269|Ref.2}.
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:0000255|PROSITE-ProRule:PRU10035, ECO:0000255|PROSITE-
CC ProRule:PRU10036};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:7487947}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000269|Ref.2}.
CC -!- MASS SPECTROMETRY: Mass=13902; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:15032748};
CC -!- TOXIC DOSE: LD(50) is 1.2 mg/kg by intravenous injection into mice.
CC {ECO:0000269|PubMed:7487947}.
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC D49 sub-subfamily. {ECO:0000305}.
CC -!- CAUTION: Ref.2 refers to only one protein (TMV-D49-PLA2), but
CC erroneously shows two sequences. The translation of AF408409 (mentioned
CC in Ref.2 as submitted to GenBank) differs by one amino acid from the
CC sequence shown in Fig.1 and described in the text (see the conflict at
CC position 71). {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X77645; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AF408409; AAK97534.1; -; mRNA.
DR PIR; S59522; S59522.
DR RefSeq; XP_015675832.1; XM_015820346.1.
DR RefSeq; XP_015675833.1; XM_015820347.1.
DR AlphaFoldDB; Q90W39; -.
DR SMR; Q90W39; -.
DR GeneID; 107291353; -.
DR KEGG; pmur:107291353; -.
DR OrthoDB; 1422829at2759; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004623; F:phospholipase A2 activity; IEA:UniProtKB-EC.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
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 CDD; cd00125; PLA2c; 1.
DR Gene3D; 1.20.90.10; -; 1.
DR InterPro; IPR001211; PLipase_A2.
DR InterPro; IPR033112; PLipase_A2_Asp_AS.
DR InterPro; IPR016090; PLipase_A2_dom.
DR InterPro; IPR036444; PLipase_A2_dom_sf.
DR InterPro; IPR033113; PLipase_A2_His_AS.
DR PANTHER; PTHR11716; PTHR11716; 1.
DR Pfam; PF00068; Phospholip_A2_1; 1.
DR PRINTS; PR00389; PHPHLIPASEA2.
DR SMART; SM00085; PA2c; 1.
DR SUPFAM; SSF48619; SSF48619; 1.
DR PROSITE; PS00119; PA2_ASP; 1.
DR PROSITE; PS00118; PA2_HIS; 1.
PE 1: Evidence at protein level;
KW Calcium; Direct protein sequencing; Disulfide bond; Hydrolase;
KW Lipid degradation; Lipid metabolism; Metal-binding; Myotoxin; Neurotoxin;
KW Presynaptic neurotoxin; Secreted; Signal; Toxin.
FT SIGNAL 1..16
FT /evidence="ECO:0000269|PubMed:15032748"
FT CHAIN 17..138
FT /note="Basic phospholipase A2 trimucrotoxin"
FT /id="PRO_0000022965"
FT ACT_SITE 63
FT /evidence="ECO:0000250"
FT ACT_SITE 105
FT /evidence="ECO:0000250"
FT BINDING 43
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 45
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 47
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 64
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT DISULFID 42..131
FT /evidence="ECO:0000250"
FT DISULFID 44..60
FT /evidence="ECO:0000250"
FT DISULFID 59..111
FT /evidence="ECO:0000250"
FT DISULFID 65..138
FT /evidence="ECO:0000250"
FT DISULFID 66..104
FT /evidence="ECO:0000250"
FT DISULFID 73..97
FT /evidence="ECO:0000250"
FT DISULFID 91..102
FT /evidence="ECO:0000250"
FT MUTAGEN 22..24
FT /note="NKM->ETL: 76% loss of PA2 activity and 97% loss of
FT toxicity."
FT /evidence="ECO:0000269|PubMed:9792175"
FT MUTAGEN 22
FT /note="N->A: 47% loss of PA2 activity and 67% loss of
FT toxicity."
FT /evidence="ECO:0000269|PubMed:9792175"
FT MUTAGEN 22
FT /note="N->E: 10% loss of PA2 activity and 90% loss of
FT toxicity."
FT /evidence="ECO:0000269|PubMed:9792175"
FT MUTAGEN 22
FT /note="N->R: 83% loss of PA2 activity and 97% loss of
FT toxicity."
FT /evidence="ECO:0000269|PubMed:9792175"
FT CONFLICT 71
FT /note="T -> Y (in Ref. 2; no nucleotide entry)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 138 AA; 15668 MW; AA8542A33DF52AB8 CRC64;
MRTLWIVAVL LLGVEGNLLQ FNKMIKIMTK KNAIPFYSSY GCYCGWGGQG KPKDATDRCC
FVHDCCYGKL TDCSPKSDIY SYSWKTGIII CGEGTECEKK ICECDRAAAV CLGHNLRTYK
KRYMFYPDFL CTDPSEKC
