PA2B_BOTNI
ID PA2B_BOTNI Reviewed; 122 AA.
AC C0HJL8;
DT 09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT 09-DEC-2015, sequence version 1.
DT 03-AUG-2022, entry version 17.
DE RecName: Full=Phospholipase A2 nigroviriditoxin basic subunit B {ECO:0000305|PubMed:25434534};
DE Short=Ngvtx-B {ECO:0000303|PubMed:25434534};
DE Short=svPLA2 {ECO:0000305};
DE EC=3.1.1.4 {ECO:0000255|PROSITE-ProRule:PRU10035};
DE AltName: Full=Phospholipase A(2) {ECO:0000255|PROSITE-ProRule:PRU10035};
OS Bothriechis nigroviridis (Black-speckled palm pit viper).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Bothriechis.
OX NCBI_TaxID=88079 {ECO:0000303|PubMed:25434534};
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE OF 1-121, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, MASS
RP SPECTROMETRY, TOXIC DOSE, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Venom {ECO:0000303|PubMed:25434534};
RX PubMed=25434534; DOI=10.1016/j.toxicon.2014.11.235;
RA Lomonte B., Mora-Obando D., Fernandez J., Sanz L., Pla D., Gutierrez J.M.,
RA Calvete J.J.;
RT "First crotoxin-like phospholipase A(2) complex from a New World non-
RT rattlesnake species: nigroviriditoxin, from the arboreal Neotropical snake
RT Bothriechis nigroviridis.";
RL Toxicon 93:144-154(2015).
RN [2]
RP PROTEIN SEQUENCE OF 1-64, SUBCELLULAR LOCATION, MASS SPECTROMETRY, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Venom {ECO:0000303|PubMed:20590130};
RX PubMed=20590130; DOI=10.1021/pr100545d;
RA Fernandez J., Lomonte B., Sanz L., Angulo Y., Gutierrez J.M., Calvete J.J.;
RT "Snake venomics of Bothriechis nigroviridis reveals extreme variability
RT among palm pitviper venoms: different evolutionary solutions for the same
RT trophic purpose.";
RL J. Proteome Res. 9:4234-4241(2010).
CC -!- FUNCTION: Heterodimer A-B: Nigroviriditoxin possesses phospholipase A2
CC (PLA2) activity. It consists of a non-covalent association of a basic
CC PLA2 subunit B with a non-enzymatic subunit A.
CC {ECO:0000269|PubMed:25434534}.
CC -!- FUNCTION: Subunit B: Snake venom phospholipase A2 (PLA2) that induces
CC myonecrosis in mice. PLA2 catalyzes the calcium-dependent hydrolysis of
CC the 2-acyl groups in 3-sn-phosphoglycerides.
CC {ECO:0000269|PubMed:25434534}.
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};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:P24027};
CC Note=Binds 1 Ca(2+) ion. {ECO:0000250|UniProtKB:P24027};
CC -!- SUBUNIT: Nigroviriditoxin is a heterodimer of an acidic subunit A and a
CC basic subunit B. {ECO:0000269|PubMed:25434534}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20590130,
CC ECO:0000269|PubMed:25434534}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:25434534}.
CC -!- MASS SPECTROMETRY: Mass=14083; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:25434534};
CC -!- MASS SPECTROMETRY: Mass=14092; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:20590130};
CC -!- TOXIC DOSE: LD(50) is 2.9 mg/kg by intravenous injection in mice.
CC Toxicity is higher in combination with subunit A.
CC {ECO:0000269|PubMed:25434534}.
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC D49 sub-subfamily. {ECO:0000305}.
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DR AlphaFoldDB; C0HJL8; -.
DR SMR; C0HJL8; -.
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:InterPro.
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 Metal-binding; Secreted; Toxin.
FT CHAIN 1..122
FT /note="Phospholipase A2 nigroviriditoxin basic subunit B"
FT /id="PRO_0000434985"
FT ACT_SITE 47
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10035"
FT ACT_SITE 89
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10036"
FT BINDING 27
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P24027"
FT BINDING 29
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P24027"
FT BINDING 31
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P24027"
FT BINDING 48
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P24027"
FT DISULFID 26..115
FT /evidence="ECO:0000250|UniProtKB:P24027"
FT DISULFID 28..44
FT /evidence="ECO:0000250|UniProtKB:P24027"
FT DISULFID 43..95
FT /evidence="ECO:0000250|UniProtKB:P24027"
FT DISULFID 49..122
FT /evidence="ECO:0000250|UniProtKB:P24027"
FT DISULFID 50..88
FT /evidence="ECO:0000250|UniProtKB:P24027"
FT DISULFID 57..81
FT /evidence="ECO:0000250|UniProtKB:P24027"
FT DISULFID 75..86
FT /evidence="ECO:0000250|UniProtKB:P24027"
FT UNSURE 122
FT /note="Assigned by similarity to orthologs"
FT /evidence="ECO:0000305|PubMed:25434534"
FT CONFLICT 61
FT /note="S -> W (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 122 AA; 14126 MW; 24D4D9A362CB399F CRC64;
NLLQFNRMIK LETKKNAVPF YAFYGCYCGW GGQGQPKDAT DRCCFEHDCC YGKLTKCNTK
SDLYSYSSKY GFLLCGKGTW CEEQICECDR IAATCLRRSL DTYKLKYMFY LDSYCKGPSE
KC
