PA2HB_BOTAL
ID PA2HB_BOTAL Reviewed; 121 AA.
AC P86453;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 1.
DT 25-MAY-2022, entry version 36.
DE RecName: Full=Basic phospholipase A2 homolog BaTX {ECO:0000303|PubMed:17270350, ECO:0000303|PubMed:19463969};
DE Short=svPLA2 homolog;
OS Bothrops alternatus (Urutu) (Rhinocerophis alternatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX NCBI_TaxID=64174;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, MASS SPECTROMETRY, AND
RP TOXIC DOSE.
RC TISSUE=Venom;
RX PubMed=17270350; DOI=10.1016/j.bbagen.2006.11.015;
RA Ponce-Soto L.A., Lomonte B., Gutierrez J.M., Rodrigues-Simioni L.,
RA Novello J.C., Marangoni S.;
RT "Structural and functional properties of BaTX, a new Lys49 phospholipase A2
RT homologue isolated from the venom of the snake Bothrops alternatus.";
RL Biochim. Biophys. Acta 1770:585-593(2007).
RN [2]
RP FUNCTION.
RC TISSUE=Venom;
RX PubMed=17915277; DOI=10.1016/j.toxicon.2007.08.007;
RA Gutierrez J.M., Ponce-Soto L.A., Marangoni S., Lomonte B.;
RT "Systemic and local myotoxicity induced by snake venom group II
RT phospholipases A2: comparison between crotoxin, crotoxin B and a Lys49 PLA2
RT homologue.";
RL Toxicon 51:80-92(2008).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=19463969; DOI=10.1016/j.cbpc.2009.05.007;
RA Ponce-Soto L.A., Barros J.C., Marangoni S., Hernandez S., Dal Belo C.A.,
RA Corrado A.P., Hyslop S., Rodrigues-Simioni L.;
RT "Neuromuscular activity of BaTX, a presynaptic basic PLA2 isolated from
RT Bothrops alternatus snake venom.";
RL Comp. Biochem. Physiol. 150:291-297(2009).
CC -!- FUNCTION: Snake venom phospholipase A2 homolog that lacks enzymatic
CC activity (PubMed:17270350). Is myotoxic and displays edema-inducing
CC activities (PubMed:17270350, PubMed:17915277). In vitro, produced time-
CC dependent, irreversible neuromuscular blockade in isolated mouse
CC phrenic nerve-diaphragm and chick biventer cervicis preparations
CC (PubMed:17270350, PubMed:19463969). A model of myotoxic mechanism has
CC been proposed: an apo Lys49-PLA2 is activated by the entrance of a
CC hydrophobic molecule (e.g. fatty acid) at the hydrophobic channel of
CC the protein leading to a reorientation of a monomer (By similarity).
CC This reorientation causes a transition between 'inactive' to 'active'
CC states, causing alignment of C-terminal and membrane-docking sites
CC (MDoS) side-by-side and putting the membrane-disruption sites (MDiS) in
CC the same plane, exposed to solvent and in a symmetric position for both
CC monomers (By similarity). The MDoS region stabilizes the toxin on
CC membrane by the interaction of charged residues with phospholipid head
CC groups (By similarity). Subsequently, the MDiS region destabilizes the
CC membrane with penetration of hydrophobic residues (By similarity). This
CC insertion causes a disorganization of the membrane, allowing an
CC uncontrolled influx of ions (i.e. calcium and sodium), and eventually
CC triggering irreversible intracellular alterations and cell death (By
CC similarity). {ECO:0000250|UniProtKB:I6L8L6,
CC ECO:0000269|PubMed:17270350, ECO:0000269|PubMed:17915277,
CC ECO:0000269|PubMed:19463969}.
CC -!- SUBUNIT: Homodimer; non-covalently linked.
CC {ECO:0000250|UniProtKB:P24605}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17270350,
CC ECO:0000269|PubMed:19463969}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:17270350, ECO:0000305|PubMed:19463969}.
CC -!- MASS SPECTROMETRY: Mass=13898.71; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:17270350};
CC -!- TOXIC DOSE: LD(50) is 7 mg/kg by intravenous injection into mice.
CC {ECO:0000269|PubMed:17270350}.
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC K49 sub-subfamily. {ECO:0000305}.
CC -!- CAUTION: Does not bind calcium as one of the calcium-binding sites is
CC lost (Asp->Lys in position 48, which corresponds to 'Lys-49' in the
CC current nomenclature). {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 AlphaFoldDB; P86453; -.
DR SMR; P86453; -.
DR BRENDA; 3.1.1.4; 6825.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0090729; F:toxin activity; IDA:UniProtKB.
DR GO; GO:0050482; P:arachidonic acid secretion; IEA:InterPro.
DR GO; GO:0044649; P:envenomation resulting in cytolysis in another organism; IDA:UniProtKB.
DR GO; GO:0044398; P:envenomation resulting in induction of edema in another organism; IDA:UniProtKB.
DR GO; GO:0044534; P:envenomation resulting in modulation of apoptotic process in another organism; IDA:UniProtKB.
DR GO; GO:0044521; P:envenomation resulting in muscle damage in another organism; IDA:UniProtKB.
DR GO; GO:0016042; P:lipid catabolic process; IEA:InterPro.
DR GO; GO:0045932; P:negative regulation of muscle contraction; IDA:UniProtKB.
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 Direct protein sequencing; Disulfide bond; Myotoxin; Neurotoxin;
KW Presynaptic neurotoxin; Secreted; Toxin.
FT CHAIN 1..121
FT /note="Basic phospholipase A2 homolog BaTX"
FT /id="PRO_0000392638"
FT REGION 105..117
FT /note="Important for membrane-damaging activities in
FT eukaryotes and bacteria; heparin-binding"
FT /evidence="ECO:0000250|UniProtKB:P24605"
FT SITE 105
FT /note="Important residue of the cationic membrane-docking
FT site (MDoS)"
FT /evidence="ECO:0000250|UniProtKB:I6L8L6"
FT SITE 108
FT /note="Important residue of the cationic membrane-docking
FT site (MDoS)"
FT /evidence="ECO:0000250|UniProtKB:I6L8L6"
FT SITE 111
FT /note="Hydrophobic membrane-disruption site (MDiS)"
FT /evidence="ECO:0000250|UniProtKB:I6L8L6"
FT SITE 112
FT /note="Cationic membrane-docking site (MDoS)"
FT /evidence="ECO:0000250|UniProtKB:I6L8L6"
FT SITE 114
FT /note="Hydrophobic membrane-disruption site (MDiS)"
FT /evidence="ECO:0000250|UniProtKB:I6L8L6"
FT SITE 117
FT /note="Cationic membrane-docking site (MDoS)"
FT /evidence="ECO:0000250|UniProtKB:I6L8L6"
FT DISULFID 26..115
FT /evidence="ECO:0000250|UniProtKB:Q90249"
FT DISULFID 28..44
FT /evidence="ECO:0000250|UniProtKB:Q90249"
FT DISULFID 43..95
FT /evidence="ECO:0000250|UniProtKB:Q90249"
FT DISULFID 49..121
FT /evidence="ECO:0000250|UniProtKB:Q90249"
FT DISULFID 50..88
FT /evidence="ECO:0000250|UniProtKB:Q90249"
FT DISULFID 57..81
FT /evidence="ECO:0000250|UniProtKB:Q90249"
FT DISULFID 75..86
FT /evidence="ECO:0000250|UniProtKB:Q90249"
SQ SEQUENCE 121 AA; 13897 MW; 98C146E1FFA9E6A4 CRC64;
SLFELGKMIL QETGKNPAKS YGAYYCYCGW GGQGQPKDAT DRCCYVHKCC YKKLTGCNPK
KDRYSYSWKD KTIVCGENNS CLKELCECDK AVAICLRENL NTYNKKYRYY LKPLCKKADA
C
