PA2HB_BOTLC
ID PA2HB_BOTLC Reviewed; 121 AA.
AC P86975;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 1.
DT 25-MAY-2022, entry version 24.
DE RecName: Full=Basic phospholipase A2 homolog blK-PLA2 {ECO:0000303|PubMed:17110015};
DE Short=svPLA2 homolog;
OS Bothrops leucurus (Whitetail lancehead).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX NCBI_TaxID=157295;
RN [1]
RP PROTEIN SEQUENCE, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RA Sanchez E.F.;
RL Submitted (JUN-2011) to UniProtKB.
RN [2]
RP PROTEIN SEQUENCE OF 1-48, FUNCTION, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=17110015; DOI=10.1016/j.biochi.2006.10.010;
RA Higuchi D.A., Barbosa C.M., Bincoletto C., Chagas J.R., Magalhaes A.,
RA Richardson M., Sanchez E.F., Pesquero J.B., Araujo R.C., Pesquero J.L.;
RT "Purification and partial characterization of two phospholipases A2 from
RT Bothrops leucurus (white-tailed-jararaca) snake venom.";
RL Biochimie 89:319-328(2007).
CC -!- FUNCTION: Snake venom phospholipase A2 (PLA2) homolog that lacks
CC enzymatic activity (By similarity). Shows myotoxic and edema-inducing
CC activities in vivo (By similarity). 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:0000250|UniProtKB:P82287}.
CC -!- SUBUNIT: Homodimer; non-covalently linked.
CC {ECO:0000250|UniProtKB:Q90249}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17110015,
CC ECO:0000269|Ref.1}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:17110015, ECO:0000305|Ref.1}.
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; P86975; -.
DR SMR; P86975; -.
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:InterPro.
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 Direct protein sequencing; Disulfide bond; Myotoxin; Secreted; Toxin.
FT CHAIN 1..121
FT /note="Basic phospholipase A2 homolog blK-PLA2"
FT /id="PRO_0000413007"
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; 13717 MW; E2025E6594E41713 CRC64;
SLFELGKMIL QETGKNSVKS YGVYGCNCGV GGRGKPKDAT DRCCYVHKCC YKKLTGCDPK
KDRYSYSWKD KTIVCGENNP CLKELCECDK AVAICLRENL GTYNKKYRYH LKPFCKKADP
C
