PA2H_GLOUS
ID PA2H_GLOUS Reviewed; 122 AA.
AC P0DKU1;
DT 06-FEB-2013, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2013, sequence version 1.
DT 25-MAY-2022, entry version 22.
DE RecName: Full=Basic phospholipase A2 homolog Gln49-PLA2;
DE Short=svPLA2 homolog;
OS Gloydius ussuriensis (Ussuri mamushi) (Gloydius blomhoffii ussuriensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Gloydius.
OX NCBI_TaxID=35671;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 1-21, FUNCTION, BIOASSAY,
RP MASS SPECTROMETRY, AND TOXIC DOSE.
RC TISSUE=Venom, and Venom gland;
RX PubMed=15618013; DOI=10.1016/j.biocel.2004.05.022;
RA Bao Y., Bu P., Jin L., Hongxia W., Yang Q., An L.;
RT "Purification, characterization and gene cloning of a novel phospholipase
RT A2 from the venom of Agkistrodon blomhoffii ussurensis.";
RL Int. J. Biochem. Cell Biol. 37:558-565(2005).
RN [2]
RP FUNCTION AS A NEUROTOXIN, AND TOXIC DOSE.
RX PubMed=17299814; DOI=10.1002/jat.1222;
RA Chang Y., Li Y., Bao Y., An L.;
RT "Neurotoxic activity of Gln49 phospholipase A(2) from Gloydius ussuriensis
RT snake venom.";
RL J. Appl. Toxicol. 27:447-452(2007).
RN [3]
RP FUNCTION.
RX PubMed=19277489; DOI=10.1007/s12010-009-8573-4;
RA Zhang Y., Jiang B., Li W., Zhou C., Ji F., Xie Q., Sun X., An L., Bao Y.;
RT "Mechanisms of analgesic action of Gln49-PLA(2) from Gloydius ussurensis
RT snake venom.";
RL Appl. Biochem. Biotechnol. 160:773-779(2010).
CC -!- FUNCTION: Snake venom phospholipase A2 (PLA2) homolog that shows local
CC myotoxicity, apparent anticoagulant activity (PubMed:15618013), and
CC neurotoxicity (PubMed:17299814). Shows analgesic effect on mice due to
CC a decrease of action potentials and nerve conduction velocity. These
CC effects are caused by inhibition of voltage-gated ion channels
CC (potassium (Kv) and sodium (Nav)) (PubMed:19277489). In addition,
CC analgesic effects are antagonized by naloxone, implying the mechanism
CC of action is correlated with opioid receptors (probably indirectly)
CC (PubMed:17299814). Does not show detectable PLA2 activity on egg yolk
CC phospholipids (PubMed:15618013). {ECO:0000269|PubMed:15618013,
CC ECO:0000269|PubMed:17299814, ECO:0000269|PubMed:19277489}.
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- MASS SPECTROMETRY: Mass=13881.85; Mass_error=0.33; Method=Unknown;
CC Evidence={ECO:0000269|PubMed:15618013};
CC -!- TOXIC DOSE: LD(50) is 18.2 mg/kg by intraperitoneal injection into
CC mice. {ECO:0000269|PubMed:15618013, ECO:0000269|PubMed:17299814}.
CC -!- MISCELLANEOUS: Does not show hemorrhagic activities.
CC {ECO:0000305|PubMed:15618013}.
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC Q49 sub-subfamily. {ECO:0000305}.
CC -!- CAUTION: Does not bind calcium as one of the calcium-binding sites is
CC lost (Asp->Gln in position 48, which corresponds to 'Gln-49' in the
CC current nomenclature). {ECO:0000305}.
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DR AlphaFoldDB; P0DKU1; -.
DR SMR; P0DKU1; -.
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:0015459; F:potassium channel regulator activity; IEA:UniProtKB-KW.
DR GO; GO:0017080; F:sodium channel regulator activity; IEA:UniProtKB-KW.
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.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Hemostasis impairing toxin;
KW Ion channel impairing toxin; Myotoxin; Neurotoxin;
KW Potassium channel impairing toxin; Secreted; Toxin;
KW Voltage-gated potassium channel impairing toxin;
KW Voltage-gated sodium channel impairing toxin.
FT CHAIN 1..122
FT /note="Basic phospholipase A2 homolog Gln49-PLA2"
FT /id="PRO_0000420882"
FT DISULFID 26..115
FT /evidence="ECO:0000250"
FT DISULFID 28..44
FT /evidence="ECO:0000250"
FT DISULFID 43..95
FT /evidence="ECO:0000250"
FT DISULFID 49..122
FT /evidence="ECO:0000250"
FT DISULFID 50..88
FT /evidence="ECO:0000250"
FT DISULFID 57..81
FT /evidence="ECO:0000250"
FT DISULFID 75..86
FT /evidence="ECO:0000250"
SQ SEQUENCE 122 AA; 13896 MW; 8293B644F1ED1301 CRC64;
SLLQFRKMIK KMTGKEPVVS YAFYGCYCGS GGRGKPKDAT DRCCFVHQCC YEKVTGCDPK
WDDYTYSWKD GDIVCGGDDP CKKEVCECDR AAAICFRDNL KTYKKIYMAY PDIFCSSKSE
KC
