PA2H_PROMB
ID PA2H_PROMB Reviewed; 121 AA.
AC P84776;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 25-MAY-2022, entry version 63.
DE RecName: Full=Basic phospholipase A2 homolog zhaoermiatoxin;
DE Short=svPLA2 homolog;
OS Protobothrops mangshanensis (Mangshan pitviper) (Zhaoermia mangshanensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Protobothrops.
OX NCBI_TaxID=242058;
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND MASS SPECTROMETRY.
RC TISSUE=Venom {ECO:0000269|PubMed:16635500};
RX PubMed=16635500; DOI=10.1016/j.toxicon.2006.01.031;
RA Mebs D., Kuch U., Coronas F.I.V., Batista C.V.F., Gumprecht A.,
RA Possani L.D.;
RT "Biochemical and biological activities of the venom of the Chinese pitviper
RT Zhaoermia mangshanensis, with the complete amino acid sequence and
RT phylogenetic analysis of a novel Arg49 phospholipase A2 myotoxin.";
RL Toxicon 47:797-811(2006).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS), AND DISULFIDE BONDS.
RC TISSUE=Venom;
RX PubMed=18295812; DOI=10.1016/j.toxicon.2007.11.018;
RA Murakami M.T., Kuch U., Betzel C., Mebs D., Arni R.K.;
RT "Crystal structure of a novel myotoxic Arg49 phospholipase A2 homolog
RT (zhaoermiatoxin) from Zhaoermia mangshanensis snake venom: insights into
RT Arg49 coordination and the role of Lys122 in the polarization of the C-
RT terminus.";
RL Toxicon 51:723-735(2008).
CC -!- FUNCTION: Snake venom phospholipase A2 homolog that induces
CC myonecrosis, and edema. Has low myotoxic activity.
CC {ECO:0000269|PubMed:16635500}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16635500}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16635500}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000269|PubMed:16635500}.
CC -!- MASS SPECTROMETRY: Mass=13972.0; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:16635500};
CC -!- TOXIC DOSE: LD(50) is in the range of 6.25-12.5 mg/kg by
CC intraperitoneal injection into mice. {ECO:0000269|PubMed:16635500}.
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC R49 sub-subfamily. {ECO:0000305}.
CC -!- CAUTION: Does not bind calcium as one of the calcium-binding sites is
CC lost (Asp->Arg in position 48, which corresponds to 'Arg-49' in the
CC current nomenclature). {ECO:0000305}.
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DR PDB; 2PH4; X-ray; 2.05 A; A/B=1-121.
DR PDBsum; 2PH4; -.
DR AlphaFoldDB; P84776; -.
DR SMR; P84776; -.
DR PRIDE; P84776; -.
DR BRENDA; 3.1.1.4; 9394.
DR EvolutionaryTrace; P84776; -.
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 3D-structure; Direct protein sequencing; Disulfide bond; Myotoxin;
KW Secreted; Toxin.
FT CHAIN 1..121
FT /note="Basic phospholipase A2 homolog zhaoermiatoxin"
FT /id="PRO_0000250615"
FT DISULFID 26..115
FT /evidence="ECO:0000269|PubMed:18295812"
FT DISULFID 28..44
FT /evidence="ECO:0000269|PubMed:18295812"
FT DISULFID 43..95
FT /evidence="ECO:0000269|PubMed:18295812"
FT DISULFID 49..121
FT /evidence="ECO:0000269|PubMed:18295812"
FT DISULFID 50..88
FT /evidence="ECO:0000269|PubMed:18295812"
FT DISULFID 57..81
FT /evidence="ECO:0000269|PubMed:18295812"
FT DISULFID 75..86
FT /evidence="ECO:0000269|PubMed:18295812"
FT HELIX 2..13
FT /evidence="ECO:0007829|PDB:2PH4"
FT HELIX 17..21
FT /evidence="ECO:0007829|PDB:2PH4"
FT STRAND 22..24
FT /evidence="ECO:0007829|PDB:2PH4"
FT TURN 25..27
FT /evidence="ECO:0007829|PDB:2PH4"
FT HELIX 39..53
FT /evidence="ECO:0007829|PDB:2PH4"
FT TURN 59..61
FT /evidence="ECO:0007829|PDB:2PH4"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:2PH4"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:2PH4"
FT HELIX 80..99
FT /evidence="ECO:0007829|PDB:2PH4"
FT HELIX 100..102
FT /evidence="ECO:0007829|PDB:2PH4"
FT HELIX 105..108
FT /evidence="ECO:0007829|PDB:2PH4"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:2PH4"
SQ SEQUENCE 121 AA; 13985 MW; B9A6B68089F5B681 CRC64;
SLIELTKMVF QETGKNPVTY YTLYGCNCGV GRRGKPKDAT DRCCFVHRCC YKKLTGCDPK
KDRYSYSWEN KAIVCGEKNP CLKELCECDK AVAICLRKNL GTYDKNYRFT MKFLCDKPEK
C
