PA2H2_CERGO
ID PA2H2_CERGO Reviewed; 121 AA.
AC P81165;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 1.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=Basic phospholipase A2 homolog GodMT-II {ECO:0000303|PubMed:9659381};
DE Short=svPLA2 homolog;
DE AltName: Full=Myotoxin II {ECO:0000303|PubMed:9659381};
OS Cerrophidion godmani (Porthidium godmani) (Bothrops godmani).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Cerrophidion.
OX NCBI_TaxID=44722;
RN [1]
RP PROTEIN SEQUENCE, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=9659381; DOI=10.1016/s0167-4838(98)00023-5;
RA de Sousa M.V., Morhy L., Arni R.K., Ward R.J., Diaz C., Gutierrez J.M.;
RT "Amino acid sequence of a myotoxic Lys49-phospholipase A2 homologue from
RT the venom of Cerrophidion (Bothrops) godmani.";
RL Biochim. Biophys. Acta 1384:204-208(1998).
RN [2]
RP SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=10698689; DOI=10.1042/bj3460631;
RA Lizano S., Angulo Y., Lomonte B., Fox J.W., Lambeau G., Lazdunski M.,
RA Gutierrez J.M.;
RT "Two phospholipase A2 inhibitors from the plasma of Cerrophidion (Bothrops)
RT godmani which selectively inhibit two different group-II phospholipase A2
RT myotoxins from its own venom: isolation, molecular cloning and biological
RT properties.";
RL Biochem. J. 346:631-639(2000).
RN [3]
RP AMINO-ACID COMPOSITION, FUNCTION, AND TOXIC DOSE.
RC TISSUE=Venom;
RX PubMed=1524423; DOI=10.1016/0003-9861(92)90104-5;
RA Diaz C., Gutierrez J.M., Lomonte B.;
RT "Isolation and characterization of basic myotoxic phospholipases A2 from
RT Bothrops godmani (Godman's pit viper) snake venom.";
RL Arch. Biochem. Biophys. 298:135-142(1992).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 1-111, DISULFIDE BONDS, AND
RP SUBUNIT.
RC TISSUE=Venom;
RX PubMed=10356281; DOI=10.1006/abbi.1999.1210;
RA Arni R.K., Fontes M.R.M., Barberato C., Gutierrez J.M., Diaz C., Ward R.J.;
RT "Crystal structure of myotoxin II, a monomeric Lys49-phospholipase A2
RT homologue isolated from the venom of Cerrophidion (Bothrops) godmani.";
RL Arch. Biochem. Biophys. 366:177-182(1999).
CC -!- FUNCTION: Snake venom phospholipase A2 homolog that lacks enzymatic
CC activity but shows high myotoxic activities (PubMed:1524423). In vivo,
CC induces a mild edema when subcutaneously injected into mice foot pad
CC (PubMed:1524423). {ECO:0000269|PubMed:1524423}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:10356281}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10698689,
CC ECO:0000269|PubMed:9659381}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:10698689, ECO:0000305|PubMed:9659381}.
CC -!- TOXIC DOSE: LD(50) is 4.2 ug/g by intravenous injection into mice.
CC {ECO:0000269|PubMed:1524423}.
CC -!- MISCELLANEOUS: Is not inhibited by the gamma-phospholipase A2 inhibitor
CC (PLI) CgMIP-I (AC P0DQP7) and by the alpha-PLI CgMIP-II (AC P0DQP8).
CC {ECO:0000269|PubMed:10698689}.
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}.
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DR PDB; 1GOD; X-ray; 2.80 A; A=1-111.
DR PDBsum; 1GOD; -.
DR AlphaFoldDB; P81165; -.
DR SMR; P81165; -.
DR EvolutionaryTrace; P81165; -.
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 GodMT-II"
FT /evidence="ECO:0000269|PubMed:9659381"
FT /id="PRO_0000161640"
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 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:0000269|PubMed:10356281,
FT ECO:0007744|PDB:1GOD"
FT DISULFID 28..44
FT /evidence="ECO:0000269|PubMed:10356281,
FT ECO:0007744|PDB:1GOD"
FT DISULFID 43..95
FT /evidence="ECO:0000269|PubMed:10356281,
FT ECO:0007744|PDB:1GOD"
FT DISULFID 49..121
FT /evidence="ECO:0000269|PubMed:10356281,
FT ECO:0007744|PDB:1GOD"
FT DISULFID 50..88
FT /evidence="ECO:0000269|PubMed:10356281,
FT ECO:0007744|PDB:1GOD"
FT DISULFID 57..81
FT /evidence="ECO:0000269|PubMed:10356281,
FT ECO:0007744|PDB:1GOD"
FT DISULFID 75..86
FT /evidence="ECO:0000269|PubMed:10356281,
FT ECO:0007744|PDB:1GOD"
FT HELIX 2..13
FT /evidence="ECO:0007829|PDB:1GOD"
FT HELIX 17..20
FT /evidence="ECO:0007829|PDB:1GOD"
FT TURN 21..23
FT /evidence="ECO:0007829|PDB:1GOD"
FT TURN 25..28
FT /evidence="ECO:0007829|PDB:1GOD"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:1GOD"
FT HELIX 39..51
FT /evidence="ECO:0007829|PDB:1GOD"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:1GOD"
FT TURN 59..61
FT /evidence="ECO:0007829|PDB:1GOD"
FT STRAND 67..71
FT /evidence="ECO:0007829|PDB:1GOD"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:1GOD"
FT HELIX 81..98
FT /evidence="ECO:0007829|PDB:1GOD"
FT HELIX 100..102
FT /evidence="ECO:0007829|PDB:1GOD"
FT TURN 105..109
FT /evidence="ECO:0007829|PDB:1GOD"
SQ SEQUENCE 121 AA; 13714 MW; A05E7209F3DF61CF CRC64;
SMYQLWKMIL QETGKNAVPS YGLYGCNCGV GSRGKPKDAT DRCCFVHKCC YKKLTDCSPK
TDSYSYSWKD KTIVCGDNNP CLQEMCECDK AVAICLRENL DTYNKNYKIY PKPLCKKADA
C
