ID   PA2HB_ATRNM             Reviewed;         121 AA.
AC   P82950;
DT   05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=Basic phospholipase A2 homolog;
DE            Short=svPLA2 homolog;
DE   AltName: Full=Myotoxin II;
OS   Atropoides nummifer (Jumping pit viper) (Porthidium nummifer).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Atropoides.
OX   NCBI_TaxID=44730;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, AND SUBUNIT.
RC   TISSUE=Venom;
RX   PubMed=12127577; DOI=10.1016/s1357-2725(02)00060-2;
RA   Angulo Y., Olamendi-Portugal T., Alape-Giron A., Possani L.D., Lomonte B.;
RT   "Structural characterization and phylogenetic relationships of myotoxin II
RT   from Atropoides (Bothrops) nummifer snake venom, a Lys49 phospholipase A(2)
RT   homologue.";
RL   Int. J. Biochem. Cell Biol. 34:1268-1278(2002).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.08 ANGSTROMS), AND DISULFIDE BONDS.
RX   PubMed=16682766; DOI=10.1107/s1744309106010700;
RA   Murakami M.T., Melo C.C., Angulo Y., Lomonte B., Arni R.K.;
RT   "Structure of myotoxin II, a catalytically inactive Lys49 phospholipase A2
RT   homologue from Atropoides nummifer venom.";
RL   Acta Crystallogr. F 62:423-426(2006).
CC   -!- FUNCTION: Snake venom phospholipase A2 homolog that lacks enzymatic
CC       activity, but has myotoxic and cytolytic activities.
CC       {ECO:0000269|PubMed:12127577}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12127577}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
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; 2AOZ; X-ray; 2.08 A; A=1-121.
DR   PDBsum; 2AOZ; -.
DR   AlphaFoldDB; P82950; -.
DR   SMR; P82950; -.
DR   EvolutionaryTrace; P82950; -.
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:0019835; P:cytolysis; IEA:UniProtKB-KW.
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; 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; PS00118; PA2_HIS; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytolysis; Direct protein sequencing; Disulfide bond;
KW   Myotoxin; Secreted; Toxin.
FT   CHAIN           1..121
FT                   /note="Basic phospholipase A2 homolog"
FT                   /id="PRO_0000161608"
FT   DISULFID        26..115
FT                   /evidence="ECO:0000269|PubMed:16682766"
FT   DISULFID        28..44
FT                   /evidence="ECO:0000269|PubMed:16682766"
FT   DISULFID        43..95
FT                   /evidence="ECO:0000269|PubMed:16682766"
FT   DISULFID        49..121
FT                   /evidence="ECO:0000269|PubMed:16682766"
FT   DISULFID        50..88
FT                   /evidence="ECO:0000269|PubMed:16682766"
FT   DISULFID        57..81
FT                   /evidence="ECO:0000269|PubMed:16682766"
FT   DISULFID        75..86
FT                   /evidence="ECO:0000269|PubMed:16682766"
FT   HELIX           2..13
FT                   /evidence="ECO:0007829|PDB:2AOZ"
FT   HELIX           17..21
FT                   /evidence="ECO:0007829|PDB:2AOZ"
FT   TURN            25..27
FT                   /evidence="ECO:0007829|PDB:2AOZ"
FT   STRAND          28..31
FT                   /evidence="ECO:0007829|PDB:2AOZ"
FT   HELIX           39..50
FT                   /evidence="ECO:0007829|PDB:2AOZ"
FT   HELIX           51..53
FT                   /evidence="ECO:0007829|PDB:2AOZ"
FT   TURN            59..61
FT                   /evidence="ECO:0007829|PDB:2AOZ"
FT   STRAND          66..68
FT                   /evidence="ECO:0007829|PDB:2AOZ"
FT   STRAND          73..75
FT                   /evidence="ECO:0007829|PDB:2AOZ"
FT   HELIX           80..98
FT                   /evidence="ECO:0007829|PDB:2AOZ"
FT   TURN            99..102
FT                   /evidence="ECO:0007829|PDB:2AOZ"
FT   TURN            105..107
FT                   /evidence="ECO:0007829|PDB:2AOZ"
FT   HELIX           112..114
FT                   /evidence="ECO:0007829|PDB:2AOZ"
SQ   SEQUENCE   121 AA;  13712 MW;  7063B3833AF7680D CRC64;
     NLYQLWKMIL QETGKNAAPS YGFYGCNCGV GSRGKPKDAT DRCCFVHKCC YKALTDCSPK
     TDSYSYSWKD KTIVCGKNNP CLKQECECDK AVAICLRDNL DTYNKNYKIY PKPLCKKADD
     C