ID   PA2H1_NOTSC             Reviewed;         119 AA.
AC   P00607;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=Basic phospholipase A2 homolog 1;
DE            Short=svPLA2 homolog;
DE   AltName: Full=Notechis II-1;
OS   Notechis scutatus scutatus (Mainland tiger snake) (Common tiger snake).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Acanthophiinae; Notechis.
OX   NCBI_TaxID=70142;
RN   [1]
RP   PROTEIN SEQUENCE, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom;
RX   PubMed=7007039; DOI=10.1111/j.1432-1033.1980.tb04954.x;
RA   Lind P., Eaker D.;
RT   "Complete amino-acid sequence of a non-neurotoxic, non-enzymatic
RT   phospholipase A2 homolog from the venom of the Australian tiger snake
RT   Notechis scutatus scutatus.";
RL   Eur. J. Biochem. 111:403-409(1980).
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:7007039}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:7007039}.
CC   -!- SIMILARITY: Belongs to the phospholipase A2 family. Group I subfamily.
CC       D49 sub-subfamily. {ECO:0000305}.
CC   -!- CAUTION: Lacks one of the four calcium-binding sites (Gly->Ser in
CC       position 30) found in other family members. {ECO:0000305}.
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DR   PIR; A00746; PSNOA1.
DR   AlphaFoldDB; P00607; -.
DR   SMR; P00607; -.
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: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; Secreted.
FT   CHAIN           1..119
FT                   /note="Basic phospholipase A2 homolog 1"
FT                   /evidence="ECO:0000269|PubMed:7007039"
FT                   /id="PRO_0000161674"
FT   REGION          107..117
FT                   /note="Important for membrane-damaging activities in
FT                   eukaryotes and bacteria; heparin-binding"
FT                   /evidence="ECO:0000250|UniProtKB:P24605"
FT   DISULFID        11..72
FT                   /evidence="ECO:0000250"
FT   DISULFID        27..118
FT                   /evidence="ECO:0000250|UniProtKB:P24605"
FT   DISULFID        29..45
FT                   /evidence="ECO:0000250|UniProtKB:P24605"
FT   DISULFID        44..99
FT                   /evidence="ECO:0000250|UniProtKB:P24605"
FT   DISULFID        51..92
FT                   /evidence="ECO:0000250|UniProtKB:P24605"
FT   DISULFID        61..85
FT                   /evidence="ECO:0000250|UniProtKB:P24605"
FT   DISULFID        79..90
FT                   /evidence="ECO:0000250|UniProtKB:P24605"
SQ   SEQUENCE   119 AA;  13323 MW;  23709A7F644B7509 CRC64;
     NLVQFSNMIQ CANHGSRPSL AYADYGCYCS AGGSGTPVDE LDRCCKTHDD CYARATKSYS
     CTPYWTLYSW QCIEKTPTCD SKTGCQRFVC DCDATAAKCF AKAPYNKENY NIDPKKRCQ