ID   PA2HA_BUNFA             Reviewed;         118 AA.
AC   P29601;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=Acidic phospholipase A2 homolog;
DE            Short=svPLA2 homolog;
OS   Bungarus fasciatus (Banded krait) (Pseudoboa fasciata).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Bungarinae; Bungarus.
OX   NCBI_TaxID=8613;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom;
RX   PubMed=1478931; DOI=10.1093/oxfordjournals.jbchem.a123962;
RA   Liu C.-S., Kuo P.-Y., Chen J.-M., Chen S.-W., Chang C.-H., Tseng C.-C.,
RA   Tseng M.-C., Lo T.-B.;
RT   "Primary structure of an inactive mutant of phospholipase A2 in the venom
RT   of Bungarus fasciatus (banded krait).";
RL   J. Biochem. 112:707-713(1992).
CC   -!- FUNCTION: Snake venom phospholipase A2 (PLA2) homolog that lacks both
CC       catalytic and neurotoxicity activities. {ECO:0000269|PubMed:1478931}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1478931}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:1478931}.
CC   -!- SIMILARITY: Belongs to the phospholipase A2 family. Group I subfamily.
CC       A49 sub-subfamily. {ECO:0000305}.
CC   -!- CAUTION: Does not bind calcium as three of the calcium-binding ligands
CC       are lost. {ECO:0000305}.
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DR   AlphaFoldDB; P29601; -.
DR   SMR; P29601; -.
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..118
FT                   /note="Acidic phospholipase A2 homolog"
FT                   /id="PRO_0000161639"
FT   DISULFID        11..70
FT                   /evidence="ECO:0000250"
FT   DISULFID        25..117
FT                   /evidence="ECO:0000250|UniProtKB:P24605"
FT   DISULFID        27..43
FT                   /evidence="ECO:0000250|UniProtKB:P24605"
FT   DISULFID        42..98
FT                   /evidence="ECO:0000250|UniProtKB:P24605"
FT   DISULFID        49..91
FT                   /evidence="ECO:0000250|UniProtKB:P24605"
FT   DISULFID        59..84
FT                   /evidence="ECO:0000250|UniProtKB:P24605"
FT   DISULFID        77..89
FT                   /evidence="ECO:0000250|UniProtKB:P24605"
SQ   SEQUENCE   118 AA;  13103 MW;  66C6AE44B0FFBC9A CRC64;
     NMVQFKSMVQ CTSTRPWLDY VDYGCNCDIG GTGTPLDELD RCCQTHANCY TEARKFPECA
     PYYKTYSYTC SGGTITCNAD NDECAASVCN CDRTAALCFA GAPYNQNNFD VDLETRCQ