ID   PA2H1_MICPY             Reviewed;          26 AA.
AC   P0CAS8;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   22-APR-2020, entry version 24.
DE   RecName: Full=Phospholipase A2 homolog A1;
DE            Short=svPLA2 homolog;
DE   Flags: Fragment;
OS   Micrurus pyrrhocryptus (Coral snake).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Elapinae; Micrurus.
OX   NCBI_TaxID=129468;
RN   [1]
RP   PROTEIN SEQUENCE, MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom;
RX   PubMed=19135468; DOI=10.1016/j.toxicon.2008.12.015;
RA   Dokmetjian J.C., Del Canto S., Vinzon S., de Jimenez Bonino M.B.;
RT   "Biochemical characterization of the Micrurus pyrrhocryptus venom.";
RL   Toxicon 53:375-382(2009).
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19135468}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:19135468}.
CC   -!- PTM: Contains 7 disulfide bonds. {ECO:0000250}.
CC   -!- MASS SPECTROMETRY: Mass=13679; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:19135468};
CC   -!- SIMILARITY: Belongs to the phospholipase A2 family. Group I subfamily.
CC       {ECO:0000305}.
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DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004623; F:phospholipase A2 activity; IEA:InterPro.
DR   GO; GO:0050482; P:arachidonic acid secretion; IEA:InterPro.
DR   GO; GO:0006644; P:phospholipid metabolic process; IEA:InterPro.
DR   InterPro; IPR036444; PLipase_A2_dom_sf.
DR   SUPFAM; SSF48619; SSF48619; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Secreted.
FT   CHAIN           1..>26
FT                   /note="Phospholipase A2 homolog A1"
FT                   /id="PRO_0000376925"
FT   NON_TER         26
SQ   SEQUENCE   26 AA;  3209 MW;  EEA926A9A34AD9A8 CRC64;
     NFKQIIKMIQ CTNTRPWXNF LDYGCY