ID   PLIG_MALRE              Reviewed;         201 AA.
AC   Q9I8P7;
DT   02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=Phospholipase A2 inhibitor PIP {ECO:0000305};
DE   AltName: Full=Phospholipase inhibitor from python {ECO:0000303|PubMed:10924158};
DE            Short=PIP {ECO:0000303|PubMed:10924158};
DE   AltName: Full=gamma-PLI;
DE   Flags: Precursor;
OS   Malayopython reticulatus (Reticulate python) (Python reticulatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Henophidia; Pythonidae; Malayopython.
OX   NCBI_TaxID=1496311;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 20-37, RECOMBINANT
RP   EXPRESSION, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, MASS SPECTROMETRY, AND
RP   GLYCOSYLATION.
RC   TISSUE=Liver, and Serum;
RX   PubMed=10924158; DOI=10.1021/bi000395z;
RA   Thwin M.M., Gopalakrishnakone P., Kini R.M., Armugam A., Jeyaseelan K.;
RT   "Recombinant antitoxic and antiinflammatory factor from the nonvenomous
RT   snake Python reticulatus: phospholipase A2 inhibition and venom
RT   neutralizing potential.";
RL   Biochemistry 39:9604-9611(2000).
CC   -!- FUNCTION: Inhibits the enzymatic activity of phospholipase A2 (PA2)
CC       (PubMed:10924158). Binds to the major PLA2 toxin of D.russelli
CC       siamensis (Daboiatoxin, AC Q7T2R1, and AC Q7T3T5) at 1-2-fold molar
CC       excess of inhibitor to toxin (PubMed:10924158). It exhibits broad
CC       spectra in neutralizing the toxicity of various snake venoms and toxins
CC       and inhibits the formation of edema in mice (PubMed:10924158). May bind
CC       to PLA2 through its proline-rich hydrophobic core region (Probable).
CC       {ECO:0000269|PubMed:10924158, ECO:0000305|PubMed:10924158}.
CC   -!- SUBUNIT: Homohexamer. {ECO:0000269|PubMed:10924158}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10924158}.
CC       Note=Secreted in blood plasma. {ECO:0000269|PubMed:10924158}.
CC   -!- TISSUE SPECIFICITY: Expressed by the liver.
CC       {ECO:0000305|PubMed:10924158}.
CC   -!- PTM: Glycosylated. {ECO:0000269|PubMed:10924158}.
CC   -!- MASS SPECTROMETRY: Mass=23264; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:10924158};
CC   -!- SIMILARITY: Belongs to the CNF-like-inhibitor family. {ECO:0000305}.
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DR   EMBL; AF232771; AAF73945.1; -; mRNA.
DR   AlphaFoldDB; Q9I8P7; -.
DR   PRIDE; Q9I8P7; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0019834; F:phospholipase A2 inhibitor activity; IEA:UniProtKB-KW.
DR   GO; GO:0032429; P:regulation of phospholipase A2 activity; IEA:InterPro.
DR   Gene3D; 2.10.60.10; -; 2.
DR   InterPro; IPR016054; LY6_UPA_recep-like.
DR   InterPro; IPR016338; PLipase_A2-inh_a/b-type.
DR   InterPro; IPR004126; PLipase_A2_inh.
DR   InterPro; IPR045860; Snake_toxin-like_sf.
DR   Pfam; PF02988; PLA2_inh; 1.
DR   Pfam; PF00021; UPAR_LY6; 1.
DR   PIRSF; PIRSF002023; PLA2_inhib_alpha/gamma; 1.
DR   SMART; SM00134; LU; 1.
DR   SUPFAM; SSF57302; SSF57302; 2.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein;
KW   Phospholipase A2 inhibitor; Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000269|PubMed:10924158"
FT   CHAIN           20..201
FT                   /note="Phospholipase A2 inhibitor PIP"
FT                   /evidence="ECO:0000305|PubMed:10924158"
FT                   /id="PRO_5004327205"
FT   CARBOHYD        157
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        22..46
FT                   /evidence="ECO:0000250|UniProtKB:Q7LZI1"
FT   DISULFID        25..32
FT                   /evidence="ECO:0000250|UniProtKB:Q7LZI1"
FT   DISULFID        39..67
FT                   /evidence="ECO:0000250|UniProtKB:Q7LZI1"
FT   DISULFID        73..94
FT                   /evidence="ECO:0000250|UniProtKB:Q7LZI1"
FT   DISULFID        95..100
FT                   /evidence="ECO:0000250|UniProtKB:Q7LZI1"
FT   DISULFID        118..143
FT                   /evidence="ECO:0000250|UniProtKB:Q7LZI1"
FT   DISULFID        136..165
FT                   /evidence="ECO:0000250|UniProtKB:Q7LZI1"
FT   DISULFID        169..191
FT                   /evidence="ECO:0000250|UniProtKB:Q7LZI1"
SQ   SEQUENCE   201 AA;  22218 MW;  BBB8ACBE51AB3099 CRC64;
     MKSLQTICLL FIFIARGTSD KCEICHGFGD DCDGYQEECP SPEDRCGKIL IDIALAPVSF
     RATHKNCFSS SICKLGRVDI HVWDGVYIRG RTNCCDNDQC EDQPLPGLPL SLQNGLYCPG
     AFGIFTEDST EHEVKCRGTE TMCLDLVGYR QESYAGNITY NIKGCVSSCP LVTLSERGHE
     GRKNDLKKVE CREALKPASS D