ID   PLIG2_LACMU             Reviewed;         200 AA.
AC   P60592;
DT   15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2004, sequence version 1.
DT   25-MAY-2022, entry version 52.
DE   RecName: Full=Phospholipase A2 inhibitor LNF2 {ECO:0000303|PubMed:12782092};
DE   AltName: Full=Lachesis neutralizing factor 2 {ECO:0000305};
DE   AltName: Full=gamma-PLI;
DE   Flags: Precursor;
OS   Lachesis muta muta (Bushmaster).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Lachesis.
OX   NCBI_TaxID=8753;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   PubMed=12782092; DOI=10.1016/s0041-0101(03)00073-4;
RA   Fortes-Dias C.L., Barcellos C.J., Estevao-Costa M.I.;
RT   "Molecular cloning of a gamma-phospholipase A2 inhibitor from Lachesis muta
RT   muta (the bushmaster snake).";
RL   Toxicon 41:909-917(2003).
CC   -!- FUNCTION: Inhibits the enzymatic activity of phospholipase A2 (PA2).
CC   -!- SUBUNIT: Occurs as a mixture of oligomers. Tetrameric arrangement
CC       appears to be the predominant quaternary structure.
CC       {ECO:0000250|UniProtKB:Q90358}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:12782092}.
CC       Note=Secreted in blood plasma. {ECO:0000305|PubMed:12782092}.
CC   -!- TISSUE SPECIFICITY: Expressed by the liver.
CC       {ECO:0000305|PubMed:12782092}.
CC   -!- SIMILARITY: Belongs to the CNF-like-inhibitor family. {ECO:0000305}.
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DR   EMBL; AY425346; AAR04437.1; -; mRNA.
DR   AlphaFoldDB; P60592; -.
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; -; 1.
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   PIRSF; PIRSF002023; PLA2_inhib_alpha/gamma; 1.
DR   SMART; SM00134; LU; 1.
DR   SUPFAM; SSF57302; SSF57302; 2.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Phospholipase A2 inhibitor; Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..200
FT                   /note="Phospholipase A2 inhibitor LNF2"
FT                   /evidence="ECO:0000305|PubMed:12782092"
FT                   /id="PRO_0000023003"
FT   CARBOHYD        176
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
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   200 AA;  22207 MW;  101EAB9F980DF8E3 CRC64;
     MKSLHTICLL FIFVARGNSR SCDFCHNIGK DCDGYEQECS SPEDVCGKVF LEISSASLSV
     RTVHKNCFSS SICKLGQIDV NIGHHSYIRG RVNCCEKEPC EDQPFPGLPL SRPNGYYCPG
     ALGLFTEDST EYEAICHGTE TKCINIVGHR YENFPGDITY NLKGCVSSCP LLSLSNATRE
     ENRNYLQKVE CKDAIRLASL