ID   PLIG1_PROFL             Reviewed;         200 AA.
AC   O57690;
DT   28-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   25-MAY-2022, entry version 70.
DE   RecName: Full=Phospholipase A2 inhibitor 1;
DE   AltName: Full=Phospholipase A2 inhibitor I;
DE            Short=PLI-I;
DE   AltName: Full=gamma-PLI;
DE   Flags: Precursor;
OS   Protobothrops flavoviridis (Habu) (Trimeresurus flavoviridis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Protobothrops.
OX   NCBI_TaxID=88087;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], PROTEIN SEQUENCE OF 20-47;
RP   49-121; 126-160 AND 164-200, GLYCOSYLATION, AND SUBCELLULAR LOCATION.
RC   TISSUE=Liver;
RX   PubMed=9395334; DOI=10.1111/j.1432-1033.1997.00838.x;
RA   Nobuhisa I., Inamasu S., Nakai M., Tatsui A., Mimori T., Ogawa T.,
RA   Shimohigashi Y., Fukumaki Y., Hattori S., Kihara H., Ohno M.;
RT   "Characterization and evolution of a gene encoding a Trimeresurus
RT   flavoviridis serum protein that inhibits basic phospholipase A2 isozymes in
RT   the snake's venom.";
RL   Eur. J. Biochem. 249:838-845(1997).
CC   -!- FUNCTION: Inhibits basic phospholipase A2 isozymes PLA-B, BP-I and BP-
CC       II.
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:0000269|PubMed:9395334}.
CC       Note=Secreted in blood plasma. {ECO:0000269|PubMed:9395334}.
CC   -!- TISSUE SPECIFICITY: Expressed by the liver.
CC       {ECO:0000305|PubMed:9395334}.
CC   -!- PTM: N-glycosylated. {ECO:0000269|PubMed:9395334}.
CC   -!- SIMILARITY: Belongs to the CNF-like-inhibitor family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AB003473; BAA24503.1; -; Genomic_DNA.
DR   EMBL; AB003472; BAA24502.1; -; mRNA.
DR   AlphaFoldDB; O57690; -.
DR   iPTMnet; O57690; -.
DR   PRIDE; O57690; -.
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; 1.
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:9395334"
FT   CHAIN           20..200
FT                   /note="Phospholipase A2 inhibitor 1"
FT                   /evidence="ECO:0000305|PubMed:9395334"
FT                   /id="PRO_0000023004"
FT   CARBOHYD        176
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000305|PubMed:9395334"
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;  22395 MW;  3EF087525C48516E CRC64;
     MKSLHIICLL FIFVARGNSR SCDFCHNIGA DCEGFQHECS SPEDECGKVF LEISSASLSV
     RTVHKNCFSS SVCKLRHFDV NIGHDSYIRG RINCCEKEPC EDQSFPGLPL SQPNGYYCPG
     SLGLFTKDST EFEAICKGTE TKCINIVGHR YEHYPGDIAY NLKGCISSCP LLSLSNATHE
     ENRNYLEKVE CKDALQFEKQ