ID   PLIGB_ELAQU             Reviewed;         200 AA.
AC   Q9PWI3;
DT   19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 58.
DE   RecName: Full=Phospholipase A2 inhibitor gamma subunit B {ECO:0000303|PubMed:10377258};
DE            Short=gamma-PLI B {ECO:0000303|PubMed:10377258};
DE   Flags: Precursor;
OS   Elaphe quadrivirgata (Japanese four-lined ratsnake).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Colubridae; Colubrinae; Elaphe.
OX   NCBI_TaxID=86195;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 20-34, SUBCELLULAR
RP   LOCATION, AND SUBUNIT.
RC   TISSUE=Liver;
RX   PubMed=10377258; DOI=10.1042/bj3410165;
RA   Okumura K., Masui K., Inoue S., Ikeda K., Hayashi K.;
RT   "Purification, characterization and cDNA cloning of a phospholipase A2
RT   inhibitor from the serum of the non-venomous snake Elaphe quadrivirgata.";
RL   Biochem. J. 341:165-171(1999).
CC   -!- FUNCTION: Inhibits the enzymatic activity of phospholipase A2 (PA2).
CC   -!- SUBUNIT: Heterodimer of subunit A and subunit B.
CC       {ECO:0000269|PubMed:10377258}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10377258}.
CC       Note=Secreted in blood plasma. {ECO:0000269|PubMed:10377258}.
CC   -!- TISSUE SPECIFICITY: Expressed by the liver. Not expressed in esophagus,
CC       stomach, pancreas, spleen, gall bladder, small intestine, rectum,
CC       kidney, trachea, lung, testis and body fat.
CC       {ECO:0000269|PubMed:10377258}.
CC   -!- PTM: N-glycosylated. {ECO:0000269|PubMed:10377258}.
CC   -!- SIMILARITY: Belongs to the CNF-like-inhibitor family. {ECO:0000305}.
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DR   EMBL; AB021426; BAA83079.1; -; mRNA.
DR   AlphaFoldDB; Q9PWI3; -.
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   Pfam; PF00021; UPAR_LY6; 1.
DR   PIRSF; PIRSF002023; PLA2_inhib_alpha/gamma; 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:10377258"
FT   CHAIN           20..200
FT                   /note="Phospholipase A2 inhibitor gamma subunit B"
FT                   /evidence="ECO:0000305|PubMed:10377258"
FT                   /id="PRO_0000023001"
FT   CARBOHYD        31
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        22..46
FT                   /evidence="ECO:0000250|UniProtKB:Q7LZI2"
FT   DISULFID        25..32
FT                   /evidence="ECO:0000250|UniProtKB:Q7LZI2"
FT   DISULFID        39..67
FT                   /evidence="ECO:0000250|UniProtKB:Q7LZI2"
FT   DISULFID        73..94
FT                   /evidence="ECO:0000250|UniProtKB:Q7LZI2"
FT   DISULFID        95..100
FT                   /evidence="ECO:0000250|UniProtKB:Q7LZI2"
FT   DISULFID        120..145
FT                   /evidence="ECO:0000250|UniProtKB:Q7LZI2"
FT   DISULFID        138..165
FT                   /evidence="ECO:0000250|UniProtKB:Q7LZI2"
FT   DISULFID        171..191
FT                   /evidence="ECO:0000250|UniProtKB:Q7LZI2"
SQ   SEQUENCE   200 AA;  22170 MW;  DCB772411474F891 CRC64;
     MKFLLFCCLF GTFLATGMCI DCEHCVVWGQ NCTGWKETCG ENEDTCVTYQ TEVIRPPLSI
     TFTAKTCGTS DTCHLDYVEA NPHTELTLRA KRACCTGDEC QTLPPPVLEP QVNRPNGLQC
     PGCIGLTSTE CNEYLVSCQG SENQCLTIIL KKPDFSLSEM SFKGCASENL CLLFEKKFWR
     FLEASEVDVK CTPAVPQTSQ