ID   PLIGB_ELACL             Reviewed;         200 AA.
AC   C0STK9;
DT   02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   25-MAY-2022, entry version 26.
DE   RecName: Full=Phospholipase A2 inhibitor gamma subunit B {ECO:0000303|PubMed:19673083};
DE   AltName: Full=PLI-gamma B;
DE   AltName: Full=gamma-PLI B {ECO:0000303|PubMed:19673083};
DE   Flags: Precursor;
OS   Elaphe climacophora (Japanese rat snake) (Coluber climacophorus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Colubridae; Colubrinae; Elaphe.
OX   NCBI_TaxID=31143;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 20-24, SUBCELLULAR
RP   LOCATION, AND SUBUNIT.
RC   TISSUE=Liver, and Serum;
RX   PubMed=19673083; DOI=10.1016/j.toxicon.2009.02.001;
RA   Shirai R., Toriba M., Hayashi K., Ikeda K., Inoue S.;
RT   "Identification and characterization of phospholipase A2 inhibitors from
RT   the serum of the Japanese rat snake, Elaphe climacophora.";
RL   Toxicon 53:685-692(2009).
CC   -!- FUNCTION: Inhibits the enzymatic activity of the phospholipase A2
CC       (PLA2). {ECO:0000269|PubMed:19673083}.
CC   -!- SUBUNIT: Heteromer composed of subunit A and subunit B.
CC       {ECO:0000305|PubMed:19673083}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19673083}.
CC       Note=Secreted in blood plasma. {ECO:0000269|PubMed:19673083}.
CC   -!- MISCELLANEOUS: Concentration of this protein in the serum is 8-fold
CC       lower than in the E.quadrivirgata (another non-venomous snake) serum.
CC       This difference may reflect the difference in the food habits of these
CC       snakes. E.quadrivirgata preys upon snakes including the venomous
CC       snakes, whereas E.climacophora only preys upon small mammals and birds.
CC       {ECO:0000269|PubMed:19673083}.
CC   -!- SIMILARITY: Belongs to the CNF-like-inhibitor family. {ECO:0000305}.
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DR   EMBL; AB462513; BAH47551.1; -; mRNA.
DR   AlphaFoldDB; C0STK9; -.
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; Phospholipase A2 inhibitor;
KW   Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..200
FT                   /note="Phospholipase A2 inhibitor gamma subunit B"
FT                   /id="PRO_5002901919"
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        120..145
FT                   /evidence="ECO:0000250|UniProtKB:Q7LZI1"
FT   DISULFID        138..165
FT                   /evidence="ECO:0000250|UniProtKB:Q7LZI1"
FT   DISULFID        171..191
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   200 AA;  22183 MW;  7CB768411FB3F527 CRC64;
     MKFLLFCCLF GTFLATGMCI DCEHCVVWGQ NCTGWKETCG ENEDTCVTYQ TEVIRPPLSI
     TFTAKTCGTS DTCHLDYVEA NPHNELTLRA KRACCTGDEC QTLPPPVLEP QVNRPNGLQC
     PGCIGLTSTE CNEYLVSCQG SENQCLTIIL KKPDFSLSEM SFKGCASENL CLLFEKKFWR
     FLEASEVDVK CTPAVPQTSQ