ID   PLIGA_LATSE             Reviewed;         182 AA.
AC   P0DUK5;
DT   02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT   02-JUN-2021, sequence version 1.
DT   25-MAY-2022, entry version 4.
DE   RecName: Full=Phospholipase A2 inhibitor gamma subunit A {ECO:0000305};
DE   AltName: Full=LsPLI-gamma A {ECO:0000303|PubMed:9990137};
DE            Short=PLI-gamma A;
DE   AltName: Full=gamma-PLI A {ECO:0000303|PubMed:9990137};
OS   Laticauda semifasciata (Black-banded sea krait) (Pseudolaticauda
OS   semifasciata).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Laticaudinae; Laticauda.
OX   NCBI_TaxID=8631;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND
RP   GLYCOSYLATION AT ASN-157.
RC   TISSUE=Plasma;
RX   PubMed=9990137; DOI=10.1093/oxfordjournals.jbchem.a022297;
RA   Ohkura N., Kitahara Y., Inoue S., Ikeda K., Hayashi K.;
RT   "Isolation and amino acid sequence of a phospholipase A2 inhibitor from the
RT   blood plasma of the sea krait, Laticauda semifasciata.";
RL   J. Biochem. 125:375-382(1999).
CC   -!- FUNCTION: Strongly inhibits its own venom PLA2 and all other PLA2s
CC       tested including Elapid, Crotalid and Viperid venom PLA2s, as well as
CC       honeybee PLA2s. {ECO:0000269|PubMed:9990137}.
CC   -!- SUBUNIT: Heterotrimer of 2 subunits A and 1 subunit B.
CC       {ECO:0000269|PubMed:9990137}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9990137}.
CC       Note=Secreted in blood plasma. {ECO:0000269|PubMed:9990137}.
CC   -!- TISSUE SPECIFICITY: Expressed by the liver.
CC       {ECO:0000305|PubMed:9990137}.
CC   -!- PTM: N-glycosylation is not important for activity, since
CC       deglycosylation does not change its PLA2 inhibitory activity.
CC       {ECO:0000269|PubMed:9990137}.
CC   -!- SIMILARITY: Belongs to the CNF-like-inhibitor family. {ECO:0000305}.
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DR   AlphaFoldDB; P0DUK5; -.
DR   SMR; P0DUK5; -.
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.
FT   CHAIN           1..182
FT                   /note="Phospholipase A2 inhibitor gamma subunit A"
FT                   /evidence="ECO:0000269|PubMed:9990137"
FT                   /id="PRO_0000452703"
FT   CARBOHYD        157
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        3..27
FT                   /evidence="ECO:0000250|UniProtKB:Q7LZI1"
FT   DISULFID        6..13
FT                   /evidence="ECO:0000250|UniProtKB:Q7LZI1"
FT   DISULFID        20..48
FT                   /evidence="ECO:0000250|UniProtKB:Q7LZI1"
FT   DISULFID        54..75
FT                   /evidence="ECO:0000250|UniProtKB:Q7LZI1"
FT   DISULFID        76..81
FT                   /evidence="ECO:0000250|UniProtKB:Q7LZI1"
FT   DISULFID        99..124
FT                   /evidence="ECO:0000250|UniProtKB:Q7LZI1"
FT   DISULFID        117..146
FT                   /evidence="ECO:0000250|UniProtKB:Q7LZI1"
FT   DISULFID        150..172
FT                   /evidence="ECO:0000250|UniProtKB:Q7LZI1"
SQ   SEQUENCE   182 AA;  20301 MW;  23D41105D087A0B5 CRC64;
     RSCEICHNFG ADCESRAEEC DSPEDQCGTV LLEVSQAPIS FRTIHKNCFS SSLCKLERFD
     INIGHDSFMR GRIHCCDEEK CEGLQFPGLP LSLPNGYYCP GILGLFTVDS SEHEAICRGT
     ETKCINIAGF RKERYPADIA YNIKGCVSSC PELSLSNRTH EEHRNDLIKV ECTDASKIIP
     SE