PLIGA_ELACL
ID PLIGA_ELACL Reviewed; 202 AA.
AC C0STK8;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 26.
DE RecName: Full=Phospholipase A2 inhibitor gamma subunit A {ECO:0000303|PubMed:19673083};
DE AltName: Full=PLI-gamma A;
DE AltName: Full=gamma-PLI A {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 20-31, 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 -!- TISSUE SPECIFICITY: Expressed by the liver.
CC {ECO:0000305|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; AB462512; BAH47550.1; -; mRNA.
DR AlphaFoldDB; C0STK8; -.
DR SMR; C0STK8; -.
DR PRIDE; C0STK8; -.
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 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 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Phospholipase A2 inhibitor;
KW Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:19673083"
FT CHAIN 20..202
FT /note="Phospholipase A2 inhibitor gamma subunit A"
FT /id="PRO_5002902078"
FT DISULFID 22..47
FT /evidence="ECO:0000250|UniProtKB:Q7LZI1"
FT DISULFID 25..32
FT /evidence="ECO:0000250|UniProtKB:Q7LZI1"
FT DISULFID 40..68
FT /evidence="ECO:0000250|UniProtKB:Q7LZI1"
FT DISULFID 74..95
FT /evidence="ECO:0000250|UniProtKB:Q7LZI1"
FT DISULFID 96..101
FT /evidence="ECO:0000250|UniProtKB:Q7LZI1"
FT DISULFID 119..144
FT /evidence="ECO:0000250|UniProtKB:Q7LZI1"
FT DISULFID 137..166
FT /evidence="ECO:0000250|UniProtKB:Q7LZI1"
FT DISULFID 170..192
FT /evidence="ECO:0000250|UniProtKB:Q7LZI1"
SQ SEQUENCE 202 AA; 22608 MW; 71B6E33F6EF8D767 CRC64;
MKSLQIICLL FIFVARGSCR SCEICHNVGN DCGYDYVEEC HSPEDQCGKV FLEISSAPLS
IRSIHRNCFS SSLCKLEHFD VNTGQETYLR GRIHCCDEEK CEGRPFPGLP LSHPNGYVCP
GVLGLFSEDS SESEAACKGD ETKCINIVGY RKERFPGDIA YNIKGCVSSC PELRLSNRTH
EERRNDLIKV ECRDAVKITP SE