PLIGA_GLOBS
ID PLIGA_GLOBS Reviewed; 200 AA.
AC P82144; Q9I851;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2002, sequence version 2.
DT 25-MAY-2022, entry version 66.
DE RecName: Full=Phospholipase A2 inhibitor gamma subunit A;
DE Short=gamma-PLI A;
DE AltName: Full=Phospholipase A2 inhibitor gamma 25 kDa subunit;
DE Flags: Precursor;
OS Gloydius brevicaudus siniticus (Chinese mamushi) (Agkistrodon blomhoffii
OS siniticus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Gloydius.
OX NCBI_TaxID=31147;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=10791922; DOI=10.1080/713803475;
RA Okumura K., Inoue S., Ohkura N., Ikeda K., Hayashi K.;
RT "cDNA cloning of the two subunits of a phospholipase A2 inhibitor PLIgamma
RT from blood plasma of the Chinese mamushi, Agkistrodon blomhoffii
RT siniticus.";
RL IUBMB Life 48:99-104(1999).
RN [2]
RP PROTEIN SEQUENCE OF 20-49, AND SUBCELLULAR LOCATION.
RC TISSUE=Plasma;
RX PubMed=9230137; DOI=10.1042/bj3250527;
RA Ohkura N., Okuhara H., Inoue S., Ikeda K., Hayashi K.;
RT "Purification and characterization of three distinct types of phospholipase
RT A2 inhibitors from the blood plasma of the Chinese mamushi, Agkistrodon
RT blomhoffii siniticus.";
RL Biochem. J. 325:527-531(1997).
CC -!- FUNCTION: Inhibits the enzymatic activity of phospholipase A2 (PA2).
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:9230137}.
CC Note=Secreted in blood plasma. {ECO:0000269|PubMed:9230137}.
CC -!- TISSUE SPECIFICITY: Expressed by the liver.
CC {ECO:0000305|PubMed:10791922}.
CC -!- SIMILARITY: Belongs to the CNF-like-inhibitor family. {ECO:0000305}.
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DR EMBL; AB018372; BAA86970.1; -; mRNA.
DR AlphaFoldDB; P82144; -.
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:9230137"
FT CHAIN 20..200
FT /note="Phospholipase A2 inhibitor gamma subunit A"
FT /evidence="ECO:0000305|PubMed:9230137"
FT /id="PRO_0000022997"
FT CARBOHYD 176
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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"
FT CONFLICT 41
FT /note="S -> I (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 200 AA; 22270 MW; 6D20A7BDE5039EEE CRC64;
MKSLHTICLL FIFIARGNSR SCDYCHNIGK DCDGYEHECS SPEDVCGKVF LEISSASLSV
RTVHKNCFSS SVCKLGHFDI NIGHHSYIRG RINCCEKEPC EDQPFPGLPL SQPNGYYCPG
ALGLFTEDST EYEAICKGTE TKCINIVGHR HENYPGDISY NLKGCVSSCP LLSLSNSTHE
ENRNYLEKVE CKDAFKIASH