ID   PLIGA_NOTAT             Reviewed;         201 AA.
AC   Q9PTC3;
DT   02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 55.
DE   RecName: Full=Phospholipase A2 inhibitor NAI {ECO:0000305};
DE   AltName: Full=Notechis ater inhibitor {ECO:0000303|PubMed:10625636};
DE            Short=NAI {ECO:0000303|PubMed:10625636};
DE   AltName: Full=gamma-PLI;
DE   Flags: Precursor;
OS   Notechis ater (Black tiger snake).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Acanthophiinae; Notechis.
OX   NCBI_TaxID=111176;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RA   Sekuloski S., Dunn R.D., Broady K.W.;
RT   "Identification of alpha and beta subunit isoforms of a Phospholipase A2
RT   inhibitor isolated from four species of Elapidae.";
RL   Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PROTEIN SEQUENCE OF 20-48, FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND
RP   GLYCOSYLATION.
RC   TISSUE=Serum;
RX   PubMed=10625636; DOI=10.1074/jbc.275.2.983;
RA   Hains P.G., Sung K.L., Tseng A., Broady K.W.;
RT   "Functional characteristics of a phospholipase A(2) inhibitor from Notechis
RT   ater serum.";
RL   J. Biol. Chem. 275:983-991(2000).
CC   -!- FUNCTION: Inhibits the enzymatic activity of all phospholipase A2
CC       tested, binding them with micromole to nanomole affinity.
CC       {ECO:0000269|PubMed:10625636}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 4-12. Important decrease in activity at pH 2.
CC         {ECO:0000269|PubMed:10625636};
CC       Temperature dependence:
CC         Optimum temperature is 4-90 degrees Celsius. Weak decrease in
CC         activity at 100 degrees Celsius. {ECO:0000269|PubMed:10625636};
CC   -!- SUBUNIT: Heterotrimer of 2 subunits A and 1 subunit B; non-covalently
CC       linked. {ECO:0000305|PubMed:10625636}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10625636}.
CC       Note=Secreted in blood plasma. {ECO:0000305|PubMed:10625636}.
CC   -!- TISSUE SPECIFICITY: Expressed by the liver. {ECO:0000305|Ref.1}.
CC   -!- PTM: N-glycosylated, probably by biantennary structure. Glycosylation
CC       does not change PLA2 inhibitory activity.
CC       {ECO:0000269|PubMed:10625636}.
CC   -!- SIMILARITY: Belongs to the CNF-like-inhibitor family. {ECO:0000305}.
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DR   EMBL; AF211162; AAF23779.1; -; mRNA.
DR   AlphaFoldDB; Q9PTC3; -.
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; 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:10625636"
FT   CHAIN           20..201
FT                   /note="Phospholipase A2 inhibitor NAI"
FT                   /evidence="ECO:0000305|PubMed:10625636"
FT                   /id="PRO_5004331294"
FT   CARBOHYD        176
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
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..191
FT                   /evidence="ECO:0000250|UniProtKB:Q7LZI1"
FT   CONFLICT        30
FT                   /note="K -> R (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        37
FT                   /note="T -> A (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        43
FT                   /note="A -> P (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   201 AA;  22315 MW;  FBE89DB7FE665744 CRC64;
     MKSLQIICLL FVLVARGSCH SCEICHNFGK DCQSDETEEC ASAEDQCGTV LMEVSSAPIS
     FRSIHRKCFS SSLCKLERFD INIGHDSYLR GRIHCCDEAR CEAQQFPGLP LSFPNGYHCP
     GILGVFSVDS SEHEAICRGT ETKCINLAGF RKERYPIDIA YNIKGCTSSC PELRLNRTHE
     EHGNGLIKVE CTEASKITPS E