PLIGB_NOTAT
ID PLIGB_NOTAT Reviewed; 200 AA.
AC Q78CF9;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 47.
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, SUBCELLULAR LOCATION, FUNCTION, SUBUNIT, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
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 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 -!- SIMILARITY: Belongs to the CNF-like-inhibitor family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF211155; AAF21046.1; -; mRNA.
DR AlphaFoldDB; Q78CF9; -.
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; -; 2.
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:0000269|PubMed:10625636"
FT CHAIN 20..200
FT /note="Phospholipase A2 inhibitor NAI"
FT /evidence="ECO:0000305|PubMed:10625636"
FT /id="PRO_5004287583"
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:0000305"
FT DISULFID 171..191
FT /evidence="ECO:0000250|UniProtKB:Q7LZI1"
SQ SEQUENCE 200 AA; 21904 MW; FD7ADAAB44B46028 CRC64;
MKSLLFCCLF GTFLATGMCL ECEICIGLGL ECNTWTKTCD ANQDTCVTFQ TEVIRAPVSL
SLISKSCGTS DTCHLNYVET SPHNELTVKT KRTCCTGEEC KTLPPPVLGH KVNPPNGLQC
PGCLGLSSKE CTEHLVSCRG SENQCLSIIG KEFGLFFRAL SYKGCATESL CTLFEKRFWN
VLEDVEVDFK CTPALPKSSQ