ID   PLIB_GLOBS              Reviewed;         331 AA.
AC   O93233;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=Phospholipase A2 inhibitor;
DE            Short=beta-PLI;
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], PROTEIN SEQUENCE OF 24-53; 59-87; 93-105;
RP   165-173; 177-195; 204-219; 225-230; 305-313 AND 317-330, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=9677367; DOI=10.1074/jbc.273.31.19469;
RA   Okumura K., Ohkura N., Inoue S., Ikeda K., Hayashi K.;
RT   "A novel phospholipase A2 inhibitor with leucine-rich repeats from the
RT   blood plasma of Agkistrodon blomhoffii siniticus. Sequence homologies with
RT   human leucine-rich alpha2-glycoprotein.";
RL   J. Biol. Chem. 273:19469-19475(1998).
RN   [2]
RP   PROTEIN SEQUENCE OF 24-53, FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
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 the basic phospholipase A2
CC       (PLA2). {ECO:0000269|PubMed:9230137}.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:9230137}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9230137}.
CC       Note=Secreted in plasma. {ECO:0000269|PubMed:9230137}.
CC   -!- MASS SPECTROMETRY: Mass=43857.2; Mass_error=81.9; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:9677367};
CC   -!- SIMILARITY: Belongs to the beta-type phospholipase A2 inhibitor family.
CC       {ECO:0000305}.
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DR   EMBL; AB007198; BAA31994.1; -; mRNA.
DR   AlphaFoldDB; O93233; -.
DR   SMR; O93233; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0019834; F:phospholipase A2 inhibitor activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.80.10.10; -; 3.
DR   InterPro; IPR000483; Cys-rich_flank_reg_C.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   Pfam; PF13855; LRR_8; 3.
DR   SMART; SM00369; LRR_TYP; 7.
DR   SMART; SM00082; LRRCT; 1.
DR   PROSITE; PS51450; LRR; 9.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Glycoprotein; Leucine-rich repeat;
KW   Phospholipase A2 inhibitor; Repeat; Secreted; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000269|PubMed:9230137,
FT                   ECO:0000269|PubMed:9677367"
FT   CHAIN           24..331
FT                   /note="Phospholipase A2 inhibitor"
FT                   /id="PRO_0000022068"
FT   REPEAT          78..101
FT                   /note="LRR 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          103..125
FT                   /note="LRR 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          127..149
FT                   /note="LRR 3"
FT                   /evidence="ECO:0000255"
FT   REPEAT          150..173
FT                   /note="LRR 4"
FT                   /evidence="ECO:0000255"
FT   REPEAT          175..197
FT                   /note="LRR 5"
FT                   /evidence="ECO:0000255"
FT   REPEAT          199..221
FT                   /note="LRR 6"
FT                   /evidence="ECO:0000255"
FT   REPEAT          223..244
FT                   /note="LRR 7"
FT                   /evidence="ECO:0000255"
FT   REPEAT          245..268
FT                   /note="LRR 8"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          279..330
FT                   /note="LRRCT"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        35
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        125
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        232
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        271
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        45
FT                   /note="S -> L (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   331 AA;  37092 MW;  C82FB5DE0E494C46 CRC64;
     MKSSVPSLLI ACLVMSLNSY TQQVLYCPPT PAPENVTEFV CNSPSLHEFP TGFPARAKMI
     SVEFTQVSSL GVEALQGLPN LQELHLSNNR LKTLPSGLFR NLPQLHTLDL STNHLEDLPP
     EIFTNASSLI LLPLSENQLA ELHPSWFQTL GELRILGLDH NQVKEIPISC FDKLKKLTSL
     DLSFNLLRRL APEMFSGLDN LEKLILESNP IQCIVGRTFH WHPKLTVLSL KNSSLTNIMG
     FFQPLEQLEL LDLSDNELTT MEPPVYKTSA NLSLDLSGNP WACDCRLDNL LTWVNEHNIH
     LYSKEEIVCA SPKHFKGECA TSLHKSQICP C