ID   PLIB_ELACL              Reviewed;         332 AA.
AC   C0STK7;
DT   02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   29-SEP-2021, entry version 29.
DE   RecName: Full=Phospholipase A2 inhibitor beta {ECO:0000303|PubMed:19673083};
DE            Short=PLI-beta {ECO:0000303|PubMed:19673083};
DE            Short=beta-PLI;
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 24-30, SUBCELLULAR
RP   LOCATION, 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 basic phospholipase A2
CC       (PLA2). {ECO:0000269|PubMed:19673083}.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:19673083}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19673083}.
CC       Note=Secreted in plasma. {ECO:0000269|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 beta-type phospholipase A2 inhibitor family.
CC       {ECO:0000305}.
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DR   EMBL; AB462511; BAH47549.1; -; mRNA.
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; -; 2.
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; PF00560; LRR_1; 1.
DR   Pfam; PF13855; LRR_8; 2.
DR   SMART; SM00369; LRR_TYP; 6.
DR   SMART; SM00082; LRRCT; 1.
DR   PROSITE; PS51450; LRR; 7.
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:19673083"
FT   CHAIN           24..332
FT                   /note="Phospholipase A2 inhibitor beta"
FT                   /evidence="ECO:0000305|PubMed:19673083"
FT                   /id="PRO_5002903549"
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          198..221
FT                   /note="LRR 6"
FT                   /evidence="ECO:0000255"
FT   REPEAT          223..245
FT                   /note="LRR 7"
FT                   /evidence="ECO:0000255"
FT   REPEAT          247..269
FT                   /note="LRR 8"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          280..331
FT                   /note="LRRCT"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        35
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        232
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        272
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   332 AA;  37244 MW;  3B8E29357C01D835 CRC64;
     MKSSVPSLLF VSLVMSLNSY TQQVLYCPPD PAPENITEFV CNSPSLHEFP TGFPVRTKII
     SVEFTQVSSL GVEALQGLPN LQELHLSNNR LKTLPSGLFR NLPELHTLDL STNLLEDLPP
     EIFTSTTSLT LLSISENRLA KLRLSWFETL KELRILSLDN NQLKEVPISC FDKLEKLTFL
     DLSSNHLHRL SPDMFSGLDN LERLSLENNP IRCIAPKSFH GRPKLSIISL KNCSLTNIIT
     GVFQPLNHXV LLDLSDNELT MLDPPVAIPS ANLSLDLTGN PWACNCRMDN LLTWVKEHKI
     DLYSKQEIVC AFPKSFKGEE ATSLHRSQIC PC