ID   PLIA_BOTJR              Reviewed;         151 AA.
AC   B2D1Y0;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   25-MAY-2022, entry version 45.
DE   RecName: Full=Phospholipase A2 inhibitor BjussuMIP;
DE            Short=alpha-PLI;
DE   Flags: Precursor; Fragment;
OS   Bothrops jararacussu (Jararacussu).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX   NCBI_TaxID=8726;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 5-25; 27-40; 51-74 AND
RP   86-93, IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SUBUNIT,
RP   GLYCOSYLATION, AND SUBCELLULAR LOCATION.
RC   TISSUE=Liver, and Plasma;
RX   PubMed=18549822; DOI=10.1016/j.biochi.2008.05.009;
RA   Oliveira C.Z., Menaldo D.L., Marcussi S., Santos-Filho N.A., Silveira L.B.,
RA   Boldrini-Franca J., Rodrigues V.M., Soares A.M.;
RT   "An alpha-type phospholipase A(2) inhibitor from Bothrops jararacussu snake
RT   plasma: structural and functional characterization.";
RL   Biochimie 90:1506-1514(2008).
CC   -!- FUNCTION: Inhibits enzymatic, anticoagulant, edema formation,
CC       myotoxicity activities induced by snakes phospholipase A2. Is
CC       oligomeric, but it is probable that each of its subunits can bind and
CC       inactive a PLA2 molecule. {ECO:0000269|PubMed:18549822}.
CC   -!- SUBUNIT: Oligomer. {ECO:0000269|PubMed:18549822}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18549822}.
CC       Note=Secreted in plasma. {ECO:0000269|PubMed:18549822}.
CC   -!- TISSUE SPECIFICITY: Expressed by the liver.
CC   -!- SIMILARITY: Belongs to the alpha-type phospholipase A2 inhibitor
CC       family. {ECO:0000305}.
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DR   EMBL; EU574627; ACB70224.1; -; mRNA.
DR   AlphaFoldDB; B2D1Y0; -.
DR   SMR; B2D1Y0; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR   GO; GO:0019834; F:phospholipase A2 inhibitor activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.10.100.10; -; 1.
DR   InterPro; IPR001304; C-type_lectin-like.
DR   InterPro; IPR016186; C-type_lectin-like/link_sf.
DR   InterPro; IPR018378; C-type_lectin_CS.
DR   InterPro; IPR016187; CTDL_fold.
DR   Pfam; PF00059; Lectin_C; 1.
DR   SUPFAM; SSF56436; SSF56436; 1.
DR   PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
DR   PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PE   1: Evidence at protein level;
KW   Calcium; Direct protein sequencing; Disulfide bond; Glycoprotein; Lectin;
KW   Phospholipase A2 inhibitor; Secreted; Signal.
FT   SIGNAL          <1..4
FT                   /evidence="ECO:0000269|PubMed:18549822"
FT   CHAIN           5..151
FT                   /note="Phospholipase A2 inhibitor BjussuMIP"
FT                   /id="PRO_5000337460"
FT   DOMAIN          31..146
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   CARBOHYD        107
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        68..145
FT                   /evidence="ECO:0000250|UniProtKB:P21755"
FT   DISULFID        123..137
FT                   /evidence="ECO:0000250|UniProtKB:P21755"
FT   NON_TER         1
SQ   SEQUENCE   151 AA;  16621 MW;  76716F26CF898558 CRC64;
     LANGDEVDPD GHVLNSLIET VMRLQREFAN LKYAFLTVHK ARSFGSGSER LYVTNKEVKN
     FEPLGEICSQ AGGRIPSPQL ENQNKAFASV LERHNKAAYL VVGDSANFTN WAAGEPNEAD
     GTCVKADTHG SWHSASCDEN LLVVCEFYFI L