ID   PLIA_BOTMO              Reviewed;         166 AA.
AC   Q8AYA2;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 59.
DE   RecName: Full=Phospholipase A2 myotoxin inhibitor protein;
DE            Short=BmjMIP;
DE            Short=alpha-PLI;
DE   Flags: Precursor;
OS   Bothrops moojeni (Lance-headed viper) (Caissaca).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX   NCBI_TaxID=98334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 20-61, FUNCTION, SUBUNIT,
RP   SUBCELLULAR LOCATION, AND GLYCOSYLATION.
RC   TISSUE=Liver, and Plasma;
RX   PubMed=12604331; DOI=10.1016/s0006-291x(03)00155-4;
RA   Soares A.M., Marcussi S., Stabeli R.G., Franca S.C., Giglio J.R.,
RA   Ward R.J., Arantes E.C.;
RT   "Structural and functional analysis of BmjMIP, a phospholipase A2 myotoxin
RT   inhibitor protein from Bothrops moojeni snake plasma.";
RL   Biochem. Biophys. Res. Commun. 302:193-200(2003).
CC   -!- FUNCTION: This phospholipase A2 inhibitor binds directly phospholipase
CC       A2 in the presence or absence of calcium. Has anti-enzymatic, anti-
CC       myotoxic, anti-edema inducing, anti-cytotoxic, anti-bactericidal, and
CC       anti-lethal properties against basic and acidic phospholipases A2 from
CC       Bothrops venoms. {ECO:0000269|PubMed:12604331}.
CC   -!- SUBUNIT: Oligomer (PubMed:12604331). Homotrimer; non-covalently linked
CC       (By similarity). {ECO:0000250|UniProtKB:A1XRN2,
CC       ECO:0000269|PubMed:12604331}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12604331}.
CC       Note=Secreted in plasma. {ECO:0000269|PubMed:12604331}.
CC   -!- TISSUE SPECIFICITY: Expressed by the liver.
CC       {ECO:0000269|PubMed:12604331}.
CC   -!- PTM: Glycosylated. The glycosylation has no role in the association of
CC       this PLI and PA2 enzyme. {ECO:0000269|PubMed:12604331}.
CC   -!- SIMILARITY: Belongs to the alpha-type phospholipase A2 inhibitor
CC       family. {ECO:0000305}.
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DR   EMBL; AF542045; AAN34657.1; -; mRNA.
DR   AlphaFoldDB; Q8AYA2; -.
DR   SMR; Q8AYA2; -.
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..19
FT                   /evidence="ECO:0000269|PubMed:12604331"
FT   CHAIN           20..166
FT                   /note="Phospholipase A2 myotoxin inhibitor protein"
FT                   /id="PRO_0000355232"
FT   DOMAIN          46..161
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   CARBOHYD        122
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        83..160
FT                   /evidence="ECO:0000250|UniProtKB:P21755"
FT   DISULFID        138..152
FT                   /evidence="ECO:0000250|UniProtKB:P21755"
SQ   SEQUENCE   166 AA;  18230 MW;  44745D014A8D03AF CRC64;
     MRLILLSGLL LLGTFLANGD ETDPDGQVLN SLIETLMHLQ REFANLKYAF LTVHKARSFG
     SGSERLYVSN KEIKNFEPLG DICSQAGGHI PSPQLENQNK AFANVLERHN KAAYLVVGDS
     ANFTNWAAGQ PNEADGTCVK ADTHGSWHSA SCDDNLLVVC EFYFIL