ID   PLIA2_CERGO             Reviewed;         166 AA.
AC   P0DQP8;
DT   02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT   02-JUN-2021, sequence version 1.
DT   25-MAY-2022, entry version 4.
DE   RecName: Full=Phospholipase A2 inhibitor CgMIP-II {ECO:0000303|PubMed:10698689};
DE   AltName: Full=Myotoxin inhibitor protein II of C.godmani {ECO:0000303|PubMed:10698689};
DE            Short=CgMIP-II {ECO:0000303|PubMed:10698689};
DE   AltName: Full=alpha-PLI;
DE   Flags: Precursor;
OS   Cerrophidion godmani (Porthidium godmani) (Bothrops godmani).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Cerrophidion.
OX   NCBI_TaxID=44722;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 20-46, SUBCELLULAR
RP   LOCATION, AND GLYCOSYLATION.
RC   TISSUE=Liver, and Plasma;
RX   PubMed=10698689; DOI=10.1042/bj3460631;
RA   Lizano S., Angulo Y., Lomonte B., Fox J.W., Lambeau G., Lazdunski M.,
RA   Gutierrez J.M.;
RT   "Two phospholipase A2 inhibitors from the plasma of Cerrophidion (Bothrops)
RT   godmani which selectively inhibit two different group-II phospholipase A2
RT   myotoxins from its own venom: isolation, molecular cloning and biological
RT   properties.";
RL   Biochem. J. 346:631-639(2000).
CC   -!- FUNCTION: Selectively inhibits the toxic properties of myotoxin-II from
CC       the same venom (AC P81165) (PubMed:10698689). Does not inhibit PLA2,
CC       anti-coagulant and lethal activities of the basic myotoxin I from the
CC       same venom (AC P0DQP6), nor the different crotoxin forms (heterodimer
CC       or subunit B alone) (PubMed:10698689). Does not block the enzymatic
CC       activity of crude acidic PLA2 fractions from the same venom
CC       (PubMed:10698689). {ECO:0000269|PubMed:10698689}.
CC   -!- SUBUNIT: Homomer composed of 20-25-kDa subunits that form oligomers of
CC       180 kDa. {ECO:0000269|PubMed:10698689}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P21755}.
CC       Note=Secreted in plasma. {ECO:0000250|UniProtKB:P21755}.
CC   -!- TISSUE SPECIFICITY: Expressed by the liver.
CC       {ECO:0000250|UniProtKB:P21755}.
CC   -!- PTM: N-glycosylated. The glycosidic chain may contain superficial
CC       sialic acid residues. {ECO:0000269|PubMed:10698689}.
CC   -!- SIMILARITY: Belongs to the alpha-type phospholipase A2 inhibitor
CC       family. {ECO:0000305}.
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DR   AlphaFoldDB; P0DQP8; -.
DR   SMR; P0DQP8; -.
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   Direct protein sequencing; Disulfide bond; Glycoprotein; Lectin;
KW   Phospholipase A2 inhibitor; Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000269|PubMed:10698689"
FT   CHAIN           20..166
FT                   /note="Phospholipase A2 inhibitor CgMIP-II"
FT                   /evidence="ECO:0000305|PubMed:10698689"
FT                   /id="PRO_0000452706"
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:0000250|UniProtKB:P21755"
FT   DISULFID        83..160
FT                   /evidence="ECO:0000250|UniProtKB:P21755"
FT   DISULFID        138..152
FT                   /evidence="ECO:0000250|UniProtKB:P21755"
FT   CONFLICT        42..43
FT                   /note="DF -> HV (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   166 AA;  18282 MW;  815410F26F79480C CRC64;
     MRLILLSGLL LLGTFLANGD EKDSEIQLLN SMIEAVMILQ RDFSNLRYAL MTVHNARSFG
     SGSERVYVSN KEVSKFEGLE EICSQAGGHI PSPQLENQNK AFADVLERHN KAAYLVVGDS
     ANFTNWAAGH PNEADGTCVK ADTHGSWHSA SCDDNLLVVC EFYFIL