ID   PLIG1_CERGO             Reviewed;         200 AA.
AC   P0DQP7;
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-I {ECO:0000305};
DE   AltName: Full=Myotoxin inhibitor protein I of C.godmani {ECO:0000303|PubMed:10698689};
DE            Short=CgMIP-I {ECO:0000303|PubMed:10698689};
DE   AltName: Full=gamma-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 20-49, FUNCTION,
RP   SUBCELLULAR 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: Inhibits the enzymatic activity of basic phospholipase A2
CC       (PubMed:10698689). Specifically neutralizes PLA2, myotoxic, edema-
CC       forming, cytolytic, and anti-coagulant activities, as well as
CC       intracerebral lethal effect of the basic myotoxin I from the same venom
CC       (AC P0DQP6), crotoxin heterodimer and crotoxin subunit B alone
CC       (PubMed:10698689). Does not block the enzymatic activity of crude
CC       acidic PLA2 fractions from the same venom (PubMed:10698689).
CC       {ECO:0000269|PubMed:10698689}.
CC   -!- SUBUNIT: Homomer of 110 kDa composed of 20-25-kDa subunits.
CC       {ECO:0000269|PubMed:10698689}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10698689}.
CC       Note=Secreted in blood plasma. {ECO:0000269|PubMed:10698689}.
CC   -!- TISSUE SPECIFICITY: Expressed by the liver.
CC       {ECO:0000305|PubMed:10698689}.
CC   -!- PTM: N-glycosylated. The glycosidic chain may contain superficial
CC       sialic acid residues. {ECO:0000269|PubMed:10698689}.
CC   -!- SIMILARITY: Belongs to the CNF-like-inhibitor family. {ECO:0000305}.
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DR   AlphaFoldDB; P0DQP7; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0019834; F:phospholipase A2 inhibitor activity; IEA:UniProtKB-KW.
DR   GO; GO:0032429; P:regulation of phospholipase A2 activity; IEA:InterPro.
DR   Gene3D; 2.10.60.10; -; 1.
DR   InterPro; IPR016054; LY6_UPA_recep-like.
DR   InterPro; IPR016338; PLipase_A2-inh_a/b-type.
DR   InterPro; IPR004126; PLipase_A2_inh.
DR   InterPro; IPR045860; Snake_toxin-like_sf.
DR   Pfam; PF02988; PLA2_inh; 1.
DR   Pfam; PF00021; UPAR_LY6; 1.
DR   PIRSF; PIRSF002023; PLA2_inhib_alpha/gamma; 1.
DR   SMART; SM00134; LU; 1.
DR   SUPFAM; SSF57302; SSF57302; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein;
KW   Phospholipase A2 inhibitor; Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000269|PubMed:10698689"
FT   CHAIN           20..200
FT                   /note="Phospholipase A2 inhibitor CgMIP-I"
FT                   /evidence="ECO:0000305|PubMed:10698689"
FT                   /id="PRO_0000452705"
FT   CARBOHYD        176
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        22..46
FT                   /evidence="ECO:0000250|UniProtKB:Q7LZI2"
FT   DISULFID        25..32
FT                   /evidence="ECO:0000250|UniProtKB:Q7LZI2"
FT   DISULFID        39..67
FT                   /evidence="ECO:0000250|UniProtKB:Q7LZI2"
FT   DISULFID        73..94
FT                   /evidence="ECO:0000250|UniProtKB:Q7LZI2"
FT   DISULFID        95..100
FT                   /evidence="ECO:0000250|UniProtKB:Q7LZI2"
FT   DISULFID        118..143
FT                   /evidence="ECO:0000250|UniProtKB:Q7LZI2"
FT   DISULFID        136..165
FT                   /evidence="ECO:0000250|UniProtKB:Q7LZI2"
FT   CONFLICT        35
FT                   /note="Y -> V (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        41
FT                   /note="S -> D (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   200 AA;  22407 MW;  77F55557C456CE0D CRC64;
     MKYLHTICLL FIFVARGNSR SCDFCHNIGK ECDGYEKECS SPEDVCGKVL LEISSASLSV
     RTVHKNCFSS SVCKLEQFDV NIGHHSYIRG RINCCEKEQC EDRPFPGLPL SQPNGYYCPG
     ALGLFTEDST EFEAICKGTE TKCINIVGHR HEDFPGDISY NLKGCISSCP LLSLSNATHE
     ENRNYLEKVE CKDAFQLARL