ID   PLIG_CRODO              Reviewed;          95 AA.
AC   C0HJU4;
DT   16-SEP-2015, integrated into UniProtKB/Swiss-Prot.
DT   16-SEP-2015, sequence version 1.
DT   25-MAY-2022, entry version 7.
DE   RecName: Full=Phospholipase A2 inhibitor gammaCdcPLI {ECO:0000303|PubMed:24513130};
DE   AltName: Full=gamma-PLI {ECO:0000250|UniProtKB:Q90358};
DE   Flags: Fragments;
OS   Crotalus durissus collilineatus (Brazilian rattlesnake).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Crotalus.
OX   NCBI_TaxID=221569 {ECO:0000303|PubMed:24513130};
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, MASS
RP   SPECTROMETRY, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Serum {ECO:0000303|PubMed:24513130};
RX   PubMed=24513130; DOI=10.1016/j.toxicon.2014.01.012;
RA   Gimenes S.N., Ferreira F.B., Silveira A.C., Rodrigues R.S., Yoneyama K.A.,
RA   Izabel Dos Santos J., Fontes M.R., de Campos Brites V.L., Santos A.L.,
RA   Borges M.H., Lopes D.S., Rodrigues V.M.;
RT   "Isolation and biochemical characterization of a gamma-type phospholipase
RT   A2 inhibitor from Crotalus durissus collilineatus snake serum.";
RL   Toxicon 81:58-66(2014).
CC   -!- FUNCTION: Inhibits the enzymatic activity of basic and acidic PLA2 from
CC       B.jararacussu and B.pauloensis, respectively, in a dose-dependent
CC       manner. Also inhibits myotoxicity and cytotoxicity of BnSp-7 of
CC       B.pauloensis. {ECO:0000269|PubMed:24513130}.
CC   -!- SUBUNIT: Forms dimers or higher order oligomers in a temperature-
CC       dependent manner in vitro. {ECO:0000269|PubMed:24513130}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24513130}.
CC       Note=Secreted in blood plasma. {ECO:0000269|PubMed:24513130}.
CC   -!- TISSUE SPECIFICITY: Expressed by the liver.
CC       {ECO:0000305|PubMed:24513130}.
CC   -!- MASS SPECTROMETRY: Mass=22340; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:24513130};
CC   -!- SIMILARITY: Belongs to the CNF-like-inhibitor family. {ECO:0000305}.
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DR   AlphaFoldDB; C0HJU4; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0019834; F:phospholipase A2 inhibitor activity; IEA:UniProtKB-KW.
DR   InterPro; IPR004126; PLipase_A2_inh.
DR   Pfam; PF02988; PLA2_inh; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Phospholipase A2 inhibitor;
KW   Secreted.
FT   CHAIN           1..95
FT                   /note="Phospholipase A2 inhibitor gammaCdcPLI"
FT                   /evidence="ECO:0000269|PubMed:24513130"
FT                   /id="PRO_0000433785"
FT   DISULFID        2..26
FT                   /evidence="ECO:0000250|UniProtKB:Q7LZI1"
FT   DISULFID        5..12
FT                   /evidence="ECO:0000250|UniProtKB:Q7LZI1"
FT   DISULFID        19..30
FT                   /evidence="ECO:0000250|UniProtKB:Q7LZI1"
FT   DISULFID        36..?
FT                   /evidence="ECO:0000250|UniProtKB:Q7LZI1"
FT   DISULFID        40..?
FT                   /evidence="ECO:0000250|UniProtKB:Q7LZI1"
FT   DISULFID        61..77
FT                   /evidence="ECO:0000250|UniProtKB:Q7LZI1"
FT   DISULFID        81..?
FT                   /evidence="ECO:0000250|UniProtKB:Q7LZI1"
FT   NON_CONS        28..29
FT                   /evidence="ECO:0000303|PubMed:24513130"
FT   NON_CONS        37..38
FT                   /evidence="ECO:0000303|PubMed:24513130"
FT   NON_CONS        52..53
FT                   /evidence="ECO:0000303|PubMed:24513130"
FT   NON_CONS        62..63
FT                   /evidence="ECO:0000303|PubMed:24513130"
FT   NON_TER         1
FT                   /evidence="ECO:0000303|PubMed:24513130"
FT   NON_TER         95
FT                   /evidence="ECO:0000303|PubMed:24513130"
SQ   SEQUENCE   95 AA;  10497 MW;  A5F0C5A4749FCE75 CRC64;
     SCDFCHNIGK DCDGYEEECS SPEDVCGKNC FSSSICKELC EDQPEPGEPL SKDSTEYEAI
     CKYEQFPGDI SYNLKGCVSS CPLLSLSNAT FEQNR