ID PLI_CRODU Reviewed; 200 AA. AC Q90358; DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 10-MAY-2017, entry version 56. DE RecName: Full=Phospholipase A2 inhibitor CNF; DE AltName: Full=Crotalus neutralizing factor; DE AltName: Full=Crotoxin inhibitor; DE AltName: Full=gamma-PLI; DE Flags: Precursor; OS Crotalus durissus terrificus (South American rattlesnake). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; OC Toxicofera; Serpentes; Colubroidea; Viperidae; Crotalinae; Crotalus. OX NCBI_TaxID=8732; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION. RC TISSUE=Liver; RX PubMed=8195214; RA Fortes-Dias C.L., Lin Y., Ewell J., Diniz C.R., Liu T.-Y.; RT "A phospholipase A2 inhibitor from the plasma of the South American RT rattlesnake (Crotalus durissus terrificus): protein structure, genomic RT structure and mechanism of action."; RL J. Biol. Chem. 269:15646-15651(1994). RN [2] RP PARTIAL PROTEIN SEQUENCE, AND FUNCTION. RX PubMed=1949070; DOI=10.1016/0041-0101(91)90082-3; RA Fortes-Dias C.L., Fonseca B.C., Kochva E., Diniz C.R.; RT "Purification and properties of an antivenom factor from the plasma of RT the South American rattlesnake (Crotalus durissus terrificus)."; RL Toxicon 29:997-1008(1991). RN [3] RP FUNCTION. RX PubMed=7851385; DOI=10.1111/j.1432-1033.1995.tb20355.x; RA Perales J., Villela C., Domont G.B., Choumet V., Saliou B., RA Moussatche H., Bon C., Faure G.; RT "Molecular structure and mechanism of action of the crotoxin inhibitor RT from Crotalus durissus terrificus serum."; RL Eur. J. Biochem. 227:19-26(1995). CC -!- FUNCTION: Acts by replacing the acid subunit in the crotoxin CC complex, inhibiting the PLA2 activity of the basic subunit. CNF is CC able to inhibit basic and acidic PLA2 from L.m.muta and CC B.jararacussu, even more efficiently. {ECO:0000269|PubMed:1949070, CC ECO:0000269|PubMed:7851385, ECO:0000269|PubMed:8195214}. CC -!- SUBUNIT: Homomer composed of six to eight subunits. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma. CC -!- SIMILARITY: Belongs to the CNF-like-inhibitor family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U08289; AAA19162.1; -; mRNA. DR PIR; A54020; A54020. DR HOVERGEN; HBG014739; -. 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 InterPro; IPR016054; LY6_UPA_recep-like. DR InterPro; IPR016338; PLipase_A2-inh_a/b-type. DR InterPro; IPR004126; PLipase_A2_inh. DR Pfam; PF02988; PLA2_inh; 1. DR PIRSF; PIRSF002023; PLA2_inhib_alpha/gamma; 1. DR SMART; SM00134; LU; 1. PE 1: Evidence at protein level; KW Direct protein sequencing; Disulfide bond; Glycoprotein; KW Phospholipase A2 inhibitor; Secreted; Signal. FT SIGNAL 1 19 {ECO:0000250}. FT CHAIN 20 200 Phospholipase A2 inhibitor CNF. FT /FTId=PRO_0000022999. FT CARBOHYD 176 176 N-linked (GlcNAc...) asparagine. FT {ECO:0000305}. FT DISULFID 22 46 {ECO:0000250}. FT DISULFID 25 32 {ECO:0000250}. FT DISULFID 39 67 {ECO:0000250}. FT DISULFID 73 94 {ECO:0000250}. FT DISULFID 95 100 {ECO:0000250}. FT DISULFID 118 143 {ECO:0000250}. FT DISULFID 136 165 {ECO:0000250}. FT DISULFID 169 191 {ECO:0000250}. SQ SEQUENCE 200 AA; 22267 MW; AE848DD6EDD9BBFF CRC64; MKYLHTICLL FIFVARGNSR SCDFCHNIGK DCDGYEEECS SPEDVCGKVL LEISSASLSV RTVHKNCFSS SICKLGQFDV NIGHHSYIRG RINCCEKELC EDQPFPGLPL SKPNGYYCPG AIGLFTKDST EYEAICKGTE TKCINIVGHR YEQFPGDISY NLKGCVSSCP LLSLSNATFE QNRNYLEKVE CKDAIRLASL //