ID PA2I_CRODU Reviewed; 200 AA. AC Q90358; DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 25-NOV-2008, entry version 40. DE RecName: Full=Gamma-phospholipase A2 inhibitor CNF; DE AltName: Full=Crotalus neutralizing factor; DE AltName: Full=Crotoxin inhibitor; DE Flags: Precursor; OS Crotalus durissus terrificus (South American rattlesnake). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Lepidosauria; Squamata; Scleroglossa; Serpentes; Colubroidea; OC Viperidae; Crotalinae; Crotalus. OX NCBI_TaxID=8732; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION. RC TISSUE=Liver; RX MEDLINE=94253151; 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 CHARACTERIZATION, AND PARTIAL PROTEIN SEQUENCE. 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 CHARACTERIZATION, AND FUNCTION. RX PubMed=7851385; 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 PA2 activity of the basic subunit. CNF is CC able to inhibit basic and acidic PA2 from L.m.muta and CC B.jararacussu, even more efficiently. 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 --------------------------------------------------------------------------- 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; Q90358; -. DR GO; GO:0005576; C:extracellular region; IEA:InterPro. DR GO; GO:0019834; F:phospholipase A2 inhibitor activity; IEA:InterPro. DR GO; GO:0032429; P:regulation of phospholipase A2 activity; IEA:InterPro. DR InterPro; IPR016054; LY6_UPA_recep-like. DR InterPro; IPR004126; PLA2_inh. DR InterPro; IPR016338; PLipase_A2-inh_a/b-type. 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; Glycoprotein; Phospholipase A2 inhibitor; KW Secreted; Signal. FT SIGNAL 1 19 By similarity. FT CHAIN 20 200 Gamma-phospholipase A2 inhibitor CNF. FT /FTId=PRO_0000022999. FT CARBOHYD 176 176 N-linked (GlcNAc...) (Probable). FT DISULFID 22 46 By similarity. FT DISULFID 25 32 By similarity. FT DISULFID 39 67 By similarity. FT DISULFID 73 94 By similarity. FT DISULFID 95 100 By similarity. FT DISULFID 118 143 By similarity. FT DISULFID 136 165 By similarity. FT DISULFID 169 191 By similarity. 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 //