ID   PLB_DRYCN               Reviewed;         553 AA.
AC   F8J2D3;
DT   06-FEB-2013, integrated into UniProtKB/Swiss-Prot.
DT   21-SEP-2011, sequence version 1.
DT   25-MAY-2022, entry version 19.
DE   RecName: Full=Phospholipase-B 81;
DE            Short=PLB;
DE            EC=3.1.1.-;
DE   Flags: Precursor;
OS   Drysdalia coronoides (White-lipped snake) (Hoplocephalus coronoides).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Notechinae; Drysdalia.
OX   NCBI_TaxID=66186;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROBABLE FUNCTION, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=21133350; DOI=10.1021/pr1008916;
RA   Chatrath S.T., Chapeaurouge A., Lin Q., Lim T.K., Dunstan N., Mirtschin P.,
RA   Kumar P.P., Kini R.M.;
RT   "Identification of novel proteins from the venom of a cryptic snake
RT   Drysdalia coronoides by a combined transcriptomics and proteomics
RT   approach.";
RL   J. Proteome Res. 10:739-750(2011).
CC   -!- FUNCTION: May cause hemolysis. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- MISCELLANEOUS: Only two tryptic peptides have been identified.
CC       {ECO:0000305|PubMed:21133350}.
CC   -!- SIMILARITY: Belongs to the phospholipase B-like family. {ECO:0000305}.
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DR   EMBL; FJ752451; ACR78473.1; -; mRNA.
DR   AlphaFoldDB; F8J2D3; -.
DR   SMR; F8J2D3; -.
DR   PRIDE; F8J2D3; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004620; F:phospholipase activity; IEA:InterPro.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.439.20; -; 1.
DR   Gene3D; 2.10.70.60; -; 1.
DR   Gene3D; 3.60.60.20; -; 1.
DR   InterPro; IPR007000; PLipase_B-like.
DR   InterPro; IPR043040; PLipase_B-like_dom1.
DR   InterPro; IPR043041; PLipase_B-like_dom2.
DR   InterPro; IPR043042; PLipase_B-like_dom3.
DR   PANTHER; PTHR12370; PTHR12370; 1.
DR   Pfam; PF04916; Phospholip_B; 1.
PE   1: Evidence at protein level;
KW   Cytolysis; Glycoprotein; Hemolysis; Hydrolase; Lipid degradation;
KW   Lipid metabolism; Secreted; Signal; Toxin.
FT   SIGNAL          1..35
FT                   /evidence="ECO:0000255"
FT   CHAIN           36..553
FT                   /note="Phospholipase-B 81"
FT                   /id="PRO_0000421162"
FT   CARBOHYD        69
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        313
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        416
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        531
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   553 AA;  64103 MW;  3572EE88298C50EC CRC64;
     MVRFGSAASS DNRRRRCWSW YWGGLLLLWA VAETRADLHY ATVYWLEAEK SFQVKDLLDK
     NGDAYGYYND TVQSTGWGIL EIKAGYGSQL VSNEILMYAA GFLEGYLTAS RMSDHVANLY
     HQMIKNVITE QKVKDFMQKQ DEWTRQQIKN NKDDPFWRNA GYIIAQLDGL YMGNLEWAKR
     QKRTPLTKFE ISFLNALGDL LDLIPALSPE SRNNGFLSMS EISKMYEWDM GHCSALIKVL
     PGYENIYFAH SSWFTYAATL RIYKHLDFRI IDPQTKTGRA SFSSYPGLLA SLDDFYILGS
     GLIMLQTTNS VFNISLLQQV VPESLFAWER VRIANMMADS GKTWAQTFKK QNSGTYNNQY
     MILDTKKIKL RRSIEDGTLY IIEQVPNLVE YSDQTTILRK GYWPSYNIPF HKVIYNMSGY
     REYVQKYGLD FSYEMAPRAK IFRRDQGKVI DIESMKRIMR YNNYKKDPYT KHNPCNTICC
     RQDLYYMTPV PAGCYDSKVA DINMAAKFTA YAINGPPVEK GLPIFSWVHF NETTHQGLPE
     SYNFDFVTMK PVL