ID   PLB_CROAD               Reviewed;         553 AA.
AC   F8S101; J3S4V6;
DT   06-FEB-2013, integrated into UniProtKB/Swiss-Prot.
DT   21-SEP-2011, sequence version 1.
DT   25-MAY-2022, entry version 22.
DE   RecName: Full=Phospholipase B;
DE            Short=PLB;
DE            EC=3.1.1.-;
DE   Flags: Precursor;
OS   Crotalus adamanteus (Eastern diamondback rattlesnake).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Crotalus.
OX   NCBI_TaxID=8729;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=21255598; DOI=10.1016/j.toxicon.2011.01.008;
RA   Rokyta D.R., Wray K.P., Lemmon A.R., Lemmon E.M., Caudle S.B.;
RT   "A high-throughput venom-gland transcriptome for the eastern diamondback
RT   rattlesnake (Crotalus adamanteus) and evidence for pervasive positive
RT   selection across toxin classes.";
RL   Toxicon 57:657-671(2011).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROBABLE FUNCTION.
RC   TISSUE=Venom gland;
RX   PubMed=23025625; DOI=10.1186/1471-2164-13-312;
RA   Rokyta D.R., Lemmon A.R., Margres M.J., Aronow K.;
RT   "The venom-gland transcriptome of the eastern diamondback rattlesnake
RT   (Crotalus adamanteus).";
RL   BMC Genomics 13:312-312(2012).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Venom;
RX   PubMed=24231107; DOI=10.1016/j.jprot.2013.11.001;
RA   Margres M.J., McGivern J.J., Wray K.P., Seavy M., Calvin K., Rokyta D.R.;
RT   "Linking the transcriptome and proteome to characterize the venom of the
RT   eastern diamondback rattlesnake (Crotalus adamanteus).";
RL   J. Proteomics 96:145-158(2014).
CC   -!- FUNCTION: May cause hemolysis or may be involved in protein folding and
CC       translation. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- SIMILARITY: Belongs to the phospholipase B-like family. {ECO:0000305}.
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DR   EMBL; HQ414105; AEJ31983.1; -; mRNA.
DR   EMBL; JU175433; AFJ50957.1; -; mRNA.
DR   AlphaFoldDB; F8S101; -.
DR   SMR; F8S101; -.
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"
FT                   /id="PRO_5000771370"
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"
FT   CONFLICT        288..290
FT                   /note="LFG -> FLV (in Ref. 2; AFJ50957)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   553 AA;  64049 MW;  74701D4B61DF1857 CRC64;
     MIRFGNPSSS DKRRQRCRSW YWGGLLLLWA VAETRADIHY ATVYWLEAEK SFQIKDVLDK
     NGDAYGYYND AIQSTGWGIL EIKAGYGNQP ISNEILMYAA GFLEGYLTAS HMSDHFANLF
     PLMIKNVIIE QKVKDFIQKQ DEWTRQQIKN NKDDPFWRNA GYVIAQLDGL YMGNVEWAKR
     QKRTPLTDFE ISFLNAIGDL LDLIPALHSE LRKSDFRSMP DVSRIYQWDM GHCSALIKVL
     PGYENIYFAH SSWFTYAATL RIYKHLDFRI TDPQTKTGRA SFSSYPGLFG SLDDFYILGS
     GLIMLQTTNS VFNLSLLKKV VPESLFAWER VRIANMMADS GKTWAETFEK QNSGTYNNQY
     MILDTKKIKL QRSLEDGTLY IIEQVPKLVK YSDQTKVLRN GYWPSYNIPF DKEIYNMSGY
     GEYVQRHGLE FSYEMAPRAK IFRRDQGKVT DMESMKFIMR YNNYKEDPYA KHNPCNTICC
     RQDLDRRTPV PAGCYDSKVA DISMAAKFTA YAINGPPVEK GLPVFSWVHF NKTKHQGLPE
     SYNFDFVTMK PVL