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Database: UniProt
Entry: T1DLW3_CROHD
LinkDB: T1DLW3_CROHD
Original site: T1DLW3_CROHD 
ID   T1DLW3_CROHD            Unreviewed;       553 AA.
AC   T1DLW3;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 13.
DE   RecName: Full=Phospholipase B-like {ECO:0000256|RuleBase:RU364138};
DE            EC=3.1.1.- {ECO:0000256|RuleBase:RU364138};
OS   Crotalus horridus (Timber rattlesnake).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Crotalus.
OX   NCBI_TaxID=35024 {ECO:0000313|EMBL:JAA96126.1};
RN   [1] {ECO:0000313|EMBL:JAA96126.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Venom gland {ECO:0000313|EMBL:JAA96126.1};
RX   PubMed=23758969; DOI=10.1186/1471-2164-14-394;
RA   Rokyta D.R., Wray K.P., Margres M.J.;
RT   "The genesis of an exceptionally lethal venom in the timber rattlesnake
RT   (Crotalus horridus) revealed through comparative venom-gland
RT   transcriptomics.";
RL   BMC Genomics 14:394-394(2013).
CC   -!- FUNCTION: Putative phospholipase. {ECO:0000256|RuleBase:RU364138}.
CC   -!- SIMILARITY: Belongs to the phospholipase B-like family.
CC       {ECO:0000256|ARBA:ARBA00007835, ECO:0000256|RuleBase:RU364138}.
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DR   EMBL; GAAZ01001817; JAA96126.1; -; mRNA.
DR   AlphaFoldDB; T1DLW3; -.
DR   GO; GO:0004620; F:phospholipase activity; IEA:InterPro.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.60.60.20; -; 1.
DR   Gene3D; 2.10.70.60; Phospholipase B-like, domain 1; 1.
DR   Gene3D; 1.10.439.20; Phospholipase B-like, domain 2; 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:SF1; PHOSPHOLIPASE B-LIKE 1; 1.
DR   PANTHER; PTHR12370; PHOSPHOLIPASE B-RELATED; 1.
DR   Pfam; PF04916; Phospholip_B; 1.
PE   2: Evidence at transcript level;
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU364138};
KW   Lipid degradation {ECO:0000256|ARBA:ARBA00022963,
KW   ECO:0000256|RuleBase:RU364138};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098,
KW   ECO:0000256|RuleBase:RU364138}; Signal {ECO:0000256|ARBA:ARBA00022729}.
SQ   SEQUENCE   553 AA;  64180 MW;  167046201608EF4B CRC64;
     MIRFGNPSSS DKRRQRCRSW YWGGLLLLWA VAETRADIHY ATVYWLEAEK SFQIKDVLDK
     NGDAYGYYND TIQSTGWGIL EIKAGYGNQP ISNEILMYAA GFLEGYLTAS HMSDHFANLF
     PLMIKNVIIE QKVKDFIQKQ DEWTRQQIKN NKDDPFWRNA GYVIAQLDGL YMGNVEWAKQ
     QKRTPLTYFE ISFLNAIGDL LDLILALHSE LRKSDFRSMP DVSRMYQWDM GHCSALIKVL
     PGYENIYFAH SSWFTYAATL RIYKHLDFKI TDPQTKTGRA SFSSYPGFLV SLDDFYILGS
     GLIMLQTTNS VFNLSLLKKI VPESLFAWER VRIANMMADS GKTWAETFEK QNSGTYNNQY
     MILDTKKIKL QRSLEDGTLY IIEQVPKLVK YSDQTKVLRN GYWPSYNIPF DKEIYNMSGY
     GEYVQRHGLE FSYEMAPRAK IFRRDQGKVT DMESMKFIMR YNNYKEDPYA KRNPCNTICC
     RQDLDRRTPV PAGCYDSKVA DISMAAKFTA YAINGPPVEK GLPVFSWVHF NKTKHQGLPE
     SYNFDFVTMK PVL
//
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