ID   LIPE_CROAD              Reviewed;         497 AA.
AC   J3RZ81;
DT   26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2012, sequence version 1.
DT   03-AUG-2022, entry version 30.
DE   RecName: Full=Putative endothelial lipase;
DE            EC=3.1.1.3;
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=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).
CC   -!- FUNCTION: Has phospholipase and triglyceride lipase activities.
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a triacylglycerol + H2O = a diacylglycerol + a fatty acid +
CC         H(+); Xref=Rhea:RHEA:12044, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17855, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868; EC=3.1.1.3;
CC   -!- ACTIVITY REGULATION: Inhibited by serum.
CC   -!- SUBUNIT: Head to tail homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC       {ECO:0000305}.
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DR   EMBL; JU174458; AFJ49984.1; -; mRNA.
DR   AlphaFoldDB; J3RZ81; -.
DR   SMR; J3RZ81; -.
DR   ESTHER; croad-lipe; Lipoprotein_Lipase.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR   GO; GO:0004465; F:lipoprotein lipase activity; IEA:InterPro.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd00707; Pancreat_lipase_like; 1.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR013818; Lipase.
DR   InterPro; IPR016272; Lipase_LIPH.
DR   InterPro; IPR033906; Lipase_N.
DR   InterPro; IPR002330; Lipo_Lipase.
DR   InterPro; IPR001024; PLAT/LH2_dom.
DR   InterPro; IPR036392; PLAT/LH2_dom_sf.
DR   InterPro; IPR000734; TAG_lipase.
DR   PANTHER; PTHR11610; PTHR11610; 1.
DR   Pfam; PF00151; Lipase; 1.
DR   Pfam; PF01477; PLAT; 1.
DR   PIRSF; PIRSF000865; Lipoprotein_lipase_LIPH; 1.
DR   PRINTS; PR00822; LIPOLIPASE.
DR   PRINTS; PR00821; TAGLIPASE.
DR   SMART; SM00308; LH2; 1.
DR   SUPFAM; SSF49723; SSF49723; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   PROSITE; PS00120; LIPASE_SER; 1.
DR   PROSITE; PS50095; PLAT; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Heparin-binding; Hydrolase;
KW   Lipid degradation; Lipid metabolism; Secreted; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..497
FT                   /note="Putative endothelial lipase"
FT                   /id="PRO_0000422919"
FT   DOMAIN          357..492
FT                   /note="PLAT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT   ACT_SITE        178
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        202
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT   ACT_SITE        284
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT   BINDING         335..347
FT                   /ligand="heparin"
FT                   /ligand_id="ChEBI:CHEBI:28304"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        89
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        145
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        403
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        73..86
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT   DISULFID        262..282
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT   DISULFID        307..326
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT   DISULFID        318..321
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
SQ   SEQUENCE   497 AA;  56087 MW;  D78F0C58F27BAB1D CRC64;
     MRACPFLLLL LLPLLLSLGR IAAVRDAAGA GPERRQDDSV SQVQKLREEP SKVRDLQVKF
     IVRTTPDLDD ADCYITAGQD HLLDDCNFNV SAKTFFVIHG WTMGGMYERW LDTLVSALQE
     REKEANVVVV NWLALAQQLY TIAVNNTRVV GKELAGLLDW LEEKKDFQLK NVHLIGYSLG
     AHIAGYTGNY ARGIIGRITG LDPAGPMFEG ADPSRRLSPD DADFVDVLHT YTRETLGISI
     GIQMPVGHID IYPNGGDIQP GCGLTDILGT LALGEIGDLV ICEHERSVHL FVDSLVNKDK
     QSFAFQCTDS GRFKKGICLS CRKNRCNSIG YNIKKMRNKR NSKMYLKTRA GMPFKVFHYQ
     LKIHVFSYKS LGETEPSFSV TFYGTSGDSE PLPLEVSDQI GLNYTNTFLV YTEEDVGDIL
     RIKLTWESTT QSWYNFWSQM KNYWSKPDPS SKELQIRRIR VKSGETQKKA MLAVEFWELK
     STCLKMVKVE KHCSRPL