LICH_CROAD
ID LICH_CROAD Reviewed; 400 AA.
AC J3SDX8;
DT 26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2012, sequence version 1.
DT 25-MAY-2022, entry version 22.
DE RecName: Full=Putative lysosomal acid lipase/cholesteryl ester hydrolase;
DE Short=Acid cholesteryl ester hydrolase;
DE Short=LAL;
DE EC=3.1.1.13;
DE AltName: Full=Cholesteryl esterase;
DE AltName: Full=Lipase A;
DE AltName: Full=Sterol esterase;
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: In physiological conditions, is crucial for intracellular
CC hydrolysis of cholesteryl esters and triglycerides that have been
CC internalized via receptor-mediated endocytosis of lipoprotein
CC particles. In venom, the biological contribution is unknown.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a sterol ester + H2O = a fatty acid + a sterol + H(+);
CC Xref=Rhea:RHEA:10100, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15889, ChEBI:CHEBI:28868, ChEBI:CHEBI:35915; EC=3.1.1.13;
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; JU173770; AFJ49296.1; -; mRNA.
DR AlphaFoldDB; J3SDX8; -.
DR SMR; J3SDX8; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004771; F:sterol esterase activity; IEA:UniProtKB-EC.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR025483; Lipase_euk.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR PIRSF; PIRSF000862; Steryl_ester_lip; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00120; LIPASE_SER; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; Hydrolase; Lipid degradation; Lipid metabolism; Secreted;
KW Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..400
FT /note="Putative lysosomal acid lipase/cholesteryl ester
FT hydrolase"
FT /id="PRO_0000422920"
FT DOMAIN 78..378
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT ACT_SITE 172
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT ACT_SITE 372
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT CARBOHYD 34
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 129
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 159
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 271
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 400 AA; 45807 MW; 2505F2E4A230D911 CRC64;
MWRLIIIAIL FQGLVNSAML ERRKRGVDPE TAMNISEIIL FRGYPSEEYE VVTGDGYILC
LNRIPYGKIS QKTKEPKPAV FLQHGLLADG SNWVTNLDYN SLGFALADAG FDVWLGNSRG
NTWSQKHINY TIKQKEFWMF SFNEMAMYDI PASVNFVLNK TGQEQLFYVG HSQGTTIGFI
AFSVLPELAK KIKMFFGLAP VMTVKFSSGG LVKLGELPEF LLKEIFGTKQ IFPQNAVIKW
LATHVCGQVL IDELCGNFFF LLCGFNEKNL NMSRVEIYST HCPAGTSVQN MLHWSQAVKS
GEVRAFDWGS RKENMAHYKQ PTPPPYKMER MLVPTALWTG GHDWLSDRKD IAILLTLIPN
LIYHKEIPEW EHLDFIWGLD APQRMFRDMI QMMHKVQYAH
