ID A0A0V1NY30_9BILA Unreviewed; 483 AA.
AC A0A0V1NY30;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 03-MAY-2023, entry version 19.
DE SubName: Full=Pancreatic triacylglycerol lipase {ECO:0000313|EMBL:KRZ88806.1};
GN Name=PNLIP {ECO:0000313|EMBL:KRZ88806.1};
GN ORFNames=T08_14685 {ECO:0000313|EMBL:KRZ88806.1};
OS Trichinella sp. T8.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92180 {ECO:0000313|EMBL:KRZ88806.1, ECO:0000313|Proteomes:UP000054924};
RN [1] {ECO:0000313|EMBL:KRZ88806.1, ECO:0000313|Proteomes:UP000054924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS272 {ECO:0000313|EMBL:KRZ88806.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000256|ARBA:ARBA00010701, ECO:0000256|RuleBase:RU004262}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRZ88806.1}.
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DR EMBL; JYDM01000079; KRZ88806.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1NY30; -.
DR STRING; 92180.A0A0V1NY30; -.
DR Proteomes; UP000054924; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:InterPro.
DR GO; GO:0016298; F:lipase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR013818; Lipase.
DR InterPro; IPR016272; Lipase_LIPH.
DR InterPro; IPR000734; TAG_lipase.
DR PANTHER; PTHR11610; LIPASE; 1.
DR Pfam; PF00151; Lipase; 1.
DR PIRSF; PIRSF000865; Lipoprotein_lipase_LIPH; 1.
DR PRINTS; PR00821; TAGLIPASE.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|PIRSR:PIRSR000865-2};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR000865-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000054924};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..483
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006883810"
FT DOMAIN 40..357
FT /note="Lipase"
FT /evidence="ECO:0000259|Pfam:PF00151"
FT ACT_SITE 184
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000865-1"
FT ACT_SITE 203
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR000865-1"
FT ACT_SITE 289
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR000865-1"
FT BINDING 217
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000865-2"
FT BINDING 219
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000865-2"
FT BINDING 222
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000865-2"
SQ SEQUENCE 483 AA; 53331 MW; B1861D43662B5A36 CRC64;
MAMSAVVSSW LFPVIFTTTL AALVENYQTN KPGQELERAC YNDVGCFDNA GSFKHMKVLP
QSPNEINTTF LLFTPESKTN GTILTKTLLL SNAKTEQVNW KNNMFVLVHG FGQFPFWMAP
MKDALVDQNN NVIIVDWTSG SVGPNYYQAA SNTRVVGAVL ADFVSTLVKS LKISLNRLTL
VGFSLGAHAC GFAGKNLSGL SLDPAGPLFS GKESEARLDS SDAEFVQCIH TNGQSFFRGG
LGSVQPMGHV DFYANGGLVQ SGCADGLEEI ILDLFHLNGT ILEELTCSHS QAPVLYIETI
KSSSFSQACQ FTSVSCDSPN SWFQGKCFNC IANGDLPAFG YKLTAQKQFK GQYYFTTLPK
NKHHETYCGK QYGFNIIPDQ AVKGSITLTL MFSNLHSMNF TFQHIDETLE ENSHAIKIGA
VPEFYPEITN ITIIYEKYSS WIWKNGPDEW VLKSLSLLDM ECNIHEVNPN VLVINKMATT
VDM
//