ID A0A0V0Y6J8_TRIPS Unreviewed; 502 AA.
AC A0A0V0Y6J8;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Lipase member H {ECO:0000313|EMBL:KRX95869.1};
DE Flags: Fragment;
GN Name=LIPH {ECO:0000313|EMBL:KRX95869.1};
GN ORFNames=T4E_159 {ECO:0000313|EMBL:KRX95869.1};
OS Trichinella pseudospiralis (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6337 {ECO:0000313|EMBL:KRX95869.1, ECO:0000313|Proteomes:UP000054815};
RN [1] {ECO:0000313|EMBL:KRX95869.1, ECO:0000313|Proteomes:UP000054815}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS141 {ECO:0000313|EMBL:KRX95869.1};
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:KRX95869.1}.
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DR EMBL; JYDU01000050; KRX95869.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0Y6J8; -.
DR Proteomes; UP000054815; 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:SF178; FI22312P1; 1.
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:UP000054815};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 58..380
FT /note="Lipase"
FT /evidence="ECO:0000259|Pfam:PF00151"
FT ACT_SITE 203
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000865-1"
FT ACT_SITE 222
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR000865-1"
FT ACT_SITE 308
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR000865-1"
FT BINDING 236
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000865-2"
FT BINDING 238
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000865-2"
FT BINDING 241
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000865-2"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRX95869.1"
SQ SEQUENCE 502 AA; 55187 MW; 8DD2CC6B824A7AFD CRC64;
LLKTVNPNCE LTACTKAVMA LSAVVSGWLS SIIFTTTTLA AVVQNFQTNK PGEQLQRACY
KDVGCFDNAG SFKHMKVLPQ SPNEINTTFL LFTPESKTNA TILTKTLLLS SAKTEQVNWT
NDMFVLVHGF GQFPFWAAPM KDALVDQNNN VIIVDWTSGS IGPNYYQAAS NTRVVGAVLA
DFVSTLVKSF KISLNRLTLV GFSLGAHACG FAGKNLGGLS LDPAGPLFSG KESEARLDSS
DAEFVQCIHT NGQSFFKGGL GSVQPMGHVD FYANGGLVQS GCADGLEEII LDLFHLNGTI
LEELTCSHSQ APVLYIETIK SSSFSQACQF TSVSCDSPSS WFQGKCFNCI ANGDLPAFGY
KFKAQKQFKG QYYFTTLPKN NHHETYCGKQ YGFNIIPDQA VKGSITLTLM FNNLHSMNFT
FQHIDETLEQ NNHAIKIGAV PEFYPKITNI SIIYEKYSSW IWKNGPDEWV LKSLTLLDME
CNIHEVNPNI LVINKMATTV DM
//