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Database: UniProt
Entry: T1JVP3_TETUR
LinkDB: T1JVP3_TETUR
Original site: T1JVP3_TETUR 
ID   T1JVP3_TETUR            Unreviewed;       431 AA.
AC   T1JVP3;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=Lipase {ECO:0000256|PIRNR:PIRNR000862};
OS   Tetranychus urticae (Two-spotted spider mite).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC   Acariformes; Trombidiformes; Prostigmata; Eleutherengona; Raphignathae;
OC   Tetranychoidea; Tetranychidae; Tetranychus.
OX   NCBI_TaxID=32264 {ECO:0000313|EnsemblMetazoa:tetur02g05320.1, ECO:0000313|Proteomes:UP000015104};
RN   [1] {ECO:0000313|Proteomes:UP000015104}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=London {ECO:0000313|Proteomes:UP000015104};
RA   Rombauts S.;
RL   Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:tetur02g05320.1}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (JUN-2015) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC       {ECO:0000256|ARBA:ARBA00010701, ECO:0000256|PIRNR:PIRNR000862}.
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DR   EMBL; CAEY01000795; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; T1JVP3; -.
DR   EnsemblMetazoa; tetur02g05320.1; tetur02g05320.1; tetur02g05320.
DR   eggNOG; KOG2624; Eukaryota.
DR   HOGENOM; CLU_010974_0_0_1; -.
DR   OMA; TRDEKFW; -.
DR   Proteomes; UP000015104; Unassembled WGS sequence.
DR   GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR006693; AB_hydrolase_lipase.
DR   InterPro; IPR025483; Lipase_euk.
DR   PANTHER; PTHR11005:SF163; LIPASE; 1.
DR   PANTHER; PTHR11005; LYSOSOMAL ACID LIPASE-RELATED; 1.
DR   Pfam; PF04083; Abhydro_lipase; 1.
DR   PIRSF; PIRSF000862; Steryl_ester_lip; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR000862};
KW   Lipid degradation {ECO:0000256|PIRNR:PIRNR000862};
KW   Lipid metabolism {ECO:0000256|PIRNR:PIRNR000862};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015104};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..431
FT                   /note="Lipase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004580699"
FT   DOMAIN          60..118
FT                   /note="Partial AB-hydrolase lipase"
FT                   /evidence="ECO:0000259|Pfam:PF04083"
FT   ACT_SITE        195
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000862-1"
FT   ACT_SITE        362
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000862-1"
FT   ACT_SITE        394
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000862-1"
SQ   SEQUENCE   431 AA;  48660 MW;  5A5EF86D0FD8283C CRC64;
     MICLFYITFY ISIVHKCCGV TVEKAGPAPI ESTNPTLAEE QAFLKLVGNG DPDEAASCGQ
     LIESRGFQYE RYYVTTKDGY ILQNFRIINR YAREARKTLK PVLLVHPLFT SCASWLFNSP
     AALGFLLANL GYDVWIINVR GTSYSTNHTH LDPEGNNPEF WDYSFYEIGI YDVTATVEHI
     KNETGFEKII VIAFSQGTLQ MITQMSLMPW FQDNYDIVIL ATPGGFVGEY GFFASIPNKP
     AQELFSLSNG PFPSDSASFL SSLSVLCAQQ LTNPICVTLV GTLGIDRKQL NASRLNVYVS
     LLDRTSNKNL LHIFQSVERD HLSFFDNGEV KNYALYGSAE PPEFPYYNIN PNKLIFMSGL
     NDQVIDQRNV QKFRNSLCDR VDTDHIIQDP YWNHGDYIIA LQAYEYFGSV VVDLIRERGD
     LTECKLKLSG N
//
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