ID   LIP1_CAEEL              Reviewed;         353 AA.
AC   Q9XTR8;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Lipase ZK262.3;
DE            EC=3.1.1.-;
DE   Flags: Precursor;
GN   ORFNames=ZK262.3;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [2]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-64, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   STRAIN=Bristol N2;
RX   PubMed=12754521; DOI=10.1038/nbt829;
RA   Kaji H., Saito H., Yamauchi Y., Shinkawa T., Taoka M., Hirabayashi J.,
RA   Kasai K., Takahashi N., Isobe T.;
RT   "Lectin affinity capture, isotope-coded tagging and mass spectrometry to
RT   identify N-linked glycoproteins.";
RL   Nat. Biotechnol. 21:667-672(2003).
RN   [3]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-64, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   STRAIN=Bristol N2;
RX   PubMed=17761667; DOI=10.1074/mcp.m600392-mcp200;
RA   Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T.,
RA   Taoka M., Takahashi N., Isobe T.;
RT   "Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis
RT   elegans and suggests an atypical translocation mechanism for integral
RT   membrane proteins.";
RL   Mol. Cell. Proteomics 6:2100-2109(2007).
CC   -!- FUNCTION: Probable lipase. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC       {ECO:0000305}.
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DR   EMBL; Z99288; CAB16546.1; -; Genomic_DNA.
DR   PIR; T27799; T27799.
DR   RefSeq; NP_507603.1; NM_075202.1.
DR   AlphaFoldDB; Q9XTR8; -.
DR   SMR; Q9XTR8; -.
DR   ESTHER; caeel-ZK262.3; Lipase_3.
DR   iPTMnet; Q9XTR8; -.
DR   EPD; Q9XTR8; -.
DR   PaxDb; Q9XTR8; -.
DR   PeptideAtlas; Q9XTR8; -.
DR   EnsemblMetazoa; ZK262.3.1; ZK262.3.1; WBGene00013950.
DR   GeneID; 191267; -.
DR   KEGG; cel:CELE_ZK262.3; -.
DR   UCSC; ZK262.3; c. elegans.
DR   CTD; 191267; -.
DR   WormBase; ZK262.3; CE19323; WBGene00013950; -.
DR   eggNOG; KOG4569; Eukaryota.
DR   GeneTree; ENSGT00940000174480; -.
DR   HOGENOM; CLU_032957_0_1_1; -.
DR   InParanoid; Q9XTR8; -.
DR   OMA; WYPGNMT; -.
DR   OrthoDB; 612344at2759; -.
DR   PhylomeDB; Q9XTR8; -.
DR   PRO; PR:Q9XTR8; -.
DR   Proteomes; UP000001940; Chromosome V.
DR   Bgee; WBGene00013950; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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; IPR002921; Fungal_lipase-like.
DR   Pfam; PF01764; Lipase_3; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   PROSITE; PS00120; LIPASE_SER; 1.
PE   1: Evidence at protein level;
KW   Disulfide bond; Glycoprotein; Hydrolase; Lipid degradation;
KW   Lipid metabolism; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..353
FT                   /note="Lipase ZK262.3"
FT                   /id="PRO_0000248513"
FT   ACT_SITE        163
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        221
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT   ACT_SITE        306
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT   CARBOHYD        32
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        64
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:12754521,
FT                   ECO:0000269|PubMed:17761667"
FT   CARBOHYD        267
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        277..288
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   353 AA;  38743 MW;  360C82827C8CE241 CRC64;
     MPKNLRFSVF LLFLLCINSV FGEFGPEDAQ YNETEARMLL SLSAAAYSLD VTPCIGRTFS
     PAENQTLLST FSVRCDFVGN PCAGYIVVSD VLQQITVVFR GTKTSSQLLL EGWTTLKPSS
     DFYGMGLVNT YFRSGHEKTW QYVQDALSIS QYRNYDVYVT GHSLGGALAG LCAPRIVHDG
     LRQSQKIKVV TFGEPRVGNI EFSRAYDQLV PYSFRVVHSG DVVPHLPGCV KDLSYTPPAG
     SDGSMPCDPV STNGGYHHAI EIWYPGNMTQ GDPFMVCTGL PRDEDFGCSD SLKVNLGDTN
     QGVWDHRNYF GVEVPDFGKG GCDPSMTFKG PPTKTGVLSL VGSVFGRKRR SIR