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PLBL2_CAEEL
ID   PLBL2_CAEEL             Reviewed;         582 AA.
AC   O62146;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 2.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Putative phospholipase B-like 2;
DE            EC=3.1.1.-;
DE   AltName: Full=LAMA-like protein 2;
DE   AltName: Full=Lamina ancestor homolog 2;
DE   Flags: Precursor;
GN   ORFNames=F09B12.3;
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-91, 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-178, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RX   PubMed=15888633; DOI=10.1093/glycob/cwi075;
RA   Fan X., She Y.-M., Bagshaw R.D., Callahan J.W., Schachter H., Mahuran D.J.;
RT   "Identification of the hydrophobic glycoproteins of Caenorhabditis
RT   elegans.";
RL   Glycobiology 15:952-964(2005).
RN   [4]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-91; ASN-141 AND ASN-178, AND
RP   IDENTIFICATION BY MASS 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: Putative phospholipase. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the phospholipase B-like family. {ECO:0000305}.
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DR   EMBL; Z83104; CAB05478.2; -; Genomic_DNA.
DR   PIR; T20630; T20630.
DR   RefSeq; NP_510509.2; NM_078108.4.
DR   AlphaFoldDB; O62146; -.
DR   SMR; O62146; -.
DR   BioGRID; 46502; 45.
DR   STRING; 6239.F09B12.3; -.
DR   iPTMnet; O62146; -.
DR   EPD; O62146; -.
DR   PaxDb; O62146; -.
DR   PeptideAtlas; O62146; -.
DR   EnsemblMetazoa; F09B12.3.1; F09B12.3.1; WBGene00008607.
DR   GeneID; 181605; -.
DR   KEGG; cel:CELE_F09B12.3; -.
DR   UCSC; F09B12.3; c. elegans.
DR   CTD; 181605; -.
DR   WormBase; F09B12.3; CE31469; WBGene00008607; -.
DR   eggNOG; KOG3774; Eukaryota.
DR   GeneTree; ENSGT00530000063509; -.
DR   HOGENOM; CLU_027106_4_0_1; -.
DR   InParanoid; O62146; -.
DR   OMA; ISQVTMS; -.
DR   OrthoDB; 724258at2759; -.
DR   PhylomeDB; O62146; -.
DR   PRO; PR:O62146; -.
DR   Proteomes; UP000001940; Chromosome X.
DR   Bgee; WBGene00008607; Expressed in larva and 4 other tissues.
DR   GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR   GO; GO:0004620; F:phospholipase activity; IBA:GO_Central.
DR   GO; GO:0009395; P:phospholipid catabolic process; IBA:GO_Central.
DR   InterPro; IPR007000; PLipase_B-like.
DR   PANTHER; PTHR12370; PTHR12370; 1.
DR   Pfam; PF04916; Phospholip_B; 1.
PE   1: Evidence at protein level;
KW   Disulfide bond; Glycoprotein; Hydrolase; Lipid degradation;
KW   Lipid metabolism; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..42
FT                   /evidence="ECO:0000255"
FT   CHAIN           43..582
FT                   /note="Putative phospholipase B-like 2"
FT                   /id="PRO_0000286114"
FT   CARBOHYD        91
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:12754521,
FT                   ECO:0000269|PubMed:17761667"
FT   CARBOHYD        141
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:17761667"
FT   CARBOHYD        178
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:15888633,
FT                   ECO:0000269|PubMed:17761667"
FT   CARBOHYD        224
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        318
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        502
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        139..146
FT                   /evidence="ECO:0000250"
FT   DISULFID        480..482
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   582 AA;  66638 MW;  BCFA3F167098E06F CRC64;
     MTRLIRSKKQ FLIRSLHSVF YYLGSLLHST FEMNVFIGLL LATVVASQSS EGRDESYTYK
     QLCIVDDKPQ VLDGFDCRNQ VAVARWQNAV NTTGWTFLEV ETKENYCPQL QAYSAGYLEG
     LLSKTVLTYH LKNAQEDYCK NFTGYCSRLS DFLTENQKWI QSSLETVAPD DLYWGAVNRT
     YHQVSGLIDA YEGREFKPRI TYELHPILYL NLNGDFYDLE KKLNKTRDPA FEQTGGKCSG
     LIKVAPGNAD LFISQVTMSG FQNMLRVIKL YKFGYDRQFY PGYASSFSSY PGLLYSSDDF
     ALQTSGLAVI ETTISVFNTS LFENTKPVGQ LPTWIRAIVS NQLARDAREW CKLYSLYNSG
     TYNNQWAVLD YKKFKPNQPL PKNGLFYVLE QMPGKIVYSD LTWFVEKYSY FPSYNIPFFK
     EITEISGFIG QAAKMGDWFK WGASPRAKIF ERDHGNVHDL DSLTALMRYN DYKNDEFSKC
     KCNPPYSAEA GISARGDLNP ANGTYEFPGQ GHVNHGALDY KGTNVELMKK LQFVAQGGPT
     WGKVPSFKWS EFDFKDKVNH VGHPDEWKFN TLVHKWETEI NA
 
 
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