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 27-MAR-2024, entry version 117.
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; 46.
DR STRING; 6239.F09B12.3.1; -.
DR iPTMnet; O62146; -.
DR EPD; O62146; -.
DR PaxDb; 6239-F09B12-3; -.
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 AGR; WB:WBGene00008607; -.
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; 180150at2759; -.
DR PhylomeDB; O62146; -.
DR PRO; PR:O62146; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00008607; Expressed in larva and 4 other cell types or 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 Gene3D; 3.60.60.30; -; 1.
DR InterPro; IPR007000; PLipase_B-like.
DR PANTHER; PTHR12370:SF7; PHOSPHOLIPASE B-LIKE 2-RELATED; 1.
DR PANTHER; PTHR12370; PHOSPHOLIPASE B-RELATED; 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
//
