ID   PA2L_CAEEL              Reviewed;         174 AA.
AC   Q9U256;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Phospholipase A2-like protein Y52B11A.8;
DE   Flags: Precursor;
GN   ORFNames=Y52B11A.8;
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-49, 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-49, 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   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the phospholipase A2 family. {ECO:0000305}.
CC   -!- CAUTION: Although strongly related to the phospholipase A2 family, it
CC       lacks the conserved active Asp in position 129, which is replaced by a
CC       Val residue, suggesting that it has no activity. {ECO:0000305}.
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DR   EMBL; AL032654; CAB63390.1; -; Genomic_DNA.
DR   RefSeq; NP_492859.1; NM_060458.3.
DR   AlphaFoldDB; Q9U256; -.
DR   SMR; Q9U256; -.
DR   BioGRID; 38413; 1.
DR   IntAct; Q9U256; 2.
DR   STRING; 6239.Y52B11A.8; -.
DR   iPTMnet; Q9U256; -.
DR   EPD; Q9U256; -.
DR   PaxDb; Q9U256; -.
DR   PeptideAtlas; Q9U256; -.
DR   EnsemblMetazoa; Y52B11A.8.1; Y52B11A.8.1; WBGene00013127.
DR   GeneID; 173004; -.
DR   KEGG; cel:CELE_Y52B11A.8; -.
DR   UCSC; Y52B11A.8; c. elegans.
DR   CTD; 173004; -.
DR   WormBase; Y52B11A.8; CE20296; WBGene00013127; -.
DR   eggNOG; ENOG502SUNX; Eukaryota.
DR   GeneTree; ENSGT00970000196607; -.
DR   HOGENOM; CLU_1541500_0_0_1; -.
DR   InParanoid; Q9U256; -.
DR   OMA; CHDESAP; -.
DR   OrthoDB; 1299904at2759; -.
DR   PhylomeDB; Q9U256; -.
DR   PRO; PR:Q9U256; -.
DR   Proteomes; UP000001940; Chromosome I.
DR   Bgee; WBGene00013127; Expressed in adult organism and 4 other tissues.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004623; F:phospholipase A2 activity; IEA:InterPro.
DR   GO; GO:0050482; P:arachidonic acid secretion; IEA:InterPro.
DR   GO; GO:0006644; P:phospholipid metabolic process; IEA:InterPro.
DR   InterPro; IPR036444; PLipase_A2_dom_sf.
DR   InterPro; IPR033113; PLipase_A2_His_AS.
DR   SUPFAM; SSF48619; SSF48619; 1.
DR   PROSITE; PS00118; PA2_HIS; 1.
PE   1: Evidence at protein level;
KW   Glycoprotein; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..174
FT                   /note="Phospholipase A2-like protein Y52B11A.8"
FT                   /id="PRO_0000248532"
FT   REGION          137..174
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        49
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:12754521,
FT                   ECO:0000269|PubMed:17761667"
FT   CARBOHYD        143
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   174 AA;  18768 MW;  EBFF0A754D375D4F CRC64;
     MRGLLVATWI FVSVAASATP TTTTKSPPPT TTTLSPQILK AKLPPVVKNA TWECGTDEFT
     KSISEGEIQA KCPKLRDHIN SCCLQHDGCY EAQSGQKFCD DTFCSCLERR SRSSKSCHDE
     SAPLFCDLVR TFGDGAYEAS GPNASTTEES PAEKDDYDYE SHVAGLNATP SSST