ID   ASP6_CAEEL              Reviewed;         389 AA.
AC   O01530;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 146.
DE   RecName: Full=Aspartic protease 6 {ECO:0000303|PubMed:17081123, ECO:0000312|WormBase:F21F8.7};
DE            EC=3.4.23.- {ECO:0000250|UniProtKB:Q9N9H4};
DE   Flags: Precursor;
GN   Name=asp-6 {ECO:0000303|PubMed:17081123, ECO:0000312|WormBase:F21F8.7};
GN   ORFNames=F21F8.7 {ECO:0000312|WormBase:F21F8.7};
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   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, IDENTIFICATION BY MASS
RP   SPECTROMETRY, AND GLYCOSYLATION.
RX   PubMed=17081123; DOI=10.1515/bc.2006.186;
RA   Lochnit G., Grabitzki J., Henkel B., Tavernarakis N., Geyer R.;
RT   "First identification of a phosphorylcholine-substituted protein from
RT   Caenorhabditis elegans: isolation and characterization of the aspartyl
RT   protease ASP-6.";
RL   Biol. Chem. 387:1487-1493(2006).
CC   -!- FUNCTION: Aspartic protease. {ECO:0000250|UniProtKB:Q9N9H4}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17081123}.
CC       Note=Secreted into the pseudocoelom. {ECO:0000269|PubMed:17081123}.
CC   -!- TISSUE SPECIFICITY: Expressed in intestine, muscles, pharynx and
CC       hypodermis. {ECO:0000269|PubMed:17081123}.
CC   -!- PTM: Glycosylated. Has phosphorylcholine-substituted oligosaccharide N-
CC       glycans. {ECO:0000269|PubMed:17081123}.
CC   -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
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DR   EMBL; FO080569; CCD64751.1; -; Genomic_DNA.
DR   PIR; T29410; T29410.
DR   RefSeq; NP_505133.1; NM_072732.7.
DR   AlphaFoldDB; O01530; -.
DR   SMR; O01530; -.
DR   BioGRID; 44250; 11.
DR   DIP; DIP-24896N; -.
DR   IntAct; O01530; 3.
DR   MINT; O01530; -.
DR   STRING; 6239.F21F8.7; -.
DR   MEROPS; A01.A71; -.
DR   EPD; O01530; -.
DR   PaxDb; O01530; -.
DR   PeptideAtlas; O01530; -.
DR   EnsemblMetazoa; F21F8.7.1; F21F8.7.1; WBGene00000219.
DR   GeneID; 179209; -.
DR   KEGG; cel:CELE_F21F8.7; -.
DR   UCSC; F21F8.7.1; c. elegans.
DR   CTD; 179209; -.
DR   WormBase; F21F8.7; CE09542; WBGene00000219; asp-6.
DR   eggNOG; KOG1339; Eukaryota.
DR   HOGENOM; CLU_013253_3_4_1; -.
DR   InParanoid; O01530; -.
DR   OMA; WYGGVQS; -.
DR   OrthoDB; 753343at2759; -.
DR   PhylomeDB; O01530; -.
DR   Reactome; R-CEL-2132295; MHC class II antigen presentation.
DR   Reactome; R-CEL-5683826; Surfactant metabolism.
DR   PRO; PR:O01530; -.
DR   Proteomes; UP000001940; Chromosome V.
DR   Bgee; WBGene00000219; Expressed in adult organism and 4 other tissues.
DR   GO; GO:0005615; C:extracellular space; IDA:WormBase.
DR   GO; GO:0005764; C:lysosome; IBA:GO_Central.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IBA:GO_Central.
DR   GO; GO:0008219; P:cell death; IBA:GO_Central.
DR   GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR   CDD; cd05471; pepsin_like; 1.
DR   Gene3D; 2.40.70.10; -; 2.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
DR   InterPro; IPR001969; Aspartic_peptidase_AS.
DR   InterPro; IPR034164; Pepsin-like_dom.
DR   InterPro; IPR033121; PEPTIDASE_A1.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   PANTHER; PTHR47966; PTHR47966; 1.
DR   Pfam; PF00026; Asp; 1.
DR   PRINTS; PR00792; PEPSIN.
DR   SUPFAM; SSF50630; SSF50630; 1.
DR   PROSITE; PS00141; ASP_PROTEASE; 1.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
PE   1: Evidence at protein level;
KW   Aspartyl protease; Disulfide bond; Glycoprotein; Hydrolase; Protease;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000255"
FT   CHAIN           16..389
FT                   /note="Aspartic protease 6"
FT                   /id="PRO_0000307864"
FT   DOMAIN          71..384
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT   ACT_SITE        89
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT   ACT_SITE        277
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT   CARBOHYD        74
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        102..106
FT                   /evidence="ECO:0000250|UniProtKB:P0DJD7"
FT   DISULFID        312..344
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
SQ   SEQUENCE   389 AA;  41520 MW;  38B1DC51910FBF84 CRC64;
     MKTFILLAVL GLASASVHQH KIVWRESKKM GMIRTGQYPA YLEYQRNLRA VSPNVLANLP
     QNVNDFGDFE YLGNITIGTP DQGFIVVLDT GSSNLWIPGP TCKTNCKTKS KFDSTASSTF
     VKNGKSWTIQ YGSGDAAGIL GQDTVRFGAK GDSQLSVPTT TFGIASKISA DFKNDATDGI
     LGLAFTSLAV DGVVPPLINA INQGILDQPL FSVWLEHRGA ANNVGGGVFT YGAIDTTNCG
     ALVAYQPLSS ATYYQFKAAG FKLGSYSNTK TVDVISDTGT SFLGGPQSVV DGLAKAAGAT
     YDDFNEVYFI DCAAQPGTLD ITIGTNTYSI QPVNYIVDAG NGQCLFAAFP FDFGGFGPSW
     ILGDPFIRQY CNIYDIGNKR MGFAPSLQK