ID   ASP17_CAEEL             Reviewed;         391 AA.
AC   Q8MYN5;
DT   16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 138.
DE   RecName: Full=Aspartic protease 17 {ECO:0000305};
DE            EC=3.4.23.- {ECO:0000250|UniProtKB:Q9LTW4};
DE   Flags: Precursor;
GN   Name=asp-17 {ECO:0000312|WormBase:Y39B6A.24};
GN   ORFNames=Y39B6A.24 {ECO:0000312|WormBase:Y39B6A.24};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN   [1] {ECO:0000312|Proteomes:UP000001940}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
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] {ECO:0000305}
RP   TISSUE SPECIFICITY, AND INDUCTION.
RX   PubMed=29664006; DOI=10.7554/elife.35037;
RA   Jiang W., Wei Y., Long Y., Owen A., Wang B., Wu X., Luo S., Dang Y.,
RA   Ma D.K.;
RT   "A genetic program mediates cold-warming response and promotes stress-
RT   induced phenoptosis in C. elegans.";
RL   Elife 7:0-0(2018).
CC   -!- FUNCTION: Aspartic proteinase. {ECO:0000250|UniProtKB:Q9LTW4}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in intestinal cells.
CC       {ECO:0000269|PubMed:29664006}.
CC   -!- INDUCTION: Induced in response to thermal stress in conditions where
CC       severe cold temperatures are followed by warmer temperatures
CC       (PubMed:29664006). In particular, induced in the warming phase (10 to
CC       22 degrees Celsius) during the cold (4 degrees Celsius) to warm (22
CC       degrees Celsius) temperature transition (PubMed:29664006).
CC       {ECO:0000269|PubMed:29664006}.
CC   -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01103}.
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DR   EMBL; BX284605; CAD31821.1; -; Genomic_DNA.
DR   RefSeq; NP_741673.1; NM_171583.3.
DR   AlphaFoldDB; Q8MYN5; -.
DR   SMR; Q8MYN5; -.
DR   STRING; 6239.Y39B6A.24; -.
DR   MEROPS; A01.A86; -.
DR   PaxDb; Q8MYN5; -.
DR   PeptideAtlas; Q8MYN5; -.
DR   EnsemblMetazoa; Y39B6A.24.1; Y39B6A.24.1; WBGene00012683.
DR   GeneID; 180250; -.
DR   KEGG; cel:CELE_Y39B6A.24; -.
DR   UCSC; Y39B6A.24.1; c. elegans.
DR   CTD; 180250; -.
DR   WormBase; Y39B6A.24; CE29865; WBGene00012683; asp-17.
DR   eggNOG; KOG1339; Eukaryota.
DR   GeneTree; ENSGT00970000195900; -.
DR   HOGENOM; CLU_013253_3_4_1; -.
DR   InParanoid; Q8MYN5; -.
DR   OMA; DEVVACQ; -.
DR   OrthoDB; 1619495at2759; -.
DR   PhylomeDB; Q8MYN5; -.
DR   Reactome; R-CEL-2132295; MHC class II antigen presentation.
DR   Reactome; R-CEL-5683826; Surfactant metabolism.
DR   PRO; PR:Q8MYN5; -.
DR   Proteomes; UP000001940; Chromosome V.
DR   Bgee; WBGene00012683; Expressed in adult organism and 1 other tissue.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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   2: Evidence at transcript 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..391
FT                   /note="Aspartic protease 17"
FT                   /id="PRO_5012067955"
FT   DOMAIN          65..385
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT   ACT_SITE        83
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT   ACT_SITE        274
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT   CARBOHYD        68
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        108
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        309..345
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
SQ   SEQUENCE   391 AA;  42754 MW;  206E0560185FD97B CRC64;
     MHLIFLLFLA PFCSAAVFQL PTKSTGSLRA KLIRAGKYQE FLITQHAARL NTISQPISDY
     SDEVYLGNFT VGTPPQPVSL VLDTGSANMW VIDASCDNMF CNGWIGSNYT RQKFDTSKSS
     SFSRENRKFS IQYGKGLCSG YLGTDTVGLG GGLTIRKQEL GIANKLDVDF AVQPMDGIFG
     LAWPALAVDQ ITPPMQNLIS QLDVPVFSVW LDRKIQASHG GSAGMITYGG IDTKNCDAGV
     TYVPLTAKTY WQFKMDGFAV GTYSQYGYNQ VISDTGSSWI SAPYAMINDI ATQTHATWDE
     MNEIYTVKCS TMKTQPDLVF TIGGALFPVK SVEYILDIGL DEGKCALAIS PLMASGFGPS
     WILGDVFIRQ YCNIYDIGNA RIGFANAHHS F