ASP1_CAEEL
ID ASP1_CAEEL Reviewed; 396 AA.
AC G5EEI4; O76830;
DT 13-FEB-2019, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Aspartic protease 1 {ECO:0000303|PubMed:10854422, ECO:0000312|WormBase:Y39B6A.20};
DE EC=3.4.23.- {ECO:0000250|UniProtKB:Q9N9H4};
DE Flags: Precursor;
GN Name=asp-1 {ECO:0000303|PubMed:10854422, ECO:0000312|WormBase:Y39B6A.20};
GN ORFNames=Y39B6A.20 {ECO:0000312|WormBase:Y39B6A.20};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|EMBL:AAF19445.1};
RN [1] {ECO:0000312|EMBL:AAF19445.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], SUBCELLULAR LOCATION, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=10854422; DOI=10.1074/jbc.m000956200;
RA Tcherepanova I., Bhattacharyya L., Rubin C.S., Freedman J.H.;
RT "Aspartic proteases from the nematode Caenorhabditis elegans. Structural
RT organization and developmental and cell-specific expression of asp-1.";
RL J. Biol. Chem. 275:26359-26369(2000).
RN [2] {ECO:0000312|EMBL:CAA08899.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:CAA08899.1};
RA Kraev A.S.;
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [3] {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 [4] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12410314; DOI=10.1038/nature01108;
RA Syntichaki P., Xu K., Driscoll M., Tavernarakis N.;
RT "Specific aspartyl and calpain proteases are required for neurodegeneration
RT in C. elegans.";
RL Nature 419:939-944(2002).
RN [5] {ECO:0000305}
RP FUNCTION, INTERACTION WITH B.THURINGIENSIS CRY6AA, INDUCTION, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=26795495; DOI=10.1371/journal.ppat.1005389;
RA Zhang F., Peng D., Cheng C., Zhou W., Ju S., Wan D., Yu Z., Shi J.,
RA Deng Y., Wang F., Ye X., Hu Z., Lin J., Ruan L., Sun M.;
RT "Bacillus thuringiensis Crystal Protein Cry6Aa Triggers Caenorhabditis
RT elegans Necrosis Pathway Mediated by Aspartic Protease (ASP-1).";
RL PLoS Pathog. 12:E1005389-E1005389(2016).
CC -!- FUNCTION: Aspartic protease, which is part of the necrosis cell death
CC pathway (PubMed:26795495, PubMed:12410314). Promotes B.thuringiensis
CC Cry6Aa stability by preventing its proteolysis by host gut proteases.
CC Required for Cry6Aa-induced necrotic death of intestinal cells
CC (PubMed:26795495). Cry6Aa uptake into the host intestinal cells
CC triggers an increase in intracellular Ca(2+) levels leading to lysosome
CC rupture and to the subsequent release of asp-1 which leads to necrosis
CC (PubMed:26795495). {ECO:0000269|PubMed:12410314,
CC ECO:0000269|PubMed:26795495}.
CC -!- SUBUNIT: Interacts with B.thuringiensis endotoxin Cry6Aa; the
CC interaction prevents Cry6Aa proteolysis by host gut proteases.
CC {ECO:0000269|PubMed:26795495}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10854422}. Lysosome
CC {ECO:0000305|PubMed:10854422}. Secreted {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: Expression begins at the 2-fold embryonic stage
CC and continues throughout the larval stages (at protein level)
CC (PubMed:10854422). During the early stages of larval development,
CC specifically expressed in the intestinal cells with the highest levels
CC in the posterior intestinal cells int7 and int8 (PubMed:10854422). Not
CC expressed in adults (PubMed:10854422). {ECO:0000269|PubMed:10854422}.
CC -!- INDUCTION: Up-regulated by B.thuringiensis endotoxin Cry6Aa (at protein
CC level). {ECO:0000269|PubMed:26795495}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown partially prevents
CC neuronal degeneration in a mec-4(u231), deg-1(u38) or gsa-1(Q227L)
CC gain-of-function mutant background. {ECO:0000269|PubMed:12410314}.
CC -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000255,
CC ECO:0000255|PROSITE-ProRule:PRU01103, ECO:0000255|RuleBase:RU000454}.
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DR EMBL; AF208526; AAF19442.1; -; mRNA.
DR EMBL; AJ009861; CAA08899.1; -; mRNA.
DR EMBL; AF210248; AAF19445.1; -; Genomic_DNA.
DR EMBL; BX284605; CAC51056.1; -; Genomic_DNA.
DR PIR; T45033; T45033.
DR RefSeq; NP_741677.1; NM_171587.4.
DR AlphaFoldDB; G5EEI4; -.
DR SMR; G5EEI4; -.
DR IntAct; G5EEI4; 4.
DR MINT; G5EEI4; -.
DR STRING; 6239.Y39B6A.20.1; -.
DR MEROPS; A01.053; -.
DR World-2DPAGE; 0011:Q9TVS4; -.
DR EPD; G5EEI4; -.
DR PaxDb; G5EEI4; -.
DR PeptideAtlas; G5EEI4; -.
DR EnsemblMetazoa; Y39B6A.20.1; Y39B6A.20.1; WBGene00000214.
DR GeneID; 180251; -.
DR KEGG; cel:CELE_Y39B6A.20; -.
DR CTD; 180251; -.
DR WormBase; Y39B6A.20; CE21681; WBGene00000214; asp-1.
DR eggNOG; KOG1339; Eukaryota.
DR GeneTree; ENSGT00970000195900; -.
DR HOGENOM; CLU_013253_3_4_1; -.
DR InParanoid; G5EEI4; -.
DR OMA; NIMDMSI; -.
DR OrthoDB; 1619495at2759; -.
DR PhylomeDB; G5EEI4; -.
DR Reactome; R-CEL-2132295; MHC class II antigen presentation.
DR Reactome; R-CEL-5683826; Surfactant metabolism.
DR SignaLink; G5EEI4; -.
DR PRO; PR:G5EEI4; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00000214; Expressed in larva and 5 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0098591; C:external side of apical plasma membrane; IDA:WormBase.
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:0012501; P:programmed cell death; IEA:UniProtKB-KW.
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; Cytoplasm; Disulfide bond; Glycoprotein; Hydrolase;
KW Lysosome; Necrosis; Protease; Reference proteome; Secreted; Signal.
FT SIGNAL 1..15
FT /evidence="ECO:0000255"
FT CHAIN 16..396
FT /note="Aspartic protease 1"
FT /evidence="ECO:0000255"
FT /id="PRO_5015092016"
FT DOMAIN 68..389
FT /note="Peptidase A1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT ACT_SITE 86
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT ACT_SITE 278
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT CARBOHYD 71
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 99..104
FT /evidence="ECO:0000250|UniProtKB:P0DJD7"
FT DISULFID 313..349
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT CONFLICT 7..11
FT /note="LALVA -> SPLW (in Ref. 2; CAA08899)"
FT /evidence="ECO:0000305"
FT CONFLICT 186
FT /note="P -> T (in Ref. 2; CAA08899)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 396 AA; 42693 MW; 8F79D757A650C0F4 CRC64;
MQTFVLLALV AACSAAVIQV PTHKTESLRA KLIKEGKYTA FLASQHAARA QQLNTGFQPF
VDYFDDFYLG NITLGTPPQP ATVVLDTGSS NLWVIDAACK TQACNGYPDS GYTKQKFDTT
KSTTFVKETR KFSIQYGSGS CNGYLGKDVL NFGGLTVQSQ EFGVSTHLAD VFGYQPVDGI
LGLGWPALAV DQVVPPMQNL IAQKQLDAPL FTVWLDRNLQ IAQGTPGGLI TYGAIDTVNC
AKQVTYVPLS AKTYWQFPLD AFAVGTYSET KKDQVISDTG TSWLGAPNTI VSAIVKQTKA
VFDWSTELYT VDCSTMKTQP DLIFTIGGAQ FPVKSVEYVL DLQLGGGKCA LAVFSMGSGG
FGPSWILGDT FIRQYCNVYD IGNGQIGFAT AVHKGL
