ASP4_CAEEL
ID ASP4_CAEEL Reviewed; 444 AA.
AC Q21966;
DT 13-FEB-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Aspartic protease 4 {ECO:0000312|WormBase:R12H7.2};
DE EC=3.4.23.- {ECO:0000250|UniProtKB:Q9N9H4};
DE Flags: Precursor;
GN Name=asp-4 {ECO:0000312|WormBase:R12H7.2};
GN ORFNames=R12H7.2 {ECO:0000312|WormBase:R12H7.2};
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 FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP 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 [3] {ECO:0000305}
RP DISRUPTION PHENOTYPE.
RX PubMed=28101079; DOI=10.3389/fmicb.2016.02058;
RA Chen P.L., Chen Y.W., Ou C.C., Lee T.M., Wu C.J., Ko W.C., Chen C.S.;
RT "A Disease Model of Muscle Necrosis Caused by Aeromonas dhakensis Infection
RT in Caenorhabditis elegans.";
RL Front. Microbiol. 7:2058-2058(2016).
RN [4] {ECO:0000305}
RP FUNCTION.
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:12410314). Involved in neuronal cell degeneration
CC (PubMed:12410314). Involved in heat stress response (PubMed:26795495).
CC {ECO:0000269|PubMed:12410314, ECO:0000269|PubMed:26795495}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12410314}. Lysosome
CC {ECO:0000269|PubMed:12410314}. Secreted {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Highly expressed in intestine and to a lower extent
CC in body wall muscles, hypodermis and neurons.
CC {ECO:0000269|PubMed:12410314}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown prevents muscle
CC degeneration caused by bacterium A.dhakensis-mediated infection
CC (PubMed:28101079). RNAi-mediated knockdown prevents neuronal
CC degeneration in a mec-4(u231), deg-1(u38) or gsa-1(Q227L) gain-of-
CC function mutant background (PubMed:12410314).
CC {ECO:0000269|PubMed:12410314, ECO:0000269|PubMed:28101079}.
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; BX284606; CAA90633.1; -; Genomic_DNA.
DR PIR; T24204; T24204.
DR RefSeq; NP_510191.1; NM_077790.5.
DR AlphaFoldDB; Q21966; -.
DR SMR; Q21966; -.
DR STRING; 6239.R12H7.2; -.
DR MEROPS; A01.068; -.
DR EPD; Q21966; -.
DR PaxDb; Q21966; -.
DR PeptideAtlas; Q21966; -.
DR EnsemblMetazoa; R12H7.2.1; R12H7.2.1; WBGene00000217.
DR GeneID; 181444; -.
DR KEGG; cel:CELE_R12H7.2; -.
DR UCSC; R12H7.2; c. elegans.
DR CTD; 181444; -.
DR WormBase; R12H7.2; CE03567; WBGene00000217; asp-4.
DR eggNOG; KOG1339; Eukaryota.
DR GeneTree; ENSGT00940000155733; -.
DR HOGENOM; CLU_013253_3_0_1; -.
DR InParanoid; Q21966; -.
DR OMA; IGELWIL; -.
DR OrthoDB; 1619495at2759; -.
DR PhylomeDB; Q21966; -.
DR Reactome; R-CEL-2132295; MHC class II antigen presentation.
DR Reactome; R-CEL-5683826; Surfactant metabolism.
DR Reactome; R-CEL-6798695; Neutrophil degranulation.
DR PRO; PR:Q21966; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00000217; Expressed in adult organism and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005764; C:lysosome; IDA:WormBase.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; ISS:WormBase.
DR GO; GO:0008219; P:cell death; IBA:GO_Central.
DR GO; GO:0070265; P:necrotic cell death; IGI:WormBase.
DR GO; GO:0012501; P:programmed cell death; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR Gene3D; 2.40.70.10; -; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
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; 2.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 2: Evidence at transcript level;
KW Aspartyl protease; Cytoplasm; Disulfide bond; Glycoprotein; Hydrolase;
KW Lysosome; Necrosis; Protease; Reference proteome; Secreted; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..444
FT /note="Aspartic protease 4"
FT /evidence="ECO:0000255"
FT /id="PRO_5004199730"
FT DOMAIN 94..410
FT /note="Peptidase A1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT REGION 413..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 112
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT ACT_SITE 298
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT CARBOHYD 106
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 433
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 125..132
FT /evidence="ECO:0000250|UniProtKB:P0DJD7"
FT DISULFID 289..293
FT /evidence="ECO:0000250|UniProtKB:P0DJD7"
FT DISULFID 332..369
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
SQ SEQUENCE 444 AA; 49277 MW; 8C0CA701B4571E7F CRC64;
MNRCILLLLG ALLLVQGLHV HKRQQKLRTV SLKKQPTLRE TLLQAGSFET FAKHRHGYKK
YLKTNGNHHF DKYQALNVEG EIDELLRNYM DAQYFGTISI GTPAQNFTVI FDTGSSNLWI
PSKKCPFYDI ACMLHHRYDS KSSSTYKEDG RKMAIQYGTG SMKGFISKDS VCVAGVCAED
QPFAEATSEP GITFVAAKFD GILGMAYPEI AVLGVQPVFN TLFEQKKVPS NLFSFWLNRN
PDSEIGGEIT FGGIDSRRYV EPITYVPVTR KGYWQFKMDK VVGSGVLGCS NGCQAIADTG
TSLIAGPKAQ IEAIQNFIGA EPLIKGEYMI SCDKVPTLPP VSFVIGGQEF SLKGEDYVLK
VSQGGKTICL SGFMGIDLPE RVGELWILGD VFIGRYYSVF DFDQNRVGFA QAKTADGRPV
DPAPRPFRSV FDNESEESME QDDE
