ASP3_CAEEL
ID ASP3_CAEEL Reviewed; 398 AA.
AC P55956; Q9TXI5;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2013, sequence version 3.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Aspartic protease 3 {ECO:0000312|WormBase:H22K11.1};
DE EC=3.4.23.- {ECO:0000250|UniProtKB:Q9N9H4};
DE Flags: Precursor;
GN Name=asp-3 {ECO:0000312|WormBase:H22K11.1};
GN ORFNames=H22K11.1 {ECO:0000312|WormBase:H22K11.1};
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 PROTEIN SEQUENCE OF 56-65.
RC STRAIN=Bristol N2;
RX PubMed=9150941; DOI=10.1002/elps.1150180337;
RA Bini L., Heid H., Liberatori S., Geier G., Pallini V., Zwilling R.;
RT "Two-dimensional gel electrophoresis of Caenorhabditis elegans homogenates
RT and identification of protein spots by microsequencing.";
RL Electrophoresis 18:557-562(1997).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP 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 [4]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-321, 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).
RN [5]
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 (Probable). 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 ECO:0000305}.
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 -!- DEVELOPMENTAL STAGE: Expressed at the 2-fold stage embryo.
CC {ECO:0000269|PubMed:12410314}.
CC -!- DISRUPTION PHENOTYPE: 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. {ECO:0000269|PubMed:12410314}.
CC -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
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DR EMBL; FO081559; CCD72415.2; -; Genomic_DNA.
DR PIR; T33383; T33383.
DR RefSeq; NP_509142.2; NM_076741.6.
DR AlphaFoldDB; P55956; -.
DR SMR; P55956; -.
DR BioGRID; 45876; 43.
DR DIP; DIP-26574N; -.
DR IntAct; P55956; 3.
DR STRING; 6239.H22K11.1; -.
DR MEROPS; A01.A69; -.
DR iPTMnet; P55956; -.
DR EPD; P55956; -.
DR PaxDb; P55956; -.
DR PeptideAtlas; P55956; -.
DR EnsemblMetazoa; H22K11.1.1; H22K11.1.1; WBGene00000216.
DR GeneID; 180947; -.
DR KEGG; cel:CELE_H22K11.1; -.
DR UCSC; H22K11.1; c. elegans.
DR CTD; 180947; -.
DR WormBase; H22K11.1; CE47856; WBGene00000216; asp-3.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_013253_3_1_1; -.
DR InParanoid; P55956; -.
DR OMA; IACRMHN; -.
DR OrthoDB; 1619495at2759; -.
DR PhylomeDB; P55956; -.
DR Reactome; R-CEL-2132295; MHC class II antigen presentation.
DR Reactome; R-CEL-5683826; Surfactant metabolism.
DR PRO; PR:P55956; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00000216; Expressed in larva 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; IBA:GO_Central.
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; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 1: Evidence at protein level;
KW Aspartyl protease; Cytoplasm; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Hydrolase; Lysosome; Necrosis; Protease; Reference proteome;
KW Secreted; Signal; Zymogen.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT PROPEP 18..55
FT /note="Removed in mature form"
FT /evidence="ECO:0000269|PubMed:9150941"
FT /id="PRO_0000025937"
FT CHAIN 56..398
FT /note="Aspartic protease 3"
FT /id="PRO_0000025938"
FT DOMAIN 69..392
FT /note="Peptidase A1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT ACT_SITE 87
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT ACT_SITE 279
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT CARBOHYD 321
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT DISULFID 100..107
FT /evidence="ECO:0000250|UniProtKB:P0DJD7"
FT DISULFID 313..351
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
SQ SEQUENCE 398 AA; 43399 MW; 5F03244C695E1F2F CRC64;
MSGRVFLLLA LVALASAIQR IKLEKRTYTR EQYKFGSIQE HLKAKYVPGY IPNKDAFNEG
LSDYSNAQYY GPVTIGTPPQ NFQVLFDTGS SNLWVPCANC PFGDIACRMH NRFDCKKSSS
CTATGASFEI QYGTGSMKGT VDNDVVCFGH DTTYCTDKNQ GLACATSEPG ITFVAAKFDG
IFGMGWDTIS VNKISQPMDQ IFANSAICKN QLFAFWLSRD ANDITNGGEI TLCDTDPNHY
VGNIAWEPLV SEDYWRIKLA SVVIDGTTYT SGPIDSIVDT GTSLLTGPTD VIKKIQHKIG
GIPLFNGEYE VECSKIPSLP NITFNLGGQN FDLQGKDYIL QMSNGNGGST CLSGFMGMDI
PAPAGPLWIL GDVFIGRFYS VFDHGNKRVG FATSRTGK
