AED3_ARATH
ID AED3_ARATH Reviewed; 449 AA.
AC O04496; Q94K53;
DT 13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Aspartyl protease AED3 {ECO:0000303|PubMed:24755512};
DE EC=3.4.23.- {ECO:0000305};
DE AltName: Full=Apoplastic EDS1-dependent protein 3 {ECO:0000303|PubMed:24755512};
DE Flags: Precursor;
GN Name=AED3 {ECO:0000303|PubMed:24755512};
GN OrderedLocusNames=At1g09750 {ECO:0000312|Araport:AT1G09750};
GN ORFNames=F21M12.13 {ECO:0000312|EMBL:AAB60729.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=24755512; DOI=10.1104/pp.114.239665;
RA Breitenbach H.H., Wenig M., Wittek F., Jorda L., Maldonado-Alconada A.M.,
RA Sarioglu H., Colby T., Knappe C., Bichlmeier M., Pabst E., Mackey D.,
RA Parker J.E., Vlot A.C.;
RT "Contrasting roles of the apoplastic aspartyl protease APOPLASTIC, ENHANCED
RT DISEASE SUSCEPTIBILITY1-DEPENDENT1 and LEGUME LECTIN-LIKE PROTEIN1 in
RT Arabidopsis systemic acquired resistance.";
RL Plant Physiol. 165:791-809(2014).
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast
CC {ECO:0000269|PubMed:24755512}.
CC -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC000132; AAB60729.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28488.1; -; Genomic_DNA.
DR EMBL; AY088375; AAM65914.1; -; mRNA.
DR EMBL; AF370291; AAK44106.2; -; mRNA.
DR EMBL; BT002332; AAN86165.1; -; mRNA.
DR PIR; D86231; D86231.
DR RefSeq; NP_563851.1; NM_100847.3.
DR AlphaFoldDB; O04496; -.
DR SMR; O04496; -.
DR STRING; 3702.AT1G09750.1; -.
DR MEROPS; A01.A36; -.
DR MEROPS; T03.008; -.
DR PaxDb; O04496; -.
DR PRIDE; O04496; -.
DR ProMEX; O04496; -.
DR ProteomicsDB; 243288; -.
DR EnsemblPlants; AT1G09750.1; AT1G09750.1; AT1G09750.
DR GeneID; 837504; -.
DR Gramene; AT1G09750.1; AT1G09750.1; AT1G09750.
DR KEGG; ath:AT1G09750; -.
DR Araport; AT1G09750; -.
DR TAIR; locus:2024306; AT1G09750.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_005738_5_1_1; -.
DR InParanoid; O04496; -.
DR OMA; YCLPSYR; -.
DR OrthoDB; 753343at2759; -.
DR PhylomeDB; O04496; -.
DR PRO; PR:O04496; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O04496; baseline and differential.
DR GO; GO:0048046; C:apoplast; HDA:TAIR.
DR GO; GO:0099503; C:secretory vesicle; HDA:TAIR.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR GO; GO:0043067; P:regulation of programmed cell death; IEA:EnsemblPlants.
DR GO; GO:0009627; P:systemic acquired resistance; IEP:TAIR.
DR Gene3D; 2.40.70.10; -; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR032799; TAXi_C.
DR InterPro; IPR032861; TAXi_N.
DR PANTHER; PTHR13683; PTHR13683; 1.
DR Pfam; PF14541; TAXi_C; 1.
DR Pfam; PF14543; TAXi_N; 1.
DR SUPFAM; SSF50630; SSF50630; 1.
DR PROSITE; PS00120; LIPASE_SER; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 1: Evidence at protein level;
KW Apoplast; Aspartyl protease; Disulfide bond; Glycoprotein; Hydrolase;
KW Nucleotide-binding; Protease; Reference proteome; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..449
FT /note="Aspartyl protease AED3"
FT /evidence="ECO:0000255"
FT /id="PRO_5005928664"
FT DOMAIN 104..444
FT /note="Peptidase A1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT ACT_SITE 122
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT ACT_SITE 328
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT CARBOHYD 140
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 148
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 184
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 211
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 297
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 353
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 132..138
FT /evidence="ECO:0000250|UniProtKB:P42210"
FT DISULFID 366..405
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
SQ SEQUENCE 449 AA; 47661 MW; A9AA6A0203DBC936 CRC64;
MASSSLHFFF FLTLLLPFTF TTATRDTCAT AAPDGSDDLS IIPINAKCSP FAPTHVSASV
IDTVLHMASS DSHRLTYLSS LVAGKPKPTS VPVASGNQLH IGNYVVRAKL GTPPQLMFMV
LDTSNDAVWL PCSGCSGCSN ASTSFNTNSS STYSTVSCST AQCTQARGLT CPSSSPQPSV
CSFNQSYGGD SSFSASLVQD TLTLAPDVIP NFSFGCINSA SGNSLPPQGL MGLGRGPMSL
VSQTTSLYSG VFSYCLPSFR SFYFSGSLKL GLLGQPKSIR YTPLLRNPRR PSLYYVNLTG
VSVGSVQVPV DPVYLTFDAN SGAGTIIDSG TVITRFAQPV YEAIRDEFRK QVNVSSFSTL
GAFDTCFSAD NENVAPKITL HMTSLDLKLP MENTLIHSSA GTLTCLSMAG IRQNANAVLN
VIANLQQQNL RILFDVPNSR IGIAPEPCN
