AED1_ARATH
ID AED1_ARATH Reviewed; 464 AA.
AC Q9LEW3; Q8H7H9;
DT 13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Aspartyl protease AED1 {ECO:0000303|PubMed:24755512};
DE EC=3.4.23.- {ECO:0000305};
DE AltName: Full=Apoplastic EDS1-dependent protein 1 {ECO:0000303|PubMed:24755512};
DE Flags: Precursor;
GN Name=AED1 {ECO:0000303|PubMed:24755512};
GN OrderedLocusNames=At5g10760 {ECO:0000312|Araport:AT5G10760};
GN ORFNames=T30N20.30 {ECO:0000312|EMBL:CAB96831.1};
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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].
RA Stracke R., Palme K.;
RT "Signal peptide selection derived cDNAs from Arabidopsis thaliana leaves
RT and guard cells.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP GENE FAMILY.
RX PubMed=16381599; DOI=10.2174/138920305774933268;
RA Faro C., Gal S.;
RT "Aspartic proteinase content of the Arabidopsis genome.";
RL Curr. Protein Pept. Sci. 6:493-500(2005).
RN [7]
RP FUNCTION, INDUCTION, 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 -!- FUNCTION: Aspartyl protease involved in a homeostatic feedback
CC mechanism regulating systemic immunity. Has only mild or no influence
CC on local defenses. Acts downstream of salicylic acid to suppress
CC systemic immunity. {ECO:0000269|PubMed:24755512}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast
CC {ECO:0000269|PubMed:24755512}.
CC -!- INDUCTION: Up-regulated locally and systematically during systemic
CC acquired resistance (SAR) and locally by salicylic acid. The local
CC induction is independent of EDS1 while the systemic induction is EDS1-
CC dependent. {ECO:0000269|PubMed:24755512}.
CC -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
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DR EMBL; AL365234; CAB96831.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91593.1; -; Genomic_DNA.
DR EMBL; AF083666; AAN60226.1; -; mRNA.
DR EMBL; AY072168; AAL59990.1; -; mRNA.
DR EMBL; AY133788; AAM91722.1; -; mRNA.
DR EMBL; AK226446; BAE98588.1; -; mRNA.
DR PIR; T50785; T50785.
DR RefSeq; NP_196637.1; NM_121114.4.
DR AlphaFoldDB; Q9LEW3; -.
DR SMR; Q9LEW3; -.
DR STRING; 3702.AT5G10760.1; -.
DR MEROPS; A01.A14; -.
DR PaxDb; Q9LEW3; -.
DR PRIDE; Q9LEW3; -.
DR ProteomicsDB; 244696; -.
DR EnsemblPlants; AT5G10760.1; AT5G10760.1; AT5G10760.
DR GeneID; 830943; -.
DR Gramene; AT5G10760.1; AT5G10760.1; AT5G10760.
DR KEGG; ath:AT5G10760; -.
DR Araport; AT5G10760; -.
DR TAIR; locus:2183715; AT5G10760.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_005738_5_2_1; -.
DR InParanoid; Q9LEW3; -.
DR OMA; GPCTQLN; -.
DR OrthoDB; 753343at2759; -.
DR PhylomeDB; Q9LEW3; -.
DR PRO; PR:Q9LEW3; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LEW3; baseline and differential.
DR GO; GO:0048046; C:apoplast; HDA:TAIR.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0009627; P:systemic acquired resistance; IMP: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; PS00141; ASP_PROTEASE; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 2: Evidence at transcript level;
KW Apoplast; Aspartyl protease; Disulfide bond; Hydrolase; Protease;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..464
FT /note="Aspartyl protease AED1"
FT /evidence="ECO:0000255"
FT /id="PRO_5005942997"
FT DOMAIN 132..460
FT /note="Peptidase A1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT ACT_SITE 150
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT ACT_SITE 345
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT DISULFID 384..425
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT CONFLICT 209
FT /note="V -> G (in Ref. 3; AAN60226)"
FT /evidence="ECO:0000305"
FT CONFLICT 405
FT /note="S -> G (in Ref. 3; AAN60226)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 464 AA; 49474 MW; 810E09A25FB2B68B CRC64;
MSIMRNFLSM IIMLCVCLNW CFAEGAEKSD SGKVLDSYTI QVSSLFPSSS SCVPSSKASN
TKSSLRVVHM HGACSHLSSD ARVDHDEIIR RDQARVESIY SKLSKNSANE VSEAKSTELP
AKSGITLGSG NYIVTIGIGT PKHDLSLVFD TGSDLTWTQC EPCLGSCYSQ KEPKFNPSSS
STYQNVSCSS PMCEDAESCS ASNCVYSIVY GDKSFTQGFL AKEKFTLTNS DVLEDVYFGC
GENNQGLFDG VAGLLGLGPG KLSLPAQTTT TYNNIFSYCL PSFTSNSTGH LTFGSAGISE
SVKFTPISSF PSAFNYGIDI IGISVGDKEL AITPNSFSTE GAIIDSGTVF TRLPTKVYAE
LRSVFKEKMS SYKSTSGYGL FDTCYDFTGL DTVTYPTIAF SFAGSTVVEL DGSGISLPIK
ISQVCLAFAG NDDLPAIFGN VQQTTLDVVY DVAGGRVGFA PNGC
