ALEU_ARATH
ID ALEU_ARATH Reviewed; 358 AA.
AC Q8H166; Q9LL83; Q9S9A9;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Thiol protease aleurain;
DE Short=AtALEU;
DE EC=3.4.22.16;
DE AltName: Full=Senescence-associated gene product 2;
DE Flags: Precursor;
GN Name=ALEU; Synonyms=AALP, SAG2; OrderedLocusNames=At5g60360;
GN ORFNames=MUF9.1;
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 [MRNA], SUBCELLULAR LOCATION, AND INTERACTION WITH
RP VSR1.
RX PubMed=10871276; DOI=10.1083/jcb.149.7.1335;
RA Ahmed S.U., Rojo E., Kovaleva V., Venkataraman S., Dombrowski J.E.,
RA Matsuoka K., Raikhel N.V.;
RT "The plant vacuolar sorting receptor AtELP is involved in transport of
RT NH(2)-terminal propeptide-containing vacuolar proteins in Arabidopsis
RT thaliana.";
RL J. Cell Biol. 149:1335-1344(2000).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9679202; DOI=10.1093/dnares/5.2.131;
RA Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence
RT features of the regions of 1,381,565 bp covered by twenty one physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:131-145(1998).
RN [4]
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 [5]
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 [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 137-231, INDUCTION, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Landsberg erecta; TISSUE=Leaf;
RX PubMed=8518555; DOI=10.2307/3869710;
RA Hensel L.L., Grbic V., Baumgarten D.A., Bleecker A.B.;
RT "Developmental and age-related processes that influence the longevity and
RT senescence of photosynthetic tissues in Arabidopsis.";
RL Plant Cell 5:553-564(1993).
RN [8]
RP TISSUE SPECIFICITY.
RX PubMed=9225474; DOI=10.1046/j.1365-313x.1997.11061359.x;
RA Rogers S.W., Burks M., Rogers J.C.;
RT "Monoclonal antibodies to barley aleurain and homologs from other plants.";
RL Plant J. 11:1359-1368(1997).
RN [9]
RP INDUCTION.
RX PubMed=9617813; DOI=10.1023/a:1005934428906;
RA Weaver L.M., Gan S., Quirino B., Amasino R.M.;
RT "A comparison of the expression patterns of several senescence-associated
RT genes in response to stress and hormone treatment.";
RL Plant Mol. Biol. 37:455-469(1998).
RN [10]
RP SUBCELLULAR LOCATION.
RX PubMed=12730271; DOI=10.1093/jxb/erg160;
RA Flueckiger R., De Caroli M., Piro G., Dalessandro G., Neuhaus J.-M.,
RA Di Sansebastiano G.-P.;
RT "Vacuolar system distribution in Arabidopsis tissues, visualized using GFP
RT fusion proteins.";
RL J. Exp. Bot. 54:1577-1584(2003).
RN [11]
RP INDUCTION.
RX PubMed=14617064; DOI=10.1046/j.1365-313x.2003.01908.x;
RA Gepstein S., Sabehi G., Carp M.-J., Hajouj T., Nesher M.F.O., Yariv I.,
RA Dor C., Bassani M.;
RT "Large-scale identification of leaf senescence-associated genes.";
RL Plant J. 36:629-642(2003).
CC -!- FUNCTION: May play a role in proteolysis leading to mobilization of
CC nitrogen during senescence and starvation.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of proteins, acting as an aminopeptidase (notably,
CC cleaving Arg-|-Xaa bonds) as well as an endopeptidase.; EC=3.4.22.16;
CC -!- SUBUNIT: Interacts with VSR1/BP80B. {ECO:0000269|PubMed:10871276}.
CC -!- SUBCELLULAR LOCATION: Vacuole {ECO:0000269|PubMed:10871276,
CC ECO:0000269|PubMed:12730271}. Note=Predominantly vacuolar. From the
CC Golgi apparatus, transported to the lytic vacuole (LV) in clathrin-
CC coated vesicles (CCVs) via the prevacuolar compartment (PVC). In root
CC elongating cells and stomata, localized in central vacuole and in small
CC compartments (LVs, PVCs, Golgi bodies or small vacuoles). Limited to
CC central vacuole in root elongated cells, leaf epidermal cells and
CC trichomes of the lower face of the leaf blade. Limited to small
CC compartments in root cap and apex cells, hypocotyl parenchyma cells and
CC trichomes of the upper face of the leaf blade.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q8H166-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in leaves (at protein level).
CC {ECO:0000269|PubMed:8518555, ECO:0000269|PubMed:9225474}.
CC -!- INDUCTION: Induced during senescence. Strongly induced by ethylene and
CC slightly by abscisic acid. Repressed by cytokinin and darkness. Seems
CC to be not affected by dehydration. {ECO:0000269|PubMed:14617064,
CC ECO:0000269|PubMed:8518555, ECO:0000269|PubMed:9617813}.
CC -!- SIMILARITY: Belongs to the peptidase C1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU10088, ECO:0000255|PROSITE-ProRule:PRU10089,
CC ECO:0000255|PROSITE-ProRule:PRU10090}.
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DR EMBL; AF233883; AAF43041.1; -; mRNA.
DR EMBL; AF083703; AAN60262.1; -; mRNA.
DR EMBL; AB011483; BAB08221.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97313.1; -; Genomic_DNA.
DR EMBL; AF360273; AAK25983.1; -; mRNA.
DR EMBL; BT000673; AAN31819.1; -; mRNA.
DR EMBL; BT000674; AAN31820.1; -; mRNA.
DR EMBL; BT000676; AAN31822.1; -; mRNA.
DR EMBL; AY088662; AAM66984.1; -; mRNA.
DR PIR; PQ0650; PQ0650.
DR RefSeq; NP_568921.1; NM_125429.4. [Q8H166-1]
DR AlphaFoldDB; Q8H166; -.
DR SMR; Q8H166; -.
DR BioGRID; 21402; 2.
DR IntAct; Q8H166; 1.
DR STRING; 3702.AT5G60360.3; -.
DR MEROPS; C01.163; -.
DR MEROPS; I29.003; -.
DR PaxDb; Q8H166; -.
DR PRIDE; Q8H166; -.
DR ProteomicsDB; 244854; -. [Q8H166-1]
DR EnsemblPlants; AT5G60360.1; AT5G60360.1; AT5G60360. [Q8H166-1]
DR GeneID; 836158; -.
DR Gramene; AT5G60360.1; AT5G60360.1; AT5G60360. [Q8H166-1]
DR KEGG; ath:AT5G60360; -.
DR Araport; AT5G60360; -.
DR eggNOG; KOG1543; Eukaryota.
DR HOGENOM; CLU_012184_1_2_1; -.
DR InParanoid; Q8H166; -.
DR OMA; AYNNFGC; -.
DR PhylomeDB; Q8H166; -.
DR PRO; PR:Q8H166; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8H166; baseline and differential.
DR Genevisible; Q8H166; AT.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005764; C:lysosome; IBA:GO_Central.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IBA:GO_Central.
DR CDD; cd02248; Peptidase_C1A; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR025661; Pept_asp_AS.
DR InterPro; IPR000169; Pept_cys_AS.
DR InterPro; IPR025660; Pept_his_AS.
DR InterPro; IPR000668; Peptidase_C1A_C.
DR InterPro; IPR039417; Peptidase_C1A_papain-like.
DR InterPro; IPR013201; Prot_inhib_I29.
DR Pfam; PF08246; Inhibitor_I29; 1.
DR Pfam; PF00112; Peptidase_C1; 1.
DR PRINTS; PR00705; PAPAIN.
DR SMART; SM00848; Inhibitor_I29; 1.
DR SMART; SM00645; Pept_C1; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS00640; THIOL_PROTEASE_ASN; 1.
DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
DR PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Disulfide bond; Glycoprotein; Hydrolase; Protease;
KW Reference proteome; Signal; Thiol protease; Vacuole; Zymogen.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT PROPEP 22..140
FT /note="Activation peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000026414"
FT CHAIN 141..358
FT /note="Thiol protease aleurain"
FT /id="PRO_0000026415"
FT REGION 22..42
FT /note="Interaction with VSR1"
FT /evidence="ECO:0000269|PubMed:10871276"
FT ACT_SITE 165
FT /evidence="ECO:0000250"
FT ACT_SITE 305
FT /evidence="ECO:0000250"
FT ACT_SITE 325
FT /evidence="ECO:0000250"
FT CARBOHYD 125
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 254
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 162..205
FT /evidence="ECO:0000250"
FT DISULFID 196..238
FT /evidence="ECO:0000250"
FT DISULFID 296..346
FT /evidence="ECO:0000250"
FT CONFLICT 16
FT /note="V -> F (in Ref. 5; AAN31820)"
FT /evidence="ECO:0000305"
FT CONFLICT 166
FT /note="W -> V (in Ref. 7)"
FT /evidence="ECO:0000305"
FT CONFLICT 205
FT /note="C -> S (in Ref. 7)"
FT /evidence="ECO:0000305"
FT CONFLICT 230
FT /note="P -> R (in Ref. 7)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 358 AA; 38959 MW; 3B610AB85F81C31D CRC64;
MSAKTILSSV VLVVLVAASA AANIGFDESN PIRMVSDGLR EVEESVSQIL GQSRHVLSFA
RFTHRYGKKY QNVEEMKLRF SIFKENLDLI RSTNKKGLSY KLGVNQFADL TWQEFQRTKL
GAAQNCSATL KGSHKVTEAA LPETKDWRED GIVSPVKDQG GCGSCWTFST TGALEAAYHQ
AFGKGISLSE QQLVDCAGAF NNYGCNGGLP SQAFEYIKSN GGLDTEKAYP YTGKDETCKF
SAENVGVQVL NSVNITLGAE DELKHAVGLV RPVSIAFEVI HSFRLYKSGV YTDSHCGSTP
MDVNHAVLAV GYGVEDGVPY WLIKNSWGAD WGDKGYFKME MGKNMCGIAT CASYPVVA
