ALEUL_ARATH
ID ALEUL_ARATH Reviewed; 358 AA.
AC Q8RWQ9; Q9M3E7;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Thiol protease aleurain-like;
DE EC=3.4.22.16;
DE Flags: Precursor;
GN OrderedLocusNames=At3g45310; ORFNames=F18N11.70;
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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).
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 -!- SUBCELLULAR LOCATION: Vacuole {ECO:0000250}.
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=Q8RWQ9-1; Sequence=Displayed;
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB72480.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL132953; CAB72480.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE78021.1; -; Genomic_DNA.
DR EMBL; AY091771; AAM10319.1; -; mRNA.
DR PIR; T47471; T47471.
DR RefSeq; NP_566880.1; NM_114400.4. [Q8RWQ9-1]
DR AlphaFoldDB; Q8RWQ9; -.
DR SMR; Q8RWQ9; -.
DR STRING; 3702.AT3G45310.1; -.
DR MEROPS; C01.162; -.
DR iPTMnet; Q8RWQ9; -.
DR PaxDb; Q8RWQ9; -.
DR PRIDE; Q8RWQ9; -.
DR ProteomicsDB; 244981; -. [Q8RWQ9-1]
DR EnsemblPlants; AT3G45310.1; AT3G45310.1; AT3G45310. [Q8RWQ9-1]
DR GeneID; 823669; -.
DR Gramene; AT3G45310.1; AT3G45310.1; AT3G45310. [Q8RWQ9-1]
DR KEGG; ath:AT3G45310; -.
DR Araport; AT3G45310; -.
DR TAIR; locus:2078312; AT3G45310.
DR eggNOG; KOG1543; Eukaryota.
DR HOGENOM; CLU_012184_1_2_1; -.
DR InParanoid; Q8RWQ9; -.
DR OMA; IFAFCAV; -.
DR OrthoDB; 1275401at2759; -.
DR PhylomeDB; Q8RWQ9; -.
DR PRO; PR:Q8RWQ9; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8RWQ9; baseline and differential.
DR Genevisible; Q8RWQ9; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
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 2: Evidence at transcript 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_0000026418"
FT CHAIN 141..358
FT /note="Thiol protease aleurain-like"
FT /id="PRO_0000026419"
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"
SQ SEQUENCE 358 AA; 39542 MW; 0EE54FAADBADCDFD CRC64;
MSVKLNLSSS ILLILFAAAA SKEIGFDESN PIKMVSDNLH ELEDTVVQIL GQSRHVLSFS
RFTHRYGKKY QSVEEMKLRF SVFKENLDLI RSTNKKGLSY KLSLNQFADL TWQEFQRYKL
GAAQNCSATL KGSHKITEAT VPDTKDWRED GIVSPVKEQG HCGSCWTFST TGALEAAYHQ
AFGKGISLSE QQLVDCAGTF NNFGCHGGLP SQAFEYIKYN GGLDTEEAYP YTGKDGGCKF
SAKNIGVQVR DSVNITLGAE DELKHAVGLV RPVSVAFEVV HEFRFYKKGV FTSNTCGNTP
MDVNHAVLAV GYGVEDDVPY WLIKNSWGGE WGDNGYFKME MGKNMCGVAT CSSYPVVA
