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   16-JUN-2009, entry version 46.
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; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   MEDLINE=21016720; PubMed=11130713; DOI=10.1038/35048706;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M.,
RA   Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B.,
RA   Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P.,
RA   De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P.,
RA   Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V.,
RA   Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S.,
RA   Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G.,
RA   Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B.,
RA   Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G.,
RA   Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J.,
RA   Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D.,
RA   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.,
RA   Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W.,
RA   Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J.,
RA   Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P.,
RA   Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S.,
RA   Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V.,
RA   Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C.,
RA   Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E.,
RA   Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y.,
RA   Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A.,
RA   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
RT   thaliana.";
RL   Nature 408:820-822(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of proteins, acting as an
CC       aminopeptidase (notably, cleaving Arg-|-Xaa bonds) as well as an
CC       endopeptidase.
CC   -!- SUBCELLULAR LOCATION: Vacuole (By similarity).
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.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAB72480.1; Type=Erroneous gene model prediction;
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DR   EMBL; AL132953; CAB72480.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AY091771; AAM10319.1; -; mRNA.
DR   IPI; IPI00540369; -.
DR   PIR; T47471; T47471.
DR   RefSeq; NP_566880.1; -.
DR   UniGene; At.25239; -.
DR   HSSP; P07711; 1CJL.
DR   MEROPS; C01.A07; -.
DR   PRIDE; Q8RWQ9; -.
DR   GeneID; 823669; -.
DR   GenomeReviews; BA000014_GR; AT3G45310.
DR   NMPDR; fig|3702.1.peg.15743; -.
DR   GeneFarm; 5032; 478.
DR   TAIR; At3g45310; -.
DR   OMA; Q8RWQ9; ECSANDT.
DR   BRENDA; 3.4.22.16; 302.
DR   GO; GO:0005773; C:vacuole; IEA:UniProtKB-SubCell.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   InterPro; IPR000169; Pept_cys_AS.
DR   InterPro; IPR013128; Peptidase_C1A.
DR   InterPro; IPR000668; Peptidase_C1A_C.
DR   InterPro; IPR013201; Prot_inhib_I29.
DR   PANTHER; PTHR12411; Peptidase_C1A; 1.
DR   Pfam; PF08246; Inhibitor_I29; 1.
DR   Pfam; PF00112; Peptidase_C1; 1.
DR   PRINTS; PR00705; PAPAIN.
DR   ProDom; PD000158; Peptidase_C1; 1.
DR   SMART; SM00645; Pept_C1; 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; Complete proteome; Disulfide bond; Glycoprotein;
KW   Hydrolase; Protease; Signal; Thiol protease; Vacuole; Zymogen.
FT   SIGNAL        1     21       Potential.
FT   PROPEP       22    140       Activation peptide (By similarity).
FT                                /FTId=PRO_0000026418.
FT   CHAIN       141    358       Thiol protease aleurain-like.
FT                                /FTId=PRO_0000026419.
FT   ACT_SITE    165    165       By similarity.
FT   ACT_SITE    305    305       By similarity.
FT   ACT_SITE    325    325       By similarity.
FT   CARBOHYD    125    125       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    254    254       N-linked (GlcNAc...) (Potential).
FT   DISULFID    162    205       By similarity.
FT   DISULFID    196    238       By similarity.
FT   DISULFID    296    346       By similarity.
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
//