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UniProtKB/Swiss-Prot entry Q8RWQ9


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ALEUL_ARATH
Primary accession number Q8RWQ9
Secondary accession number Q9M3E7
Integrated into Swiss-Prot on August 16, 2005
Sequence was last modified on June 1, 2002 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 40)
Name and origin of the protein
Protein name Thiol protease aleurain-like [Precursor]
Synonym EC 3.4.22.16
Gene name
OrderedLocusNames: At3g45310
ORFNames: F18N11.70
From
Arabidopsis thaliana (Mouse-ear cress) [TaxID: 3702] 
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
DOI=10.1038/35048706; PubMed=11130713 [NCBI, ExPASy, EBI, Israel, Japan]
Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
"Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
Nature 408:820-822(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
DOI=10.1126/science.1088305; PubMed=14593172 [NCBI, ExPASy, EBI, Israel, Japan]
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis genome.";
Science 302:842-846(2003).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AL132953; CAB72480.1; ALT_SEQ; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY091771; AAM10319.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T47471; T47471.
RefSeq NP_566880.1; -.
UniGene At.25239
3D structure databases
HSSP P07711; 1CJL. [HSSP ENTRY / PDB]
ModBase Q8RWQ9.
Protein family/group databases
MEROPS C01.041; -.
Organism-specific databases
GeneFarm 5032; 478.
TAIR At3g45310; -.
Ontologies
GO
GO:0005773; Cellular component: vacuole (inferred from electronic annotation from UniProtKB-KW).
GO:0004197; Molecular function: cysteine-type endopeptidase activity (inferred from electronic annotation from InterPro).
GO:0006508; Biological process: proteolysis (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR000169; Pept_cys_AS.
IPR013128; Peptidase_C1A.
IPR000668; Peptidase_C1A_C.
IPR013201; Prot_inhib_I29.
Graphical view of domain structure.
PANTHER PTHR12411; Peptidase_C1A; 1.
Pfam PF08246; Inhibitor_I29; 1.
PF00112; Peptidase_C1; 1.
Pfam graphical view of domain structure.
PRINTS PR00705; PAPAIN.
ProDom PD000158; Peptidase_C1; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00645; Pept_C1; 1.
SMART graphical view of domain structure.
PROSITE PS00640; THIOL_PROTEASE_ASN; 1.
PS00139; THIOL_PROTEASE_CYS; 1.
PS00639; THIOL_PROTEASE_HIS; 1.
ProtoNet Q8RWQ9.
Genome annotation databases
GeneID 823669; -.
GenomeReviews BA000014_GR; AT3G45310.
NMPDR fig|3702.1.peg.15743; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Alternative splicing; Complete proteome; Glycoprotein; Hydrolase; Protease; Signal; Thiol protease; Vacuole; Zymogen.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    21  21     Potential. 
PROPEP   22   140  119     Activation peptide (By similarity). PRO_0000026418
CHAIN   141   358  218     Thiol protease aleurain-like. PRO_0000026419
ACT_SITE   165   165        By similarity. 
ACT_SITE   305   305        By similarity. 
ACT_SITE   325   325        By similarity. 
CARBOHYD   125   125        N-linked (GlcNAc...) (Potential). 
CARBOHYD   254   254        N-linked (GlcNAc...) (Potential). 
DISULFID   162   205        By similarity. 
DISULFID   196   238        By similarity. 
DISULFID   296   346        By similarity. 
Sequence information
Length: 358 AA [This is the length of the unprocessed precursor] Molecular weight: 39542 Da [This is the MW of the unprocessed precursor] CRC64: 0EE54FAADBADCDFD [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSVKLNLSSS ILLILFAAAA SKEIGFDESN PIKMVSDNLH ELEDTVVQIL GQSRHVLSFS 

        70         80         90        100        110        120 
RFTHRYGKKY QSVEEMKLRF SVFKENLDLI RSTNKKGLSY KLSLNQFADL TWQEFQRYKL 

       130        140        150        160        170        180 
GAAQNCSATL KGSHKITEAT VPDTKDWRED GIVSPVKEQG HCGSCWTFST TGALEAAYHQ 

       190        200        210        220        230        240 
AFGKGISLSE QQLVDCAGTF NNFGCHGGLP SQAFEYIKYN GGLDTEEAYP YTGKDGGCKF 

       250        260        270        280        290        300 
SAKNIGVQVR DSVNITLGAE DELKHAVGLV RPVSVAFEVV HEFRFYKKGV FTSNTCGNTP 

       310        320        330        340        350 
MDVNHAVLAV GYGVEDDVPY WLIKNSWGGE WGDNGYFKME MGKNMCGVAT CSSYPVVA 

Q8RWQ9 in FASTA format

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BLAST logo BLAST submission on ExPASy/SIB
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Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
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