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Protein

Thiol protease aleurain-like

Gene

At3g45310

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Catalytic activityi

Hydrolysis of proteins, acting as an aminopeptidase (notably, cleaving Arg-|-Xaa bonds) as well as an endopeptidase.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei165 – 1651By similarity
Active sitei305 – 3051By similarity
Active sitei325 – 3251By similarity

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Enzyme and pathway databases

BioCyciARA:AT3G45310-MONOMER.
ARA:GQT-1235-MONOMER.

Protein family/group databases

MEROPSiC01.162.

Names & Taxonomyi

Protein namesi
Recommended name:
Thiol protease aleurain-like (EC:3.4.22.16)
Gene namesi
Ordered Locus Names:At3g45310
ORF Names:F18N11.70
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 3

Organism-specific databases

TAIRiAT3G45310.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Vacuole

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Sequence analysisAdd
BLAST
Propeptidei22 – 140119Activation peptideBy similarityPRO_0000026418Add
BLAST
Chaini141 – 358218Thiol protease aleurain-likePRO_0000026419Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi125 – 1251N-linked (GlcNAc...)Sequence analysis
Disulfide bondi162 ↔ 205By similarity
Disulfide bondi196 ↔ 238By similarity
Glycosylationi254 – 2541N-linked (GlcNAc...)Sequence analysis
Disulfide bondi296 ↔ 346By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PaxDbiQ8RWQ9.
PRIDEiQ8RWQ9.

PTM databases

iPTMnetiQ8RWQ9.

Expressioni

Gene expression databases

ExpressionAtlasiQ8RWQ9. baseline and differential.
GenevisibleiQ8RWQ9. AT.

Interactioni

Protein-protein interaction databases

STRINGi3702.AT3G45310.1.

Structurei

3D structure databases

ProteinModelPortaliQ8RWQ9.
SMRiQ8RWQ9. Positions 66-358.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase C1 family.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG1543. Eukaryota.
COG4870. LUCA.
HOGENOMiHOG000230774.
InParanoidiQ8RWQ9.
OMAiYSTEEYH.
PhylomeDBiQ8RWQ9.

Family and domain databases

InterProiIPR025661. Pept_asp_AS.
IPR000169. Pept_cys_AS.
IPR025660. Pept_his_AS.
IPR013128. Peptidase_C1A.
IPR000668. Peptidase_C1A_C.
IPR013201. Prot_inhib_I29.
[Graphical view]
PANTHERiPTHR12411. PTHR12411. 1 hit.
PfamiPF08246. Inhibitor_I29. 1 hit.
PF00112. Peptidase_C1. 1 hit.
[Graphical view]
PRINTSiPR00705. PAPAIN.
SMARTiSM00848. Inhibitor_I29. 1 hit.
SM00645. Pept_C1. 1 hit.
[Graphical view]
PROSITEiPS00640. THIOL_PROTEASE_ASN. 1 hit.
PS00139. THIOL_PROTEASE_CYS. 1 hit.
PS00639. THIOL_PROTEASE_HIS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 1 isoform i produced by alternative splicing. AlignAdd to basket

Note: A number of isoforms are produced. According to EST sequences.

Isoform 1 (identifier: Q8RWQ9-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSVKLNLSSS ILLILFAAAA SKEIGFDESN PIKMVSDNLH ELEDTVVQIL
60 70 80 90 100
GQSRHVLSFS RFTHRYGKKY QSVEEMKLRF SVFKENLDLI RSTNKKGLSY
110 120 130 140 150
KLSLNQFADL TWQEFQRYKL GAAQNCSATL KGSHKITEAT VPDTKDWRED
160 170 180 190 200
GIVSPVKEQG HCGSCWTFST TGALEAAYHQ AFGKGISLSE QQLVDCAGTF
210 220 230 240 250
NNFGCHGGLP SQAFEYIKYN GGLDTEEAYP YTGKDGGCKF SAKNIGVQVR
260 270 280 290 300
DSVNITLGAE DELKHAVGLV RPVSVAFEVV HEFRFYKKGV FTSNTCGNTP
310 320 330 340 350
MDVNHAVLAV GYGVEDDVPY WLIKNSWGGE WGDNGYFKME MGKNMCGVAT

CSSYPVVA
Length:358
Mass (Da):39,542
Last modified:June 1, 2002 - v1
Checksum:i0EE54FAADBADCDFD
GO

Sequence cautioni

The sequence CAB72480.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL132953 Genomic DNA. Translation: CAB72480.1. Sequence problems.
CP002686 Genomic DNA. Translation: AEE78021.1.
AY091771 mRNA. Translation: AAM10319.1.
PIRiT47471.
RefSeqiNP_566880.1. NM_114400.3. [Q8RWQ9-1]
UniGeneiAt.25239.

Genome annotation databases

EnsemblPlantsiAT3G45310.1; AT3G45310.1; AT3G45310. [Q8RWQ9-1]
GeneIDi823669.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL132953 Genomic DNA. Translation: CAB72480.1. Sequence problems.
CP002686 Genomic DNA. Translation: AEE78021.1.
AY091771 mRNA. Translation: AAM10319.1.
PIRiT47471.
RefSeqiNP_566880.1. NM_114400.3. [Q8RWQ9-1]
UniGeneiAt.25239.

3D structure databases

ProteinModelPortaliQ8RWQ9.
SMRiQ8RWQ9. Positions 66-358.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3702.AT3G45310.1.

Protein family/group databases

MEROPSiC01.162.

PTM databases

iPTMnetiQ8RWQ9.

Proteomic databases

PaxDbiQ8RWQ9.
PRIDEiQ8RWQ9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT3G45310.1; AT3G45310.1; AT3G45310. [Q8RWQ9-1]
GeneIDi823669.

Organism-specific databases

TAIRiAT3G45310.

Phylogenomic databases

eggNOGiKOG1543. Eukaryota.
COG4870. LUCA.
HOGENOMiHOG000230774.
InParanoidiQ8RWQ9.
OMAiYSTEEYH.
PhylomeDBiQ8RWQ9.

Enzyme and pathway databases

BioCyciARA:AT3G45310-MONOMER.
ARA:GQT-1235-MONOMER.

Miscellaneous databases

PROiQ8RWQ9.

Gene expression databases

ExpressionAtlasiQ8RWQ9. baseline and differential.
GenevisibleiQ8RWQ9. AT.

Family and domain databases

InterProiIPR025661. Pept_asp_AS.
IPR000169. Pept_cys_AS.
IPR025660. Pept_his_AS.
IPR013128. Peptidase_C1A.
IPR000668. Peptidase_C1A_C.
IPR013201. Prot_inhib_I29.
[Graphical view]
PANTHERiPTHR12411. PTHR12411. 1 hit.
PfamiPF08246. Inhibitor_I29. 1 hit.
PF00112. Peptidase_C1. 1 hit.
[Graphical view]
PRINTSiPR00705. PAPAIN.
SMARTiSM00848. Inhibitor_I29. 1 hit.
SM00645. Pept_C1. 1 hit.
[Graphical view]
PROSITEiPS00640. THIOL_PROTEASE_ASN. 1 hit.
PS00139. THIOL_PROTEASE_CYS. 1 hit.
PS00639. THIOL_PROTEASE_HIS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."
    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.
    Nature 408:820-822(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  2. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  3. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    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.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.

Entry informationi

Entry nameiALEUL_ARATH
AccessioniPrimary (citable) accession number: Q8RWQ9
Secondary accession number(s): Q9M3E7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: June 1, 2002
Last modified: February 17, 2016
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.