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Q9STL4

- CEP2_ARATH

UniProt

Q9STL4 - CEP2_ARATH

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Protein

KDEL-tailed cysteine endopeptidase CEP2

Gene

CEP2

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 2 out of 5- Experimental evidence at transcript leveli

Functioni

Involved in the final stage of developmental programmed cell death and in intercalation of new cells. Cleaves extensins, thus probably supporting the final cell collapse.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei152 – 1521PROSITE-ProRule annotation
Active sitei288 – 2881PROSITE-ProRule annotation
Active sitei308 – 3081PROSITE-ProRule annotation

GO - Molecular functioni

  1. cysteine-type peptidase activity Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Enzyme and pathway databases

BioCyciARA:GQT-212-MONOMER.

Protein family/group databases

MEROPSiC01.A01.

Names & Taxonomyi

Protein namesi
Recommended name:
KDEL-tailed cysteine endopeptidase CEP2 (EC:3.4.22.-)
Gene namesi
Name:CEP21 Publication
Ordered Locus Names:At3g48340Imported
ORF Names:T29H11.140Imported
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 3

Organism-specific databases

TAIRiAT3G48340.

Subcellular locationi

Endoplasmic reticulum PROSITE-ProRule annotation

GO - Cellular componenti

  1. endoplasmic reticulum Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Sequence AnalysisAdd
BLAST
Chaini21 – 361341KDEL-tailed cysteine endopeptidase CEP2PRO_0000403790Add
BLAST

Proteomic databases

PaxDbiQ9STL4.
PRIDEiQ9STL4.

Expressioni

Tissue specificityi

Expressed in roots, stems, rosette and cauline leaves, flowers, buds and green siliques. Found in the tip of young primary leaves, in very young root tips and at later stages in all tissues of lateral root, including the vascular bundle. Not expressed in lateral root primordia, while directly emerging through the epidermis.1 Publication

Gene expression databases

GenevestigatoriQ9STL4.

Interactioni

Protein-protein interaction databases

IntActiQ9STL4. 1 interaction.
STRINGi3702.AT3G48340.1-P.

Structurei

3D structure databases

ProteinModelPortaliQ9STL4.
SMRiQ9STL4. Positions 28-351.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi358 – 3614Prevents secretion from ERPROSITE-ProRule annotation

Sequence similaritiesi

Belongs to the peptidase C1 family.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG4870.
HOGENOMiHOG000230773.
InParanoidiQ9STL4.
KOiK16292.
OMAiGTDDQPC.
PhylomeDBiQ9STL4.

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]
PROSITEiPS00014. ER_TARGET. 1 hit.
PS00640. 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.

Q9STL4 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKKLLLIFLF SLVILQTACG FDYDDKEIES EEGLSTLYDR WRSHHSVPRS
60 70 80 90 100
LNEREKRFNV FRHNVMHVHN TNKKNRSYKL KLNKFADLTI NEFKNAYTGS
110 120 130 140 150
NIKHHRMLQG PKRGSKQFMY DHENLSKLPS SVDWRKKGAV TEIKNQGKCG
160 170 180 190 200
SCWAFSTVAA VEGINKIKTN KLVSLSEQEL VDCDTKQNEG CNGGLMEIAF
210 220 230 240 250
EFIKKNGGIT TEDSYPYEGI DGKCDASKDN GVLVTIDGHE DVPENDENAL
260 270 280 290 300
LKAVANQPVS VAIDAGSSDF QFYSEGVFTG SCGTELNHGV AAVGYGSERG
310 320 330 340 350
KKYWIVRNSW GAEWGEGGYI KIEREIDEPE GRCGIAMEAS YPIKLSSSNP
360
TPKDGDVKDE L
Length:361
Mass (Da):40,371
Last modified:May 1, 2000 - v1
Checksum:iFEF1381FFE780C6E
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL049659 Genomic DNA. Translation: CAB41164.1.
CP002686 Genomic DNA. Translation: AEE78403.1.
PIRiT06708.
RefSeqiNP_680113.3. NM_148860.4.
UniGeneiAt.46818.

Genome annotation databases

EnsemblPlantsiAT3G48340.1; AT3G48340.1; AT3G48340.
GeneIDi823992.
KEGGiath:AT3G48340.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL049659 Genomic DNA. Translation: CAB41164.1 .
CP002686 Genomic DNA. Translation: AEE78403.1 .
PIRi T06708.
RefSeqi NP_680113.3. NM_148860.4.
UniGenei At.46818.

3D structure databases

ProteinModelPortali Q9STL4.
SMRi Q9STL4. Positions 28-351.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q9STL4. 1 interaction.
STRINGi 3702.AT3G48340.1-P.

Protein family/group databases

MEROPSi C01.A01.

Proteomic databases

PaxDbi Q9STL4.
PRIDEi Q9STL4.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT3G48340.1 ; AT3G48340.1 ; AT3G48340 .
GeneIDi 823992.
KEGGi ath:AT3G48340.

Organism-specific databases

TAIRi AT3G48340.

Phylogenomic databases

eggNOGi COG4870.
HOGENOMi HOG000230773.
InParanoidi Q9STL4.
KOi K16292.
OMAi GTDDQPC.
PhylomeDBi Q9STL4.

Enzyme and pathway databases

BioCyci ARA:GQT-212-MONOMER.

Gene expression databases

Genevestigatori Q9STL4.

Family and domain databases

InterProi IPR025661. Pept_asp_AS.
IPR000169. Pept_cys_AS.
IPR025660. Pept_his_AS.
IPR013128. Peptidase_C1A.
IPR000668. Peptidase_C1A_C.
IPR013201. Prot_inhib_I29.
[Graphical view ]
PANTHERi PTHR12411. PTHR12411. 1 hit.
Pfami PF08246. Inhibitor_I29. 1 hit.
PF00112. Peptidase_C1. 1 hit.
[Graphical view ]
PRINTSi PR00705. PAPAIN.
SMARTi SM00848. Inhibitor_I29. 1 hit.
SM00645. Pept_C1. 1 hit.
[Graphical view ]
PROSITEi PS00014. ER_TARGET. 1 hit.
PS00640. THIOL_PROTEASE_ASN. 1 hit.
PS00139. THIOL_PROTEASE_CYS. 1 hit.
PS00639. THIOL_PROTEASE_HIS. 1 hit.
[Graphical view ]
ProtoNeti Search...

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. "KDEL-tailed cysteine endopeptidases involved in programmed cell death, intercalation of new cells, and dismantling of extensin scaffolds."
    Helm M., Schmid M., Hierl G., Terneus K., Tan L., Lottspeich F., Kieliszewski M.J., Gietl C.
    Am. J. Bot. 95:1049-1062(2008)
    Cited for: FUNCTION, TISSUE SPECIFICITY.

Entry informationi

Entry nameiCEP2_ARATH
AccessioniPrimary (citable) accession number: Q9STL4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2011
Last sequence update: May 1, 2000
Last modified: October 29, 2014
This is version 79 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

External Data

Dasty 3