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Protein

Protease Do-like 1, chloroplastic

Gene

DEGP1

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

Functioni

Serine protease that is required at high temperature. May be involved in the degradation of damaged proteins. In vivo, can degrade beta-casein.2 Publications

Enzyme regulationi

Inhibited by phenylmethylsulfonyl fluoride and O-phenanthroline.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei173 – 1731Charge relay systemSequence analysis
Active sitei203 – 2031Charge relay systemSequence analysis
Active sitei282 – 2821Charge relay systemSequence analysis

GO - Molecular functioni

  • serine-type endopeptidase activity Source: TAIR
  • serine-type peptidase activity Source: TAIR

GO - Biological processi

  • photosystem II repair Source: TAIR
  • protein catabolic process Source: TAIR
  • response to cytokinin Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Biological processi

Stress response

Enzyme and pathway databases

BioCyciARA:GQT-896-MONOMER.

Protein family/group databases

MEROPSiS01.472.

Names & Taxonomyi

Protein namesi
Recommended name:
Protease Do-like 1, chloroplastic (EC:3.4.21.-)
Alternative name(s):
Protein DEGRADATION OF PERIPLASMIC PROTEINS 1
Short name:
DEGP PROTEASE 1
Gene namesi
Name:DEGP1
Synonyms:DEG1, DEGP
Ordered Locus Names:At3g27925
ORF Names:K16N12.18
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 3

Organism-specific databases

TAIRiAT3G27925.

Subcellular locationi

GO - Cellular componenti

  • chloroplast Source: TAIR
  • chloroplast thylakoid Source: TAIR
  • chloroplast thylakoid membrane Source: UniProtKB
  • nucleus Source: TAIR
  • thylakoid Source: TAIR
  • thylakoid lumen Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Membrane, Plastid, Thylakoid

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi282 – 2821S → G: Loss of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei? – 105Thylakoid1 Publication
Transit peptidei1 – ?ChloroplastSequence analysis
Chaini106 – 439334Protease Do-like 1, chloroplasticPRO_0000026940Add
BLAST

Proteomic databases

PaxDbiO22609.
PRIDEiO22609.

Expressioni

Inductioni

By heat shock.1 Publication

Gene expression databases

GenevisibleiO22609. AT.

Interactioni

Subunit structurei

Interacts with PTAC16 and other potential targets for degradation under high light conditions.1 Publication

Protein-protein interaction databases

BioGridi7746. 13 interactions.
DIPiDIP-56439N.
IntActiO22609. 2 interactions.
STRINGi3702.AT3G27925.1.

Structurei

Secondary structure

1
439
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi116 – 12813Combined sources
Helixi129 – 1313Combined sources
Beta strandi132 – 14211Combined sources
Beta strandi144 – 1463Combined sources
Beta strandi149 – 16315Combined sources
Turni164 – 1663Combined sources
Beta strandi167 – 1704Combined sources
Helixi172 – 1754Combined sources
Beta strandi179 – 1846Combined sources
Beta strandi190 – 19910Combined sources
Helixi200 – 2023Combined sources
Beta strandi204 – 2085Combined sources
Helixi213 – 2153Combined sources
Beta strandi232 – 2376Combined sources
Helixi239 – 2413Combined sources
Beta strandi245 – 25814Combined sources
Beta strandi261 – 2655Combined sources
Beta strandi267 – 2737Combined sources
Beta strandi285 – 2873Combined sources
Beta strandi293 – 3019Combined sources
Beta strandi303 – 3064Combined sources
Beta strandi311 – 3155Combined sources
Helixi316 – 32914Combined sources
Beta strandi339 – 3413Combined sources
Turni344 – 3518Combined sources
Beta strandi353 – 3597Combined sources
Beta strandi362 – 3643Combined sources
Helixi365 – 3695Combined sources
Beta strandi378 – 3803Combined sources
Beta strandi397 – 3993Combined sources
Helixi400 – 4067Combined sources
Beta strandi414 – 4207Combined sources
Beta strandi422 – 43110Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3QO6X-ray2.50A/B/C105-439[»]
ProteinModelPortaliO22609.
SMRiO22609. Positions 111-438.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini326 – 42398PDZPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni154 – 323170Serine proteaseAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase S1C family.Curated
Contains 1 PDZ (DHR) domain.PROSITE-ProRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG1320. Eukaryota.
COG0265. LUCA.
HOGENOMiHOG000223641.
InParanoidiO22609.
OMAiQLVRFGK.
PhylomeDBiO22609.

Family and domain databases

Gene3Di2.30.42.10. 1 hit.
InterProiIPR001478. PDZ.
IPR009003. Peptidase_S1_PA.
IPR001940. Peptidase_S1C.
[Graphical view]
PfamiPF13180. PDZ_2. 1 hit.
[Graphical view]
PRINTSiPR00834. PROTEASES2C.
SMARTiSM00228. PDZ. 1 hit.
[Graphical view]
SUPFAMiSSF50156. SSF50156. 1 hit.
SSF50494. SSF50494. 1 hit.
PROSITEiPS50106. PDZ. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

O22609-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATTTSCSLL LSSTLFLHSP PSSHLSFFNL SSSRSSPISL YPIRSKRYFR
60 70 80 90 100
ILSKLSLNDN NRDDDDDTLH FTPFSAVKPF FLLCTSVALS FSLFAASPAV
110 120 130 140 150
ESASAFVVST PKKLQTDELA TVRLFQENTP SVVYITNLAV RQDAFTLDVL
160 170 180 190 200
EVPQGSGSGF VWDKQGHIVT NYHVIRGASD LRVTLADQTT FDAKVVGFDQ
210 220 230 240 250
DKDVAVLRID APKNKLRPIP VGVSADLLVG QKVFAIGNPF GLDHTLTTGV
260 270 280 290 300
ISGLRREISS AATGRPIQDV IQTDAAINPG NSGGPLLDSS GTLIGINTAI
310 320 330 340 350
YSPSGASSGV GFSIPVDTVG GIVDQLVRFG KVTRPILGIK FAPDQSVEQL
360 370 380 390 400
GVSGVLVLDA PPSGPAGKAG LQSTKRDGYG RLVLGDIITS VNGTKVSNGS
410 420 430
DLYRILDQCK VGDEVTVEVL RGDHKEKISV TLEPKPDES
Length:439
Mass (Da):46,674
Last modified:August 16, 2004 - v2
Checksum:i05EB437DCE71A251
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti12 – 2514SSTLF…PSSHL → HSPPSSQLSNST (PubMed:9507020).CuratedAdd
BLAST
Sequence conflicti38 – 381I → V in AAC39436 (PubMed:9507020).Curated
Sequence conflicti56 – 561S → P in AAC39436 (PubMed:9507020).Curated
Sequence conflicti62 – 621R → G in AAC39436 (PubMed:9507020).Curated
Sequence conflicti66 – 661D → G in AAC39436 (PubMed:9507020).Curated
Sequence conflicti70 – 712HF → LL in AAC39436 (PubMed:9507020).Curated
Sequence conflicti357 – 3571V → L in AAC39436 (PubMed:9507020).Curated
Sequence conflicti383 – 3831V → I in AAC39436 (PubMed:9507020).Curated
Sequence conflicti418 – 4181E → Q in AAC39436 (PubMed:9507020).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF028842 mRNA. Translation: AAC39436.1.
AP000371, AP001302 Genomic DNA. Translation: BAB02539.1.
CP002686 Genomic DNA. Translation: AEE77381.1.
AY039585 mRNA. Translation: AAK62640.1.
AY113073 mRNA. Translation: AAM47381.1.
RefSeqiNP_189431.2. NM_113709.4.
UniGeneiAt.47511.

Genome annotation databases

EnsemblPlantsiAT3G27925.1; AT3G27925.1; AT3G27925.
GeneIDi822416.
GrameneiAT3G27925.1; AT3G27925.1; AT3G27925.
KEGGiath:AT3G27925.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF028842 mRNA. Translation: AAC39436.1.
AP000371, AP001302 Genomic DNA. Translation: BAB02539.1.
CP002686 Genomic DNA. Translation: AEE77381.1.
AY039585 mRNA. Translation: AAK62640.1.
AY113073 mRNA. Translation: AAM47381.1.
RefSeqiNP_189431.2. NM_113709.4.
UniGeneiAt.47511.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3QO6X-ray2.50A/B/C105-439[»]
ProteinModelPortaliO22609.
SMRiO22609. Positions 111-438.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi7746. 13 interactions.
DIPiDIP-56439N.
IntActiO22609. 2 interactions.
STRINGi3702.AT3G27925.1.

Protein family/group databases

MEROPSiS01.472.

Proteomic databases

PaxDbiO22609.
PRIDEiO22609.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT3G27925.1; AT3G27925.1; AT3G27925.
GeneIDi822416.
GrameneiAT3G27925.1; AT3G27925.1; AT3G27925.
KEGGiath:AT3G27925.

Organism-specific databases

TAIRiAT3G27925.

Phylogenomic databases

eggNOGiKOG1320. Eukaryota.
COG0265. LUCA.
HOGENOMiHOG000223641.
InParanoidiO22609.
OMAiQLVRFGK.
PhylomeDBiO22609.

Enzyme and pathway databases

BioCyciARA:GQT-896-MONOMER.

Miscellaneous databases

PROiO22609.

Gene expression databases

GenevisibleiO22609. AT.

Family and domain databases

Gene3Di2.30.42.10. 1 hit.
InterProiIPR001478. PDZ.
IPR009003. Peptidase_S1_PA.
IPR001940. Peptidase_S1C.
[Graphical view]
PfamiPF13180. PDZ_2. 1 hit.
[Graphical view]
PRINTSiPR00834. PROTEASES2C.
SMARTiSM00228. PDZ. 1 hit.
[Graphical view]
SUPFAMiSSF50156. SSF50156. 1 hit.
SSF50494. SSF50494. 1 hit.
PROSITEiPS50106. PDZ. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification and characterization of DegP, a serine protease associated with the luminal side of the thylakoid membrane."
    Itzhaki H., Naveh L., Lindahl M., Cook M., Adam Z.
    J. Biol. Chem. 273:7094-7098(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, CHARACTERIZATION.
  2. "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC clones."
    Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.
    DNA Res. 7:217-221(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  4. "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.
  5. Cited for: PROTEIN SEQUENCE OF 106-120, SUBCELLULAR LOCATION.
    Strain: cv. Columbia.
  6. Cited for: GENE FAMILY, NOMENCLATURE.
  7. "High light stimulates Deg1-dependent cleavage of the minor LHCII antenna proteins CP26 and CP29 and the PsbS protein in Arabidopsis thaliana."
    Zienkiewicz M., Ferenc A., Wasilewska W., Romanowska E.
    Planta 235:279-288(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DEGP1, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-282.

Entry informationi

Entry nameiDEGP1_ARATH
AccessioniPrimary (citable) accession number: O22609
Secondary accession number(s): Q94BX6, Q9LK85
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: August 16, 2004
Last modified: June 8, 2016
This is version 141 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Peptidase families
    Classification of peptidase families and list of entries
  4. 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.