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Protein

Protease Do-like 1, chloroplastic

Gene

DEGP1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: -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)DescriptionActionsGraphical viewLength
Active sitei173Charge relay systemSequence analysis1
Active sitei203Charge relay systemSequence analysis1
Active sitei282Charge relay systemSequence analysis1

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • 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

Keywordsi

Molecular functionHydrolase, Protease, Serine protease
Biological processStress response

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

AraportiAT3G27925
TAIRilocus:2086420 AT3G27925

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Chloroplast Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertion Graphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Chloroplast, Membrane, Plastid, Thylakoid

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi282S → G: Loss of activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei? – 105Thylakoid1 Publication
Transit peptidei1 – ?ChloroplastSequence analysis
ChainiPRO_0000026940106 – 439Protease Do-like 1, chloroplasticAdd BLAST334

Proteomic databases

PaxDbiO22609
PRIDEiO22609

Expressioni

Inductioni

By heat shock.1 Publication

Gene expression databases

ExpressionAtlasiO22609 baseline and differential
GenevisibleiO22609 AT

Interactioni

Subunit structurei

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

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-2895934,EBI-2895934

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

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

Structurei

Secondary structure

1439
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi116 – 128Combined sources13
Helixi129 – 131Combined sources3
Beta strandi132 – 142Combined sources11
Beta strandi144 – 146Combined sources3
Beta strandi149 – 163Combined sources15
Turni164 – 166Combined sources3
Beta strandi167 – 170Combined sources4
Helixi172 – 175Combined sources4
Beta strandi179 – 184Combined sources6
Beta strandi190 – 199Combined sources10
Helixi200 – 202Combined sources3
Beta strandi204 – 208Combined sources5
Helixi213 – 215Combined sources3
Beta strandi232 – 237Combined sources6
Helixi239 – 241Combined sources3
Beta strandi245 – 258Combined sources14
Beta strandi261 – 265Combined sources5
Beta strandi267 – 273Combined sources7
Beta strandi285 – 287Combined sources3
Beta strandi293 – 301Combined sources9
Beta strandi303 – 306Combined sources4
Beta strandi311 – 315Combined sources5
Helixi316 – 329Combined sources14
Beta strandi339 – 341Combined sources3
Turni344 – 351Combined sources8
Beta strandi353 – 359Combined sources7
Beta strandi362 – 364Combined sources3
Helixi365 – 369Combined sources5
Beta strandi378 – 380Combined sources3
Beta strandi397 – 399Combined sources3
Helixi400 – 406Combined sources7
Beta strandi414 – 420Combined sources7
Beta strandi422 – 431Combined sources10

3D structure databases

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

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini326 – 423PDZPROSITE-ProRule annotationAdd BLAST98

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni154 – 323Serine proteaseAdd BLAST170

Sequence similaritiesi

Belongs to the peptidase S1C family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG1320 Eukaryota
COG0265 LUCA
HOGENOMiHOG000223641
InParanoidiO22609
OMAiPFGLDWT
OrthoDBiEOG09360EEW
PhylomeDBiO22609

Family and domain databases

InterProiView protein in InterPro
IPR001478 PDZ
IPR036034 PDZ_sf
IPR009003 Peptidase_S1_PA
IPR001940 Peptidase_S1C
PfamiView protein in Pfam
PF13180 PDZ_2, 1 hit
PRINTSiPR00834 PROTEASES2C
SMARTiView protein in SMART
SM00228 PDZ, 1 hit
SUPFAMiSSF50156 SSF50156, 1 hit
SSF50494 SSF50494, 1 hit
PROSITEiView protein in PROSITE
PS50106 PDZ, 1 hit

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)DescriptionActionsGraphical viewLength
Sequence conflicti12 – 25SSTLF…PSSHL → HSPPSSQLSNST (PubMed:9507020).CuratedAdd BLAST14
Sequence conflicti38I → V in AAC39436 (PubMed:9507020).Curated1
Sequence conflicti56S → P in AAC39436 (PubMed:9507020).Curated1
Sequence conflicti62R → G in AAC39436 (PubMed:9507020).Curated1
Sequence conflicti66D → G in AAC39436 (PubMed:9507020).Curated1
Sequence conflicti70 – 71HF → LL in AAC39436 (PubMed:9507020).Curated2
Sequence conflicti357V → L in AAC39436 (PubMed:9507020).Curated1
Sequence conflicti383V → I in AAC39436 (PubMed:9507020).Curated1
Sequence conflicti418E → Q in AAC39436 (PubMed:9507020).Curated1

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
CP002686 Genomic DNA Translation: ANM63717.1
AY039585 mRNA Translation: AAK62640.1
AY113073 mRNA Translation: AAM47381.1
RefSeqiNP_001325789.1, NM_001338921.1
NP_189431.2, NM_113709.5
UniGeneiAt.47511

Genome annotation databases

EnsemblPlantsiAT3G27925.1; AT3G27925.1; AT3G27925
AT3G27925.2; AT3G27925.2; AT3G27925
GeneIDi822416
GrameneiAT3G27925.1; AT3G27925.1; AT3G27925
AT3G27925.2; AT3G27925.2; AT3G27925
KEGGiath:AT3G27925

Similar proteinsi

Entry informationi

Entry nameiDEGP1_ARATH
AccessioniPrimary (citable) accession number: O22609
Secondary accession number(s): Q94BX6, Q9LK85
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: August 16, 2004
Last modified: April 25, 2018
This is version 152 of the entry and version 2 of the sequence. See 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

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