DEGP1_ARATH
ID DEGP1_ARATH Reviewed; 439 AA.
AC O22609; Q94BX6; Q9LK85;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 2.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Protease Do-like 1, chloroplastic;
DE EC=3.4.21.-;
DE AltName: Full=Protein DEGRADATION OF PERIPLASMIC PROTEINS 1;
DE Short=DEGP PROTEASE 1;
DE Flags: Precursor;
GN Name=DEGP1; Synonyms=DEG1, DEGP; OrderedLocusNames=At3g27925;
GN ORFNames=K16N12.18;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND CHARACTERIZATION.
RX PubMed=9507020; DOI=10.1074/jbc.273.12.7094;
RA Itzhaki H., Naveh L., Lindahl M., Cook M., Adam Z.;
RT "Identification and characterization of DegP, a serine protease associated
RT with the luminal side of the thylakoid membrane.";
RL J. Biol. Chem. 273:7094-7098(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP PROTEIN SEQUENCE OF 106-120, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=11719511; DOI=10.1074/jbc.m108575200;
RA Schubert M., Petersson U.A., Haas B.J., Funk C., Schroeder W.P.,
RA Kieselbach T.;
RT "Proteome map of the chloroplast lumen of Arabidopsis thaliana.";
RL J. Biol. Chem. 277:8354-8365(2002).
RN [6]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=11299370; DOI=10.1104/pp.125.4.1912;
RA Adam Z., Adamska I., Nakabayashi K., Ostersetzer O., Haussuhl K.,
RA Manuell A., Zheng B., Vallon O., Rodermel S.R., Shinozaki K., Clarke A.K.;
RT "Chloroplast and mitochondrial proteases in Arabidopsis. A proposed
RT nomenclature.";
RL Plant Physiol. 125:1912-1918(2001).
RN [7]
RP INTERACTION WITH DEGP1, SUBCELLULAR LOCATION, AND MUTAGENESIS OF SER-282.
RX PubMed=21877139; DOI=10.1007/s00425-011-1505-x;
RA Zienkiewicz M., Ferenc A., Wasilewska W., Romanowska E.;
RT "High light stimulates Deg1-dependent cleavage of the minor LHCII antenna
RT proteins CP26 and CP29 and the PsbS protein in Arabidopsis thaliana.";
RL Planta 235:279-288(2012).
CC -!- FUNCTION: Serine protease that is required at high temperature. May be
CC involved in the degradation of damaged proteins. In vivo, can degrade
CC beta-casein. {ECO:0000269|PubMed:21877139, ECO:0000269|PubMed:9507020}.
CC -!- ACTIVITY REGULATION: Inhibited by phenylmethylsulfonyl fluoride and O-
CC phenanthroline. {ECO:0000269|PubMed:9507020}.
CC -!- SUBUNIT: Interacts with PTAC16 and other potential targets for
CC degradation under high light conditions. {ECO:0000269|PubMed:21877139}.
CC -!- INTERACTION:
CC O22609; O22609: DEGP1; NbExp=2; IntAct=EBI-2895934, EBI-2895934;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000269|PubMed:11719511, ECO:0000269|PubMed:21877139,
CC ECO:0000269|PubMed:9507020}; Peripheral membrane protein
CC {ECO:0000269|PubMed:11719511, ECO:0000269|PubMed:9507020}; Lumenal side
CC {ECO:0000269|PubMed:11719511, ECO:0000269|PubMed:9507020}.
CC -!- INDUCTION: By heat shock. {ECO:0000269|PubMed:9507020}.
CC -!- SIMILARITY: Belongs to the peptidase S1C family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF028842; AAC39436.1; -; mRNA.
DR EMBL; AP000371; BAB02539.1; -; Genomic_DNA.
DR EMBL; AP001302; BAB02539.1; JOINED; Genomic_DNA.
DR EMBL; CP002686; AEE77381.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM63717.1; -; Genomic_DNA.
DR EMBL; AY039585; AAK62640.1; -; mRNA.
DR EMBL; AY113073; AAM47381.1; -; mRNA.
DR RefSeq; NP_001325789.1; NM_001338921.1.
DR RefSeq; NP_189431.2; NM_113709.5.
DR PDB; 3QO6; X-ray; 2.50 A; A/B/C=105-439.
DR PDBsum; 3QO6; -.
DR AlphaFoldDB; O22609; -.
DR SMR; O22609; -.
DR BioGRID; 7746; 13.
DR DIP; DIP-56439N; -.
DR IntAct; O22609; 2.
DR STRING; 3702.AT3G27925.1; -.
DR MEROPS; S01.472; -.
DR PaxDb; O22609; -.
DR PRIDE; O22609; -.
DR ProteomicsDB; 224601; -.
DR EnsemblPlants; AT3G27925.1; AT3G27925.1; AT3G27925.
DR EnsemblPlants; AT3G27925.2; AT3G27925.2; AT3G27925.
DR GeneID; 822416; -.
DR Gramene; AT3G27925.1; AT3G27925.1; AT3G27925.
DR Gramene; AT3G27925.2; AT3G27925.2; AT3G27925.
DR KEGG; ath:AT3G27925; -.
DR Araport; AT3G27925; -.
DR TAIR; locus:2086420; AT3G27925.
DR eggNOG; KOG1320; Eukaryota.
DR HOGENOM; CLU_020120_2_0_1; -.
DR InParanoid; O22609; -.
DR OMA; FWNDERT; -.
DR OrthoDB; 630723at2759; -.
DR PhylomeDB; O22609; -.
DR PRO; PR:O22609; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; O22609; baseline and differential.
DR Genevisible; O22609; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009534; C:chloroplast thylakoid; IDA:TAIR.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0009579; C:thylakoid; HDA:TAIR.
DR GO; GO:0031977; C:thylakoid lumen; HDA:TAIR.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IDA:TAIR.
DR GO; GO:0008236; F:serine-type peptidase activity; IDA:TAIR.
DR GO; GO:0010206; P:photosystem II repair; IMP:TAIR.
DR GO; GO:0030163; P:protein catabolic process; TAS:TAIR.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 2.40.10.10; -; 2.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001940; Peptidase_S1C.
DR Pfam; PF13180; PDZ_2; 1.
DR PRINTS; PR00834; PROTEASES2C.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chloroplast; Direct protein sequencing; Hydrolase; Membrane;
KW Plastid; Protease; Reference proteome; Serine protease; Stress response;
KW Thylakoid; Transit peptide.
FT TRANSIT 1..?
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT TRANSIT ?..105
FT /note="Thylakoid"
FT /evidence="ECO:0000269|PubMed:11719511"
FT CHAIN 106..439
FT /note="Protease Do-like 1, chloroplastic"
FT /id="PRO_0000026940"
FT DOMAIN 326..423
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 154..323
FT /note="Serine protease"
FT ACT_SITE 173
FT /note="Charge relay system"
FT /evidence="ECO:0000255"
FT ACT_SITE 203
FT /note="Charge relay system"
FT /evidence="ECO:0000255"
FT ACT_SITE 282
FT /note="Charge relay system"
FT /evidence="ECO:0000255"
FT MUTAGEN 282
FT /note="S->G: Loss of activity."
FT /evidence="ECO:0000269|PubMed:21877139"
FT CONFLICT 12..25
FT /note="SSTLFLHSPPSSHL -> HSPPSSQLSNST (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 38
FT /note="I -> V (in Ref. 1; AAC39436)"
FT /evidence="ECO:0000305"
FT CONFLICT 56
FT /note="S -> P (in Ref. 1; AAC39436)"
FT /evidence="ECO:0000305"
FT CONFLICT 62
FT /note="R -> G (in Ref. 1; AAC39436)"
FT /evidence="ECO:0000305"
FT CONFLICT 66
FT /note="D -> G (in Ref. 1; AAC39436)"
FT /evidence="ECO:0000305"
FT CONFLICT 70..71
FT /note="HF -> LL (in Ref. 1; AAC39436)"
FT /evidence="ECO:0000305"
FT CONFLICT 357
FT /note="V -> L (in Ref. 1; AAC39436)"
FT /evidence="ECO:0000305"
FT CONFLICT 383
FT /note="V -> I (in Ref. 1; AAC39436)"
FT /evidence="ECO:0000305"
FT CONFLICT 418
FT /note="E -> Q (in Ref. 1; AAC39436)"
FT /evidence="ECO:0000305"
FT HELIX 116..128
FT /evidence="ECO:0007829|PDB:3QO6"
FT HELIX 129..131
FT /evidence="ECO:0007829|PDB:3QO6"
FT STRAND 132..142
FT /evidence="ECO:0007829|PDB:3QO6"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:3QO6"
FT STRAND 149..163
FT /evidence="ECO:0007829|PDB:3QO6"
FT TURN 164..166
FT /evidence="ECO:0007829|PDB:3QO6"
FT STRAND 167..170
FT /evidence="ECO:0007829|PDB:3QO6"
FT HELIX 172..175
FT /evidence="ECO:0007829|PDB:3QO6"
FT STRAND 179..184
FT /evidence="ECO:0007829|PDB:3QO6"
FT STRAND 190..199
FT /evidence="ECO:0007829|PDB:3QO6"
FT HELIX 200..202
FT /evidence="ECO:0007829|PDB:3QO6"
FT STRAND 204..208
FT /evidence="ECO:0007829|PDB:3QO6"
FT HELIX 213..215
FT /evidence="ECO:0007829|PDB:3QO6"
FT STRAND 232..237
FT /evidence="ECO:0007829|PDB:3QO6"
FT HELIX 239..241
FT /evidence="ECO:0007829|PDB:3QO6"
FT STRAND 245..258
FT /evidence="ECO:0007829|PDB:3QO6"
FT STRAND 261..265
FT /evidence="ECO:0007829|PDB:3QO6"
FT STRAND 267..273
FT /evidence="ECO:0007829|PDB:3QO6"
FT STRAND 285..287
FT /evidence="ECO:0007829|PDB:3QO6"
FT STRAND 293..301
FT /evidence="ECO:0007829|PDB:3QO6"
FT STRAND 303..306
FT /evidence="ECO:0007829|PDB:3QO6"
FT STRAND 311..315
FT /evidence="ECO:0007829|PDB:3QO6"
FT HELIX 316..329
FT /evidence="ECO:0007829|PDB:3QO6"
FT STRAND 339..341
FT /evidence="ECO:0007829|PDB:3QO6"
FT TURN 344..351
FT /evidence="ECO:0007829|PDB:3QO6"
FT STRAND 353..359
FT /evidence="ECO:0007829|PDB:3QO6"
FT STRAND 362..364
FT /evidence="ECO:0007829|PDB:3QO6"
FT HELIX 365..369
FT /evidence="ECO:0007829|PDB:3QO6"
FT STRAND 378..380
FT /evidence="ECO:0007829|PDB:3QO6"
FT STRAND 397..399
FT /evidence="ECO:0007829|PDB:3QO6"
FT HELIX 400..406
FT /evidence="ECO:0007829|PDB:3QO6"
FT STRAND 414..420
FT /evidence="ECO:0007829|PDB:3QO6"
FT STRAND 422..431
FT /evidence="ECO:0007829|PDB:3QO6"
SQ SEQUENCE 439 AA; 46674 MW; 05EB437DCE71A251 CRC64;
MATTTSCSLL LSSTLFLHSP PSSHLSFFNL SSSRSSPISL YPIRSKRYFR ILSKLSLNDN
NRDDDDDTLH FTPFSAVKPF FLLCTSVALS FSLFAASPAV ESASAFVVST PKKLQTDELA
TVRLFQENTP SVVYITNLAV RQDAFTLDVL EVPQGSGSGF VWDKQGHIVT NYHVIRGASD
LRVTLADQTT FDAKVVGFDQ DKDVAVLRID APKNKLRPIP VGVSADLLVG QKVFAIGNPF
GLDHTLTTGV ISGLRREISS AATGRPIQDV IQTDAAINPG NSGGPLLDSS GTLIGINTAI
YSPSGASSGV GFSIPVDTVG GIVDQLVRFG KVTRPILGIK FAPDQSVEQL GVSGVLVLDA
PPSGPAGKAG LQSTKRDGYG RLVLGDIITS VNGTKVSNGS DLYRILDQCK VGDEVTVEVL
RGDHKEKISV TLEPKPDES
