DEGP2_ARATH
ID DEGP2_ARATH Reviewed; 607 AA.
AC O82261; Q9FPE9;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Protease Do-like 2, chloroplastic;
DE EC=3.4.21.-;
DE Flags: Precursor;
GN Name=DEGP2; OrderedLocusNames=At2g47940; ORFNames=F17A22.33, T9J23.7;
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], FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=11179216; DOI=10.1093/emboj/20.4.713;
RA Haussuhl K., Andersson B., Adamska I.;
RT "A chloroplast DegP2 protease performs the primary cleavage of the
RT photodamaged D1 protein in plant photosystem II.";
RL EMBO J. 20:713-722(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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 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).
CC -!- FUNCTION: Serine protease that performs the primary cleavage of the
CC photodamaged D1 protein in plant photosystem II.
CC {ECO:0000269|PubMed:11179216}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000269|PubMed:11179216}; Peripheral membrane protein
CC {ECO:0000269|PubMed:11179216}; Stromal side
CC {ECO:0000269|PubMed:11179216}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=O82261-1; Sequence=Displayed;
CC -!- INDUCTION: By high salt, desiccation and light stresses (at protein
CC level). {ECO:0000269|PubMed:11179216}.
CC -!- SIMILARITY: Belongs to the peptidase S1C family. {ECO:0000305}.
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DR EMBL; AF245171; AAK14061.1; -; mRNA.
DR EMBL; AC005309; AAC63648.2; -; Genomic_DNA.
DR EMBL; AC006072; AAM15122.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10914.1; -; Genomic_DNA.
DR EMBL; AF326865; AAG41447.1; -; mRNA.
DR EMBL; AF349516; AAK15563.1; -; mRNA.
DR EMBL; AY075700; AAL77706.1; -; mRNA.
DR EMBL; AY102139; AAM26706.1; -; mRNA.
DR PIR; D84921; D84921.
DR RefSeq; NP_566115.1; NM_130361.5. [O82261-1]
DR PDB; 4FLN; X-ray; 2.80 A; A/B/C=71-607.
DR PDB; 5ILB; X-ray; 1.85 A; A/B=110-315.
DR PDBsum; 4FLN; -.
DR PDBsum; 5ILB; -.
DR AlphaFoldDB; O82261; -.
DR SMR; O82261; -.
DR STRING; 3702.AT2G47940.1; -.
DR MEROPS; S01.279; -.
DR iPTMnet; O82261; -.
DR PaxDb; O82261; -.
DR PRIDE; O82261; -.
DR ProteomicsDB; 224602; -. [O82261-1]
DR EnsemblPlants; AT2G47940.1; AT2G47940.1; AT2G47940. [O82261-1]
DR GeneID; 819406; -.
DR Gramene; AT2G47940.1; AT2G47940.1; AT2G47940. [O82261-1]
DR KEGG; ath:AT2G47940; -.
DR Araport; AT2G47940; -.
DR TAIR; locus:2043403; AT2G47940.
DR eggNOG; KOG1320; Eukaryota.
DR InParanoid; O82261; -.
DR PhylomeDB; O82261; -.
DR PRO; PR:O82261; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O82261; baseline and differential.
DR Genevisible; O82261; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0009533; C:chloroplast stromal thylakoid; IDA:TAIR.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IDA:TAIR.
DR GO; GO:0009658; P:chloroplast organization; IMP:TAIR.
DR GO; GO:0010206; P:photosystem II repair; IDA:TAIR.
DR GO; GO:0030163; P:protein catabolic process; IMP: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; IPR041517; DEGP_PDZ.
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 Pfam; PF17815; PDZ_3; 1.
DR PRINTS; PR00834; PROTEASES2C.
DR SUPFAM; SSF50156; SSF50156; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Chloroplast; Hydrolase; Membrane;
KW Plastid; Protease; Reference proteome; Serine protease; Thylakoid;
KW Transit peptide.
FT TRANSIT 1..?
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT TRANSIT ?..69
FT /note="Thylakoid"
FT CHAIN 70..607
FT /note="Protease Do-like 2, chloroplastic"
FT /id="PRO_0000045830"
FT DOMAIN 308..403
FT /note="PDZ"
FT REGION 41..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 118..317
FT /note="Serine protease"
FT COMPBIAS 41..58
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..104
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 159
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 190
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 268
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT HELIX 113..117
FT /evidence="ECO:0007829|PDB:5ILB"
FT STRAND 118..125
FT /evidence="ECO:0007829|PDB:5ILB"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:4FLN"
FT STRAND 140..150
FT /evidence="ECO:0007829|PDB:5ILB"
FT STRAND 153..156
FT /evidence="ECO:0007829|PDB:5ILB"
FT HELIX 158..160
FT /evidence="ECO:0007829|PDB:5ILB"
FT STRAND 164..170
FT /evidence="ECO:0007829|PDB:5ILB"
FT STRAND 178..186
FT /evidence="ECO:0007829|PDB:5ILB"
FT TURN 187..190
FT /evidence="ECO:0007829|PDB:5ILB"
FT STRAND 191..196
FT /evidence="ECO:0007829|PDB:5ILB"
FT HELIX 199..202
FT /evidence="ECO:0007829|PDB:5ILB"
FT STRAND 219..224
FT /evidence="ECO:0007829|PDB:5ILB"
FT STRAND 227..229
FT /evidence="ECO:0007829|PDB:4FLN"
FT STRAND 233..247
FT /evidence="ECO:0007829|PDB:5ILB"
FT TURN 248..251
FT /evidence="ECO:0007829|PDB:5ILB"
FT STRAND 252..259
FT /evidence="ECO:0007829|PDB:5ILB"
FT TURN 265..269
FT /evidence="ECO:0007829|PDB:4FLN"
FT STRAND 271..273
FT /evidence="ECO:0007829|PDB:5ILB"
FT STRAND 275..277
FT /evidence="ECO:0007829|PDB:4FLN"
FT STRAND 279..286
FT /evidence="ECO:0007829|PDB:5ILB"
FT STRAND 296..300
FT /evidence="ECO:0007829|PDB:5ILB"
FT HELIX 301..314
FT /evidence="ECO:0007829|PDB:5ILB"
FT STRAND 325..329
FT /evidence="ECO:0007829|PDB:4FLN"
FT HELIX 333..339
FT /evidence="ECO:0007829|PDB:4FLN"
FT STRAND 342..345
FT /evidence="ECO:0007829|PDB:4FLN"
FT STRAND 347..352
FT /evidence="ECO:0007829|PDB:4FLN"
FT HELIX 357..360
FT /evidence="ECO:0007829|PDB:4FLN"
FT STRAND 367..371
FT /evidence="ECO:0007829|PDB:4FLN"
FT STRAND 377..383
FT /evidence="ECO:0007829|PDB:4FLN"
FT STRAND 389..391
FT /evidence="ECO:0007829|PDB:4FLN"
FT HELIX 393..397
FT /evidence="ECO:0007829|PDB:4FLN"
FT STRAND 404..411
FT /evidence="ECO:0007829|PDB:4FLN"
FT STRAND 414..421
FT /evidence="ECO:0007829|PDB:4FLN"
FT STRAND 446..450
FT /evidence="ECO:0007829|PDB:4FLN"
FT HELIX 453..456
FT /evidence="ECO:0007829|PDB:4FLN"
FT STRAND 461..464
FT /evidence="ECO:0007829|PDB:4FLN"
FT HELIX 466..474
FT /evidence="ECO:0007829|PDB:4FLN"
FT STRAND 485..490
FT /evidence="ECO:0007829|PDB:4FLN"
FT HELIX 494..496
FT /evidence="ECO:0007829|PDB:4FLN"
FT STRAND 504..510
FT /evidence="ECO:0007829|PDB:4FLN"
FT HELIX 518..526
FT /evidence="ECO:0007829|PDB:4FLN"
FT STRAND 530..537
FT /evidence="ECO:0007829|PDB:4FLN"
FT STRAND 542..546
FT /evidence="ECO:0007829|PDB:4FLN"
FT HELIX 547..558
FT /evidence="ECO:0007829|PDB:4FLN"
FT TURN 559..562
FT /evidence="ECO:0007829|PDB:4FLN"
FT HELIX 569..572
FT /evidence="ECO:0007829|PDB:4FLN"
SQ SEQUENCE 607 AA; 66802 MW; 2E1A319A4D48A9C3 CRC64;
MAASVANCCF SVLNASVKIQ SSSISSPWCF VSASSLTPRA SSNIKRKSSR SDSPSPILNP
EKNYPGRVRD ESSNPPQKMA FKAFGSPKKE KKESLSDFSR DQQTDPAKIH DASFLNAVVK
VYCTHTAPDY SLPWQKQRQF TSTGSAFMIG DGKLLTNAHC VEHDTQVKVK RRGDDRKYVA
KVLVRGVDCD IALLSVESED FWKGAEPLRL GHLPRLQDSV TVVGYPLGGD TISVTKGVVS
RIEVTSYAHG SSDLLGIQID AAINPGNSGG PAFNDQGECI GVAFQVYRSE ETENIGYVIP
TTVVSHFLTD YERNGKYTGY PCLGVLLQKL ENPALRECLK VPTNEGVLVR RVEPTSDASK
VLKEGDVIVS FDDLHVGCEG TVPFRSSERI AFRYLISQKF AGDIAEIGII RAGEHKKVQV
VLRPRVHLVP YHIDGGQPSY IIVAGLVFTP LSEPLIEEEC EDTIGLKLLT KARYSVARFR
GEQIVILSQV LANEVNIGYE DMNNQQVLKF NGIPIRNIHH LAHLIDMCKD KYLVFEFEDN
YVAVLEREAS NSASLCILKD YGIPSERSAD LLEPYVDPID DTQALDQGIG DSPVSNLEIG
FDGLVWA
