DEGP9_ARATH
ID DEGP9_ARATH Reviewed; 592 AA.
AC Q9FL12;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Protease Do-like 9;
DE EC=3.4.21.-;
GN Name=DEGP9; OrderedLocusNames=At5g40200; ORFNames=MSN9.10, MSN9.100;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9679202; DOI=10.1093/dnares/5.2.131;
RA Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence
RT features of the regions of 1,381,565 bp covered by twenty one physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:131-145(1998).
RN [2]
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 [3]
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 [4]
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [6]
RP FUNCTION, INTERACTION WITH ARR4, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AND INDUCTION BY TRANS-ZEATIN.
RX PubMed=27274065; DOI=10.1073/pnas.1601724113;
RA Chi W., Li J., He B., Chai X., Xu X., Sun X., Jiang J., Feng P., Zuo J.,
RA Lin R., Rochaix J.D., Zhang L.;
RT "DEG9, a serine protease, modulates cytokinin and light signaling by
RT regulating the level of ARABIDOPSIS RESPONSE REGULATOR 4.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:E3568-E3576(2016).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 65-592, FUNCTION, SUBUNIT, AND
RP MUTAGENESIS OF PRO-579.
RX PubMed=29180814; DOI=10.1038/s41477-017-0060-2;
RA Ouyang M., Li X., Zhao S., Pu H., Shen J., Adam Z., Clausen T., Zhang L.;
RT "The crystal structure of Deg9 reveals a novel octameric-type HtrA
RT protease.";
RL Nat. Plants 3:973-982(2017).
CC -!- FUNCTION: Serine protease that degrades the two-component response
CC regulator ARR4 (PubMed:27274065, PubMed:29180814). Regulates ARR4
CC stability by targeting ARR4 in the nucleus for degradation. Acts
CC upstream of ARR4 and regulates the activity of ARR4 in cytokinin and
CC light-signaling pathways. ARR4 mediates the cross-talk between light
CC and cytokinin signaling through modulation of the activity of
CC phytochrome B (PubMed:27274065). {ECO:0000269|PubMed:27274065,
CC ECO:0000269|PubMed:29180814}.
CC -!- SUBUNIT: Homooctamer formed by 4 homodimers (PubMed:29180814).
CC Interacts with ARR4 (PubMed:27274065). {ECO:0000269|PubMed:27274065,
CC ECO:0000269|PubMed:29180814}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:27274065}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, cotyledons, rosette leaves,
CC cauline leaves, stems, flowers and siliques.
CC {ECO:0000269|PubMed:27274065}.
CC -!- INDUCTION: Induced by trans-zeatin (at protein level).
CC {ECO:0000269|PubMed:27274065}.
CC -!- SIMILARITY: Belongs to the peptidase S1C family. {ECO:0000305}.
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DR EMBL; AB010699; BAB10901.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94519.1; -; Genomic_DNA.
DR EMBL; AY046023; AAK76697.1; -; mRNA.
DR EMBL; AY142608; AAN13177.1; -; mRNA.
DR RefSeq; NP_568577.1; NM_123384.3.
DR PDB; 5IL9; X-ray; 2.20 A; A/B=65-592.
DR PDB; 5ILA; X-ray; 3.00 A; A/B=65-327.
DR PDB; 5ILB; X-ray; 1.85 A; A/B=326-592.
DR PDB; 5JYK; X-ray; 2.30 A; A/B=65-592.
DR PDB; 5Y09; X-ray; 2.45 A; A/B=65-592.
DR PDBsum; 5IL9; -.
DR PDBsum; 5ILA; -.
DR PDBsum; 5ILB; -.
DR PDBsum; 5JYK; -.
DR PDBsum; 5Y09; -.
DR AlphaFoldDB; Q9FL12; -.
DR SMR; Q9FL12; -.
DR STRING; 3702.AT5G40200.1; -.
DR MEROPS; S01.A05; -.
DR iPTMnet; Q9FL12; -.
DR PaxDb; Q9FL12; -.
DR PRIDE; Q9FL12; -.
DR ProteomicsDB; 222205; -.
DR EnsemblPlants; AT5G40200.1; AT5G40200.1; AT5G40200.
DR GeneID; 834018; -.
DR Gramene; AT5G40200.1; AT5G40200.1; AT5G40200.
DR KEGG; ath:AT5G40200; -.
DR Araport; AT5G40200; -.
DR TAIR; locus:2173727; AT5G40200.
DR eggNOG; KOG1320; Eukaryota.
DR HOGENOM; CLU_020120_10_0_1; -.
DR InParanoid; Q9FL12; -.
DR OMA; MVEACKE; -.
DR OrthoDB; 594175at2759; -.
DR PhylomeDB; Q9FL12; -.
DR BRENDA; 3.4.21.107; 399.
DR PRO; PR:Q9FL12; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FL12; baseline and differential.
DR Genevisible; Q9FL12; AT.
DR GO; GO:0005730; C:nucleolus; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0008236; F:serine-type peptidase activity; IDA:UniProtKB.
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; Hydrolase; Nucleus; Protease; Reference proteome;
KW Serine protease.
FT CHAIN 1..592
FT /note="Protease Do-like 9"
FT /id="PRO_0000093863"
FT DOMAIN 334..414
FT /note="PDZ"
FT REGION 1..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 141..318
FT /note="Serine protease"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..53
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 169
FT /note="Charge relay system"
FT /evidence="ECO:0000255"
FT ACT_SITE 200
FT /note="Charge relay system"
FT /evidence="ECO:0000255"
FT ACT_SITE 278
FT /note="Charge relay system"
FT /evidence="ECO:0000255"
FT MUTAGEN 579
FT /note="P->A: Reduces protease activity."
FT /evidence="ECO:0000269|PubMed:29180814"
FT HELIX 125..127
FT /evidence="ECO:0007829|PDB:5IL9"
FT STRAND 128..135
FT /evidence="ECO:0007829|PDB:5IL9"
FT STRAND 140..142
FT /evidence="ECO:0007829|PDB:5IL9"
FT STRAND 150..159
FT /evidence="ECO:0007829|PDB:5IL9"
FT TURN 160..162
FT /evidence="ECO:0007829|PDB:5IL9"
FT STRAND 163..166
FT /evidence="ECO:0007829|PDB:5IL9"
FT HELIX 169..171
FT /evidence="ECO:0007829|PDB:5IL9"
FT STRAND 174..180
FT /evidence="ECO:0007829|PDB:5IL9"
FT STRAND 187..196
FT /evidence="ECO:0007829|PDB:5IL9"
FT TURN 197..200
FT /evidence="ECO:0007829|PDB:5IL9"
FT STRAND 201..207
FT /evidence="ECO:0007829|PDB:5IL9"
FT HELIX 209..212
FT /evidence="ECO:0007829|PDB:5IL9"
FT STRAND 229..234
FT /evidence="ECO:0007829|PDB:5IL9"
FT STRAND 243..258
FT /evidence="ECO:0007829|PDB:5IL9"
FT STRAND 263..271
FT /evidence="ECO:0007829|PDB:5IL9"
FT TURN 275..279
FT /evidence="ECO:0007829|PDB:5IL9"
FT STRAND 280..284
FT /evidence="ECO:0007829|PDB:5IL9"
FT STRAND 289..294
FT /evidence="ECO:0007829|PDB:5IL9"
FT STRAND 297..299
FT /evidence="ECO:0007829|PDB:5IL9"
FT HELIX 301..303
FT /evidence="ECO:0007829|PDB:5IL9"
FT STRAND 306..310
FT /evidence="ECO:0007829|PDB:5IL9"
FT HELIX 311..324
FT /evidence="ECO:0007829|PDB:5IL9"
FT STRAND 335..338
FT /evidence="ECO:0007829|PDB:5ILB"
FT HELIX 343..348
FT /evidence="ECO:0007829|PDB:5ILB"
FT STRAND 358..363
FT /evidence="ECO:0007829|PDB:5ILB"
FT HELIX 368..371
FT /evidence="ECO:0007829|PDB:5ILB"
FT STRAND 378..382
FT /evidence="ECO:0007829|PDB:5ILB"
FT STRAND 391..395
FT /evidence="ECO:0007829|PDB:5ILB"
FT TURN 396..398
FT /evidence="ECO:0007829|PDB:5ILB"
FT STRAND 399..402
FT /evidence="ECO:0007829|PDB:5ILB"
FT HELIX 404..408
FT /evidence="ECO:0007829|PDB:5ILB"
FT STRAND 415..422
FT /evidence="ECO:0007829|PDB:5ILB"
FT STRAND 425..432
FT /evidence="ECO:0007829|PDB:5ILB"
FT STRAND 451..454
FT /evidence="ECO:0007829|PDB:5ILB"
FT STRAND 457..461
FT /evidence="ECO:0007829|PDB:5ILB"
FT TURN 464..466
FT /evidence="ECO:0007829|PDB:5ILB"
FT HELIX 475..478
FT /evidence="ECO:0007829|PDB:5ILB"
FT HELIX 481..489
FT /evidence="ECO:0007829|PDB:5ILB"
FT STRAND 500..505
FT /evidence="ECO:0007829|PDB:5ILB"
FT HELIX 509..511
FT /evidence="ECO:0007829|PDB:5ILB"
FT STRAND 519..525
FT /evidence="ECO:0007829|PDB:5ILB"
FT HELIX 533..541
FT /evidence="ECO:0007829|PDB:5ILB"
FT STRAND 545..552
FT /evidence="ECO:0007829|PDB:5ILB"
FT TURN 553..555
FT /evidence="ECO:0007829|PDB:5ILB"
FT STRAND 556..561
FT /evidence="ECO:0007829|PDB:5ILB"
FT HELIX 562..567
FT /evidence="ECO:0007829|PDB:5ILB"
FT HELIX 569..575
FT /evidence="ECO:0007829|PDB:5ILB"
FT HELIX 584..586
FT /evidence="ECO:0007829|PDB:5ILB"
SQ SEQUENCE 592 AA; 65153 MW; 9D20C56BEAFBAE08 CRC64;
MKNSEKRGRK HKRQDASSAE NAGGEVKEAS ANEASLPQSP EPVSASEANP SPSRRSRGRG
KKRRLNNESE AGNQRTSSPE RSRSRLHHSD TKNGDCSNGM IVSTTTESIP AAPSWETVVK
VVPSMDAVVK VFCVHTEPNF SLPWQRKRQY SSGSSGFIIG GRRVLTNAHS VEHHTQVKLK
KRGSDTKYLA TVLAIGTECD IALLTVTDDE FWEGVSPVEF GDLPALQDAV TVVGYPIGGD
TISVTSGVVS RMEILSYVHG STELLGLQID AAINSGNSGG PAFNDKGKCV GIAFQSLKHE
DAENIGYVIP TPVIVHFIQD YEKHDKYTGF PVLGIEWQKM ENPDLRKSMG MESHQKGVRI
RRIEPTAPES QVLKPSDIIL SFDGVNIAND GTVPFRHGER IGFSYLISQK YTGDSALVKV
LRNKEILEFN IKLAIHKRLI PAHISGKPPS YFIVAGFVFT TVSVPYLRSE YGKEYEFDAP
VKLLEKHLHA MAQSVDEQLV VVSQVLVSDI NIGYEEIVNT QVVAFNGKPV KNLKGLAGMV
ENCEDEYMKF NLDYDQIVVL DTKTAKEATL DILTTHCIPS AMSDDLKTEE RN
