DEG15_ARATH
ID DEG15_ARATH Reviewed; 709 AA.
AC Q8VZD4; Q9FZA5;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 2.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Glyoxysomal processing protease, glyoxysomal;
DE Short=AtDEG15;
DE EC=3.4.21.-;
DE AltName: Full=DEG-protease;
GN Name=DEG15; Synonyms=GPP; OrderedLocusNames=At1g28320;
GN ORFNames=F3H9.2, F3H9.3;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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 SUBCELLULAR LOCATION.
RX PubMed=15333753; DOI=10.1104/pp.104.043695;
RA Reumann S., Ma C., Lemke S., Babujee L.;
RT "AraPerox. A database of putative Arabidopsis proteins from plant
RT peroxisomes.";
RL Plant Physiol. 136:2587-2608(2004).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17592111; DOI=10.1073/pnas.0704733104;
RA Helm M., Lueck C., Prestele J., Hierl G., Huesgen P.F., Froehlich T.,
RA Arnold G.J., Adamska I., Goerg A., Lottspeich F., Gietl C.;
RT "Dual specificities of the glyoxysomal/peroxisomal processing protease
RT Deg15 in higher plants.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:11501-11506(2007).
RN [6]
RP FUNCTION, MUTAGENESIS OF SER-237; SER-252; CYS-276; SER-377; HIS-392;
RP 397-TRP--HIS-462; ASP-491; CYS-532; SER-540; SER-580 AND SER-613, ACTIVITY
RP REGULATION, SUBUNIT, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=18952862; DOI=10.1104/pp.108.125377;
RA Schuhmann H., Huesgen P.F., Gietl C., Adamska I.;
RT "The DEG15 serine protease cleaves peroxisomal targeting signal 2-
RT containing proteins in Arabidopsis.";
RL Plant Physiol. 148:1847-1856(2008).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19748917; DOI=10.1104/pp.109.142505;
RA Lingard M.J., Bartel B.;
RT "Arabidopsis LON2 is necessary for peroxisomal function and sustained
RT matrix protein import.";
RL Plant Physiol. 151:1354-1365(2009).
CC -!- FUNCTION: Trypsin-like serine endopeptidase involved in the processing
CC of glyoxysomal higher molecular weight precursor. The dimeric form
CC carries out the specific cleavages needed to remove PTS2-containing
CC presequences, whereas the monomeric form degrades the removed
CC presequences and misfolded proteins (Probable). Not required for
CC degradation of glyoxylate cycle enzymes during seedling development.
CC {ECO:0000269|PubMed:17592111, ECO:0000269|PubMed:18952862,
CC ECO:0000269|PubMed:19748917, ECO:0000305}.
CC -!- ACTIVITY REGULATION: Inhibited by N-methylmaleimide (NEM), but not by
CC E64, benzamidine, aprotinin, leupeptin, pefabloc, pepstatin A, EGTA,
CC EDTA and 1,10-phenanthroline. {ECO:0000269|PubMed:18952862}.
CC -!- SUBUNIT: Monomer and homodimer. Multimerization requires calcium ions
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:15333753,
CC ECO:0000269|PubMed:18952862}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype, but loss of processing of
CC glyoxysomal precursor proteins. Increased resistance to the herbicide
CC precursor 4-(2,4-dichlorophenoxy) butyric acid (2,4-DB) and to the
CC inhibitory effects of indole-3-butyric acid (IBA) on root elongation.
CC {ECO:0000269|PubMed:17592111, ECO:0000269|PubMed:18952862,
CC ECO:0000269|PubMed:19748917}.
CC -!- SIMILARITY: Belongs to the peptidase S1B family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF98423.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC021044; AAF98423.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE30952.1; -; Genomic_DNA.
DR EMBL; AY065045; AAL57680.1; -; mRNA.
DR PIR; E86409; E86409.
DR RefSeq; NP_174153.2; NM_102597.5.
DR AlphaFoldDB; Q8VZD4; -.
DR BioGRID; 24961; 2.
DR STRING; 3702.AT1G28320.1; -.
DR MEROPS; S01.501; -.
DR PaxDb; Q8VZD4; -.
DR PRIDE; Q8VZD4; -.
DR ProteomicsDB; 224246; -.
DR EnsemblPlants; AT1G28320.1; AT1G28320.1; AT1G28320.
DR GeneID; 839726; -.
DR Gramene; AT1G28320.1; AT1G28320.1; AT1G28320.
DR KEGG; ath:AT1G28320; -.
DR Araport; AT1G28320; -.
DR TAIR; locus:2032142; AT1G28320.
DR eggNOG; KOG1320; Eukaryota.
DR HOGENOM; CLU_027990_0_0_1; -.
DR InParanoid; Q8VZD4; -.
DR OMA; IELCAIR; -.
DR OrthoDB; 1307240at2759; -.
DR PRO; PR:Q8VZD4; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8VZD4; baseline and differential.
DR Genevisible; Q8VZD4; AT.
DR GO; GO:0005777; C:peroxisome; IDA:TAIR.
DR GO; GO:0004175; F:endopeptidase activity; IMP:TAIR.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0016485; P:protein processing; IBA:GO_Central.
DR Gene3D; 2.40.10.10; -; 3.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR039245; TYSND1/DEG15.
DR PANTHER; PTHR21004; PTHR21004; 1.
DR SUPFAM; SSF50494; SSF50494; 2.
PE 1: Evidence at protein level;
KW Hydrolase; Peroxisome; Protease; Reference proteome; Serine protease.
FT CHAIN 1..709
FT /note="Glyoxysomal processing protease, glyoxysomal"
FT /id="PRO_0000403449"
FT ACT_SITE 392
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 491
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 580
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT MUTAGEN 237
FT /note="S->A: 75% reduction of proteolytic activity."
FT /evidence="ECO:0000269|PubMed:18952862"
FT MUTAGEN 252
FT /note="S->A: 75% reduction of proteolytic activity."
FT /evidence="ECO:0000269|PubMed:18952862"
FT MUTAGEN 276
FT /note="C->A: Slightly increased proteolytic activity."
FT /evidence="ECO:0000269|PubMed:18952862"
FT MUTAGEN 377
FT /note="S->A: 90% reduction of proteolytic activity."
FT /evidence="ECO:0000269|PubMed:18952862"
FT MUTAGEN 392
FT /note="H->A: Total loss of proteolytic activity."
FT /evidence="ECO:0000269|PubMed:18952862"
FT MUTAGEN 397..462
FT /note="Missing: 25% reduction of proteolytic activity."
FT /evidence="ECO:0000269|PubMed:18952862"
FT MUTAGEN 491
FT /note="D->A: Total loss of proteolytic activity."
FT /evidence="ECO:0000269|PubMed:18952862"
FT MUTAGEN 532
FT /note="C->A: Slightly increased proteolytic activity."
FT /evidence="ECO:0000269|PubMed:18952862"
FT MUTAGEN 540
FT /note="S->A: No effect."
FT /evidence="ECO:0000269|PubMed:18952862"
FT MUTAGEN 580
FT /note="S->A: Total loss of proteolytic activity."
FT /evidence="ECO:0000269|PubMed:18952862"
FT MUTAGEN 613
FT /note="S->A: No effect."
FT /evidence="ECO:0000269|PubMed:18952862"
FT CONFLICT 124
FT /note="A -> S (in Ref. 3; AAL57680)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 709 AA; 76126 MW; 5C9D9E7F5562FAE6 CRC64;
MDVSKVVSFS RNFAVLVKVE GPDPKGLKMR KHAFHQYHSG NATLSASGIL LPRDIFLSGE
VAAKVLFEAG QDMALVLTVA SVVEPFLTLG HRTSSSISQD PVKLIPGAMI EIMVEGQLKS
EKEAPFWVPA QLLSLVDVPV SSAALQSLIE ASSGSKDSGW DIGWSLVSAA NGSQPSINIE
HYSKPLMQLD EPHNANFMAK SATRMAILGV PLSLLGQPSM NFASSSSKGD TLVALGSPFG
ILSPVNFFNS VSTGSIANSY PSGSLKKSLM IADVRCLPGM EGAPVFAKNG HLIGILIRPL
RQKNSGVEIQ LVVPWGAITT ACSHLLLEEP SVEGKASQWG SEVLSVKSDA SIPAQVAIEK
AMESVCLITV NDGVWASGII LNEHGLILTN AHLLEPWRYG KGGVYGEGFK PYVLGAEEFS
STGSKFWEQK SQTLPRKAPR NHYSSVGENI REYKHNFLQT GHRDIRVRLC HLDSWTWCPA
NVVYICKEQL DIALLQLEYV PGKLQPITAN FSSPPLGTTA HVVGHGLFGP RCGLSPSICS
GVVAKVVHAK RRLNTQSISQ EVAEFPAMLE TTAAVHPGGS GGAVLNSSGH MIGLVTSNAR
HGAGTVIPHL NFSIPCAVLA PIFKFAEDMQ NTTILQTLDQ PSEELSSIWA LMPSLSPKTE
QSLPNLPKLL KDGNNKQTKG SQFAKFIAET QDMFVKPTKL SRDVIPSKL
