AARE_ARATH
ID AARE_ARATH Reviewed; 764 AA.
AC Q84LM4; O23313;
DT 16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 138.
DE RecName: Full=Acylamino-acid-releasing enzyme {ECO:0000305};
DE Short=AARE {ECO:0000303|PubMed:12966075};
DE EC=3.4.19.1 {ECO:0000269|PubMed:12966075};
DE AltName: Full=Oxidized protein hydrolase {ECO:0000303|PubMed:22398639};
DE Short=OPH {ECO:0000303|PubMed:22398639};
GN Name=AARE {ECO:0000303|PubMed:12966075};
GN OrderedLocusNames=At4g14570 {ECO:0000312|Araport:AT4G14570};
GN ORFNames=dl3325w {ECO:0000312|EMBL:CAB10236.1};
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, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, ACTIVE SITES, AND
RP MUTAGENESIS OF SER-618; ASP-707 AND HIS-739.
RX PubMed=12966075; DOI=10.1093/jb/mvg138;
RA Yamauchi Y., Ejiri Y., Toyoda Y., Tanaka K.;
RT "Identification and biochemical characterization of plant acylamino acid-
RT releasing enzyme.";
RL J. Biochem. 134:251-257(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9461215; DOI=10.1038/35140;
RA Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT thaliana.";
RL Nature 391:485-488(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [4]
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 [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=22398639; DOI=10.1007/s00425-012-1614-1;
RA Nakai A., Yamauchi Y., Sumi S., Tanaka K.;
RT "Role of acylamino acid-releasing enzyme/oxidized protein hydrolase in
RT sustaining homeostasis of the cytoplasmic antioxidative system.";
RL Planta 236:427-436(2012).
CC -!- FUNCTION: Catalyzes the hydrolysis of the N-terminal peptide bond of an
CC N-acetylated peptide to generate an N-acetylated amino acid and a
CC peptide with a free N-terminus. Can degrade the glycated RuBisCO
CC (ribulose-1,5-bisphosphate carboxylase/oxygenase) protein but not the
CC native protein. May be involved in the elimination of glycated proteins
CC (PubMed:12966075). Plays a homeostatic role in sustaining the
CC cytoplasmic antioxidative system. May contribute to the elimination of
CC the oxidized proteins in the cytoplasm (PubMed:22398639).
CC {ECO:0000269|PubMed:12966075, ECO:0000269|PubMed:22398639}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleavage of an N-acetyl or N-formyl amino acid from the N-
CC terminus of a polypeptide.; EC=3.4.19.1;
CC Evidence={ECO:0000269|PubMed:12966075};
CC -!- ACTIVITY REGULATION: Strongly inhibited by the serine protease
CC inhibitor diisopropyl fluorophosphate. {ECO:0000269|PubMed:12966075}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.5 mM for Ac-Ala-pNA {ECO:0000269|PubMed:12966075};
CC pH dependence:
CC Optimum pH is 7.0. {ECO:0000269|PubMed:12966075};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:12966075}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22398639}. Nucleus
CC {ECO:0000269|PubMed:22398639}.
CC -!- MISCELLANEOUS: Plants silencing AARE show enhanced ion leakage after
CC oxidative treatment. {ECO:0000269|PubMed:22398639}.
CC -!- SIMILARITY: Belongs to the peptidase S9C family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB10236.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB78499.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB109759; BAC76411.1; -; mRNA.
DR EMBL; Z97336; CAB10236.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161539; CAB78499.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; B71408; B71408.
DR AlphaFoldDB; Q84LM4; -.
DR STRING; 3702.AT4G14570.1; -.
DR ESTHER; arath-AARE; ACPH_Peptidase_S9.
DR iPTMnet; Q84LM4; -.
DR PaxDb; Q84LM4; -.
DR PRIDE; Q84LM4; -.
DR ProMEX; Q84LM4; -.
DR ProteomicsDB; 244579; -.
DR EnsemblPlants; AT4G14570.1; AT4G14570.1; AT4G14570.
DR Gramene; AT4G14570.1; AT4G14570.1; AT4G14570.
DR Araport; AT4G14570; -.
DR TAIR; locus:2129920; AT4G14570.
DR eggNOG; KOG2100; Eukaryota.
DR HOGENOM; CLU_014230_1_1_1; -.
DR InParanoid; Q84LM4; -.
DR PhylomeDB; Q84LM4; -.
DR BRENDA; 3.4.19.1; 399.
DR PRO; PR:Q84LM4; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q84LM4; baseline and differential.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0005773; C:vacuole; HDA:TAIR.
DR GO; GO:0070009; F:serine-type aminopeptidase activity; IDA:TAIR.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0051289; P:protein homotetramerization; IPI:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IDA:TAIR.
DR Gene3D; 2.120.10.30; -; 1.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR045550; AARE_N.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR011659; PD40.
DR InterPro; IPR001375; Peptidase_S9.
DR Pfam; PF19283; APEH_N; 1.
DR Pfam; PF07676; PD40; 1.
DR Pfam; PF00326; Peptidase_S9; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Hydrolase; Nucleus; Reference proteome.
FT CHAIN 1..764
FT /note="Acylamino-acid-releasing enzyme"
FT /id="PRO_0000435685"
FT ACT_SITE 618
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10084,
FT ECO:0000269|PubMed:12966075"
FT ACT_SITE 707
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10084,
FT ECO:0000269|PubMed:12966075"
FT ACT_SITE 739
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10084,
FT ECO:0000269|PubMed:12966075"
FT MUTAGEN 618
FT /note="S->A: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:12966075"
FT MUTAGEN 707
FT /note="D->N: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:12966075"
FT MUTAGEN 739
FT /note="H->A: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:12966075"
SQ SEQUENCE 764 AA; 83938 MW; 2D46D0BEC900E3C1 CRC64;
MDSSGTDSAK ELHVGLDPTT EEEYATQSKL LQEFINIPSI DKAWIFNSDS GSQAMFALSQ
ANLLANKKKK FMLSGHISNE SNQSVNFHWA PFPIEMTGAS AFVPSPSGLK LLVIRNPENE
SPTKFEIWNS SQLEKEFHIP QKVHGSVYVD GWFEGISWDS DETHVAYVAE EPSRPKPTFD
HLGYYKKENS LDKGIGSWKG EGDWEEEWGE AYAGKRQPAL FVINVDSGEV EPIKGIPRSI
SVGQVVWSPN SNGSAQYLVF AGWLGDKRKF GIKYCYNRPC AIYAIKFTSD EPKDDDANEF
PIHNLTKSIS SGFCPRFSKD GKFLVFVSAK TAVDSGAHWA TESLHRIDWP SDGKLPESTN
IVDVIQVVNC PKDGCFPGLY VTGLLSDPWL SDGHSLMLST YWRSCRVILS VNLLSGEVSR
ASPSDSDYSW NALALDGDSI VAVSSSPVSV PEIKYGKKGL DSAGKPSWLW SNIQSPIRYS
EKVMAGLSSL QFKILKVPIS DVSEGLAEGA KNPIEAIYVS SSKSKENGKC DPLIAVLHGG
PHSVSPCSFS RTMAYLSSIG YSQLIINYRG SLGYGEDALQ SLPGKVGSQD VKDCLLAVDH
AIEMGIADPS RITVLGGSHG GFLTTHLIGQ APDKFVAAAA RNPVCNMASM VGITDIPDWC
FFEAYGDQSH YTEAPSAEDL SRFHQMSPIS HISKVKTPTL FLLGTKDLRV PISNGFQYVR
ALKEKGVEVK VLVFPNDNHP LDRPQTDYES FLNIAVWFNK YCKL
