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Acylamino-acid-releasing enzyme (AARE) (EC 3.4.19.1) (Oxidized protein hydrolase) (OPH)

 AARE_ARATH              Reviewed;         764 AA.
Q84LM4; O23313;
16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
01-JUN-2003, sequence version 1.
12-SEP-2018, entry version 119.
RecName: Full=Acylamino-acid-releasing enzyme {ECO:0000305};
Short=AARE {ECO:0000303|PubMed:12966075};
EC=3.4.19.1 {ECO:0000269|PubMed:12966075};
AltName: Full=Oxidized protein hydrolase {ECO:0000303|PubMed:22398639};
Short=OPH {ECO:0000303|PubMed:22398639};
Name=AARE {ECO:0000303|PubMed:12966075};
OrderedLocusNames=At4g14570 {ECO:0000312|Araport:AT4G14570};
ORFNames=dl3325w {ECO:0000312|EMBL:CAB10236.1};
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, ACTIVE SITES, AND
MUTAGENESIS OF SER-618; ASP-707 AND HIS-739.
PubMed=12966075; DOI=10.1093/jb/mvg138;
Yamauchi Y., Ejiri Y., Toyoda Y., Tanaka K.;
"Identification and biochemical characterization of plant acylamino
acid-releasing enzyme.";
J. Biochem. 134:251-257(2003).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=9461215; DOI=10.1038/35140;
Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L.,
Ridley P., Hudson S.-A., Patel K., Murphy G., Piffanelli P.,
Wedler H., Wedler E., Wambutt R., Weitzenegger T., Pohl T., Terryn N.,
Gielen J., Villarroel R., De Clercq R., van Montagu M., Lecharny A.,
Aubourg S., Gy I., Kreis M., Lao N., Kavanagh T., Hempel S.,
Kotter P., Entian K.-D., Rieger M., Schaefer M., Funk B.,
Mueller-Auer S., Silvey M., James R., Monfort A., Pons A.,
Puigdomenech P., Douka A., Voukelatou E., Milioni D., Hatzopoulos P.,
Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A., Moores T.,
Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S., Ansorge W.,
Cooke R., Berger C., Delseny M., Voet M., Volckaert G., Mewes H.-W.,
Klosterman S., Schueller C., Chalwatzis N.;
"Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of
Arabidopsis thaliana.";
Nature 391:485-488(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617198; DOI=10.1038/47134;
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G.,
Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N.,
Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M.,
Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M.,
Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T.,
Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I.,
Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P.,
Langham S.-A., McCullagh B., Bilham L., Robben J.,
van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F.,
Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E.,
Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W.,
Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P.,
Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H.,
De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R.,
van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S.,
Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R.,
Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S.,
Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H.,
Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S.,
Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A.,
Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R.,
Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S.,
Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E.,
Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A.,
Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T.,
Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C.,
Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S.,
Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K.,
Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L.,
Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J.,
Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J.,
Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D.,
Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D.,
Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C.,
Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C.,
Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R.,
Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S.,
Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A.,
Chen E., Marra M.A., Martienssen R., McCombie W.R.;
"Sequence and analysis of chromosome 4 of the plant Arabidopsis
thaliana.";
Nature 402:769-777(1999).
[4]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[5]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=22398639; DOI=10.1007/s00425-012-1614-1;
Nakai A., Yamauchi Y., Sumi S., Tanaka K.;
"Role of acylamino acid-releasing enzyme/oxidized protein hydrolase in
sustaining homeostasis of the cytoplasmic antioxidative system.";
Planta 236:427-436(2012).
-!- FUNCTION: Catalyzes the hydrolysis of the N-terminal peptide bond
of an N-acetylated peptide to generate an N-acetylated amino acid
and a peptide with a free N-terminus. Can degrade the glycated
RuBisCO (ribulose-1,5-bisphoshate carboxylase/oxygenase) protein
but not the native protein. May be involved in the elimination of
glycated proteins (PubMed:12966075). Plays a homeostatic role in
sustaining the cytoplasmic antioxidative system. May contribute to
the elimination of the oxidized proteins in the cytoplasm
(PubMed:22398639). {ECO:0000269|PubMed:12966075,
ECO:0000269|PubMed:22398639}.
-!- CATALYTIC ACTIVITY: Cleavage of an N-acetyl or N-formyl amino acid
from the N-terminus of a polypeptide.
{ECO:0000269|PubMed:12966075}.
-!- ACTIVITY REGULATION: Strongly inhibited by the serine protease
inhibitor diisopropyl fluorophosphate.
{ECO:0000269|PubMed:12966075}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=1.5 mM for Ac-Ala-pNA {ECO:0000269|PubMed:12966075};
pH dependence:
Optimum pH is 7.0. {ECO:0000269|PubMed:12966075};
-!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:12966075}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22398639}.
Nucleus {ECO:0000269|PubMed:22398639}.
-!- MISCELLANEOUS: Plants silencing AARE show enhanced ion leakage
after oxidative treatment. {ECO:0000269|PubMed:22398639}.
-!- SIMILARITY: Belongs to the peptidase S9C family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAB10236.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=CAB78499.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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EMBL; AB109759; BAC76411.1; -; mRNA.
EMBL; Z97336; CAB10236.1; ALT_SEQ; Genomic_DNA.
EMBL; AL161539; CAB78499.1; ALT_SEQ; Genomic_DNA.
EMBL; CP002687; -; NOT_ANNOTATED_CDS; Genomic_DNA.
PIR; B71408; B71408.
ProteinModelPortal; Q84LM4; -.
STRING; 3702.AT4G14570.1; -.
ESTHER; arath-AARE; ACPH_Peptidase_S9.
MEROPS; S09.004; -.
PaxDb; Q84LM4; -.
PRIDE; Q84LM4; -.
ProMEX; Q84LM4; -.
EnsemblPlants; AT4G14570.1; AT4G14570.1; AT4G14570.
Gramene; AT4G14570.1; AT4G14570.1; AT4G14570.
Araport; AT4G14570; -.
TAIR; locus:2129920; AT4G14570.
eggNOG; KOG2100; Eukaryota.
eggNOG; COG1506; LUCA.
HOGENOM; HOG000243442; -.
OMA; PEQENVQ; -.
OrthoDB; EOG093602P3; -.
PhylomeDB; Q84LM4; -.
BRENDA; 3.4.19.1; 399.
Reactome; R-ATH-6798695; Neutrophil degranulation.
Reactome; R-ATH-72764; Eukaryotic Translation Termination.
PRO; PR:Q84LM4; -.
Proteomes; UP000006548; Chromosome 4.
ExpressionAtlas; Q84LM4; baseline and differential.
GO; GO:0009507; C:chloroplast; IDA:TAIR.
GO; GO:0005737; C:cytoplasm; IDA:TAIR.
GO; GO:0005634; C:nucleus; IDA:TAIR.
GO; GO:0005773; C:vacuole; IDA:TAIR.
GO; GO:0070009; F:serine-type aminopeptidase activity; IDA:TAIR.
GO; GO:0051289; P:protein homotetramerization; IPI:UniProtKB.
GO; GO:0006508; P:proteolysis; IDA:TAIR.
Gene3D; 3.40.50.1820; -; 1.
InterPro; IPR029058; AB_hydrolase.
InterPro; IPR011659; PD40.
InterPro; IPR001375; Peptidase_S9.
Pfam; PF07676; PD40; 1.
Pfam; PF00326; Peptidase_S9; 1.
SUPFAM; SSF53474; SSF53474; 1.
1: Evidence at protein level;
Complete proteome; Cytoplasm; Hydrolase; Nucleus; Reference proteome.
CHAIN 1 764 Acylamino-acid-releasing enzyme.
/FTId=PRO_0000435685.
ACT_SITE 618 618 Charge relay system.
{ECO:0000255|PROSITE-ProRule:PRU10084,
ECO:0000269|PubMed:12966075}.
ACT_SITE 707 707 Charge relay system.
{ECO:0000255|PROSITE-ProRule:PRU10084,
ECO:0000269|PubMed:12966075}.
ACT_SITE 739 739 Charge relay system.
{ECO:0000255|PROSITE-ProRule:PRU10084,
ECO:0000269|PubMed:12966075}.
MUTAGEN 618 618 S->A: Loss of catalytic activity.
{ECO:0000269|PubMed:12966075}.
MUTAGEN 707 707 D->N: Loss of catalytic activity.
{ECO:0000269|PubMed:12966075}.
MUTAGEN 739 739 H->A: Loss of catalytic activity.
{ECO:0000269|PubMed:12966075}.
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


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