ID   AARE2_ORYSJ             Reviewed;         772 AA.
AC   Q338C0; Q0IXP8;
DT   16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Acylamino-acid-releasing enzyme 2 {ECO:0000305};
DE            Short=AARE2 {ECO:0000305};
DE            EC=3.4.19.1 {ECO:0000305};
GN   OrderedLocusNames=Os10g0415800 {ECO:0000312|EMBL:BAF26517.1},
GN   LOC_Os10g28030 {ECO:0000312|EMBL:ABB47614.1};
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12791992; DOI=10.1126/science.1083523;
RA   Yu Y., Rambo T., Currie J., Saski C., Kim H.-R., Collura K., Thompson S.,
RA   Simmons J., Yang T.-J., Nah G., Patel A.J., Thurmond S., Henry D.,
RA   Oates R., Palmer M., Pries G., Gibson J., Anderson H., Paradkar M.,
RA   Crane L., Dale J., Carver M.B., Wood T., Frisch D., Engler F.,
RA   Soderlund C., Palmer L.E., Teytelman L., Nascimento L., De la Bastide M.,
RA   Spiegel L., Ware D., O'Shaughnessy A., Dike S., Dedhia N., Preston R.,
RA   Huang E., Ferraro K., Kuit K., Miller B., Zutavern T., Katzenberger F.,
RA   Muller S., Balija V., Martienssen R.A., Stein L., Minx P., Johnson D.,
RA   Cordum H., Mardis E., Cheng Z., Jiang J., Wilson R., McCombie W.R.,
RA   Wing R.A., Yuan Q., Ouyang S., Liu J., Jones K.M., Gansberger K.,
RA   Moffat K., Hill J., Tsitrin T., Overton L., Bera J., Kim M., Jin S.,
RA   Tallon L., Ciecko A., Pai G., Van Aken S., Utterback T., Reidmuller S.,
RA   Bormann J., Feldblyum T., Hsiao J., Zismann V., Blunt S., de Vazeille A.R.,
RA   Shaffer T., Koo H., Suh B., Yang Q., Haas B., Peterson J., Pertea M.,
RA   Volfovsky N., Wortman J., White O., Salzberg S.L., Fraser C.M., Buell C.R.,
RA   Messing J., Song R., Fuks G., Llaca V., Kovchak S., Young S., Bowers J.E.,
RA   Paterson A.H., Johns M.A., Mao L., Pan H., Dean R.A.;
RT   "In-depth view of structure, activity, and evolution of rice chromosome
RT   10.";
RL   Science 300:1566-1569(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
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. {ECO:0000250|UniProtKB:Q84LM4}.
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; Evidence={ECO:0000305};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:Q84LM4}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q84LM4}.
CC   -!- SIMILARITY: Belongs to the peptidase S9C family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAF26517.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; DP000086; ABB47614.1; -; Genomic_DNA.
DR   EMBL; AP008216; BAF26517.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AP014966; BAT10849.1; -; Genomic_DNA.
DR   RefSeq; XP_015614200.1; XM_015758714.1.
DR   AlphaFoldDB; Q338C0; -.
DR   SMR; Q338C0; -.
DR   STRING; 4530.OS10T0415800-01; -.
DR   ESTHER; orysj-q338c0; ACPH_Peptidase_S9.
DR   MEROPS; S09.004; -.
DR   PaxDb; Q338C0; -.
DR   PRIDE; Q338C0; -.
DR   EnsemblPlants; Os10t0415800-01; Os10t0415800-01; Os10g0415800.
DR   GeneID; 4348628; -.
DR   Gramene; Os10t0415800-01; Os10t0415800-01; Os10g0415800.
DR   KEGG; osa:4348628; -.
DR   eggNOG; KOG2100; Eukaryota.
DR   HOGENOM; CLU_014230_1_1_1; -.
DR   OMA; LDFQWSP; -.
DR   OrthoDB; 265965at2759; -.
DR   Proteomes; UP000000763; Chromosome 10.
DR   Proteomes; UP000059680; Chromosome 10.
DR   ExpressionAtlas; Q338C0; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR045550; AARE_N.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR002471; Pept_S9_AS.
DR   InterPro; IPR001375; Peptidase_S9.
DR   Pfam; PF19283; APEH_N; 1.
DR   Pfam; PF00326; Peptidase_S9; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   PROSITE; PS00708; PRO_ENDOPEP_SER; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Hydrolase; Reference proteome.
FT   CHAIN           1..772
FT                   /note="Acylamino-acid-releasing enzyme 2"
FT                   /id="PRO_0000435687"
FT   REGION          164..186
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        617
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10084"
FT   ACT_SITE        708
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10084"
FT   ACT_SITE        740
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10084"
SQ   SEQUENCE   772 AA;  84799 MW;  E3C8001FCE6C94CD CRC64;
     MDALASEEYA SQSKLLQEFT NAPSIDGAWV FQTNNEDRST AMYSISQTNL LANNKRKYIL
     FSHIMRNGTN LLDFQWSPFP IQMDGVSAVV PSPSGSKLLV VRNGEKGSPT KLEIVDQSHV
     EKEIHVAQSV HGPLYTDEWF HGISWNQEET LIAYIAEDSP EPKPVFDDTG YRKEGSSEKD
     CNNWKGQGDW EEDWGETYSK KGRPSLFVLD INSGEVRAAK GISRSLSVGQ VVWAPPSSCG
     RQKYLIFVGW LEHNGFQNTP RKLGIKYCSN RPCSLYSTLC PFEESDVDNA PASDSKLEPA
     SVAINLTPSI SSAFFPRFSK DGKLLVFLSA NRAVDSGAHN ATDSLHKINW PSDWKMDQYL
     EITDVIPIVM CPQDGCFPGL YCSSMLSNPW LSDRCTMILT SAWRSTEVIL SIDVLSGKAT
     RISPENSEYS WSALAVDGHN VLAVSSSPID PPQIKYGHQV SLKDQTCTWV WDEVNNNPLM
     AANNKVKALL SHHQFSILKI PVTNPSDDLS DGSKLPFEAI FVSCKDSSHK PTILVLHGGP
     HSVSVSSYSK TSAFLASLGF NLLIVNYRGT PGFGEEALQS LPGKVGSQDV QDCLTALDYV
     IEGGLIDASK VAVIGISHGG FLTTHLIGQA PDRFMVAAAR NPVCNLSLMI GTTDIPDWCY
     AVACGSEGRQ HASESPSPDH LRLFYQKSPI AHISKVKAPL LMLLGGADLR VPISNGLQYA
     RALRERGGEI RIMMFPDDIH EINIPQSDFE SFLNIGVWFK KHLSISASDA SA