PREP2_ARATH
ID PREP2_ARATH Reviewed; 1080 AA.
AC Q8VY06; Q9FX91;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Presequence protease 2, chloroplastic/mitochondrial;
DE Short=AtPreP2;
DE Short=PreP 2;
DE EC=3.4.24.-;
DE AltName: Full=Zinc metalloprotease 2;
DE Short=AtZnMP2;
DE Flags: Precursor;
GN Name=PREP2; Synonyms=ZNMP2; OrderedLocusNames=At1g49630;
GN ORFNames=F14J22.13;
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 IDENTIFICATION BY MASS SPECTROMETRY, AND FUNCTION.
RX PubMed=12138166; DOI=10.1074/jbc.m205500200;
RA Staahl A., Moberg P., Ytterberg J., Panfilov O.,
RA Brockenhuus Von Lowenhielm H., Nilsson F., Glaser E.;
RT "Isolation and identification of a novel mitochondrial metalloprotease
RT (PreP) that degrades targeting presequences in plants.";
RL J. Biol. Chem. 277:41931-41939(2002).
RN [5]
RP CHARACTERIZATION, IDENTIFICATION BY MASS SPECTROMETRY, TISSUE SPECIFICITY,
RP AND SUBCELLULAR LOCATION.
RX PubMed=15827031; DOI=10.1093/pcp/pci107;
RA Bhushan S., Staahl A., Nilsson S., Lefebvre B., Seki M., Roth C.,
RA McWilliam D., Wright S.J., Liberles D.A., Shinozaki K., Bruce B.D.,
RA Boutry M., Glaser E.;
RT "Catalysis, subcellular localization, expression and evolution of the
RT targeting peptides degrading protease, AtPreP2.";
RL Plant Cell Physiol. 46:985-996(2005).
RN [6]
RP CLEAVAGE SPECIFICITY.
RX PubMed=15893767; DOI=10.1016/j.jmb.2005.04.023;
RA Staahl A., Nilsson S., Lundberg P., Bhushan S., Biverstaahl H., Moberg P.,
RA Morisset M., Vener A., Maeler L., Langel U., Glaser E.;
RT "Two novel targeting peptide degrading proteases, PrePs, in mitochondria
RT and chloroplasts, so similar and still different.";
RL J. Mol. Biol. 349:847-860(2005).
CC -!- FUNCTION: ATP-independent protease that degrades both mitochondrial and
CC chloroplastic transit peptides after their cleavage. Also degrades
CC other unstructured peptides. Specific for peptides in the range of 10
CC to 65 residues. Shows a preference for cleavage after small polar
CC residues and before basic residues, but without any positional
CC preference. {ECO:0000269|PubMed:12138166}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Note=Binds 1 zinc ion per subunit.;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 2 Magnesium ions per subunit. {ECO:0000250};
CC -!- ACTIVITY REGULATION: Completely inhibited by the metal chelator
CC orthophenanthroline.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000269|PubMed:15827031}. Mitochondrion matrix
CC {ECO:0000269|PubMed:15827031}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves, flowers and roots, but not
CC detected in siliques and shoots. {ECO:0000269|PubMed:15827031}.
CC -!- SIMILARITY: Belongs to the peptidase M16 family. PreP subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG13049.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC011807; AAG13049.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE32451.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32452.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32453.1; -; Genomic_DNA.
DR EMBL; AY074305; AAL67002.1; -; mRNA.
DR EMBL; BT004376; AAO42370.1; -; mRNA.
DR PIR; A96533; A96533.
DR RefSeq; NP_175386.2; NM_103851.3.
DR RefSeq; NP_850961.1; NM_180630.2.
DR RefSeq; NP_850962.1; NM_180631.2.
DR AlphaFoldDB; Q8VY06; -.
DR SMR; Q8VY06; -.
DR BioGRID; 26612; 15.
DR STRING; 3702.AT1G49630.1; -.
DR MEROPS; M16.018; -.
DR MetOSite; Q8VY06; -.
DR PaxDb; Q8VY06; -.
DR PRIDE; Q8VY06; -.
DR ProteomicsDB; 236597; -.
DR EnsemblPlants; AT1G49630.1; AT1G49630.1; AT1G49630.
DR EnsemblPlants; AT1G49630.2; AT1G49630.2; AT1G49630.
DR EnsemblPlants; AT1G49630.3; AT1G49630.3; AT1G49630.
DR GeneID; 841387; -.
DR Gramene; AT1G49630.1; AT1G49630.1; AT1G49630.
DR Gramene; AT1G49630.2; AT1G49630.2; AT1G49630.
DR Gramene; AT1G49630.3; AT1G49630.3; AT1G49630.
DR KEGG; ath:AT1G49630; -.
DR Araport; AT1G49630; -.
DR TAIR; locus:2012176; AT1G49630.
DR eggNOG; KOG2019; Eukaryota.
DR HOGENOM; CLU_009165_1_0_1; -.
DR InParanoid; Q8VY06; -.
DR OrthoDB; 107079at2759; -.
DR PhylomeDB; Q8VY06; -.
DR PRO; PR:Q8VY06; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8VY06; baseline and differential.
DR Genevisible; Q8VY06; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR GO; GO:0016485; P:protein processing; IDA:TAIR.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR007863; Peptidase_M16_C.
DR InterPro; IPR013578; Peptidase_M16C_assoc.
DR Pfam; PF08367; M16C_assoc; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 1.
DR SMART; SM01264; M16C_associated; 1.
DR SUPFAM; SSF63411; SSF63411; 4.
PE 1: Evidence at protein level;
KW Chloroplast; Hydrolase; Magnesium; Metal-binding; Metalloprotease;
KW Mitochondrion; Plastid; Protease; Reference proteome; Transit peptide;
KW Zinc.
FT TRANSIT 1..84
FT /note="Chloroplast and mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 85..1080
FT /note="Presequence protease 2, chloroplastic/mitochondrial"
FT /id="PRO_0000249939"
FT ACT_SITE 164
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9LJL3"
FT ACT_SITE 239
FT /evidence="ECO:0000250|UniProtKB:Q9LJL3"
FT BINDING 161
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9LJL3"
FT BINDING 165
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9LJL3"
FT BINDING 261
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9LJL3"
SQ SEQUENCE 1080 AA; 121131 MW; 23425D0E7376E39E CRC64;
MLRSLTCSST ITSTSLFFRS FRQLPRSYLS PSSSTTVVGA SGRNIRRLST LEAAGRRLFL
RRGLKLLSAA SRGLNGQFSR LSIRAVATQS APSSYPGQDE AEKLGFEKVS EEFISECKSK
AVLFKHKKTG CEVMSVSNDD ENKVFGIVFR TPPKDSTGIP HILEHSVLCG SRKYPMKEPF
VELLKGSLHT FLNAFTYPDR TCYPVASTNK KDFYNLVDVY LDAVFFPKCV DDVHTFQQEG
WHYELNDPSE DISYKGVVFN EMKGVYSQPD NILGRVTQQA LCPENTYGVD SGGDPKDIPK
LTFEKFKEFH RQYYHPSNAR IWFYGDDDPV HRLRVLSEYL DMFDASPARD SSKVEPQKLF
SRPRRIVEKY PAGEDGDLKK KHMVCLNWLL SDKPLDLQTQ LALGFLDHLM LGTPASPLRK
ILLESGLGEA LVNSGMEDEL LQPQFSIGLK GVSDDNVQKV EELVMNTLRK LADEGFDTDA
VEASMNTIEF SLRENNTGSS PRGLSLMLQS IAKWIYDMDP FEPLKYEEPL KSLKARIAEK
GSKSVFSPLI EEYILNNPHC VTIEMQPDPE KASLEEAEEK SILEKVKASM TEEDLTELAR
ATEELRLKQE TPDPPDALKC VPSLNLSDIP KEPIYVPTEV GDINGVKVLR NDLFTNNILY
TEVVFDMGSV KHELLQLIPL FCQSLLEMGT QDLTFVQLNQ LIGRKTGGIS VYPLTSSVYG
RDDPCSKIIV RGKSMVGRAE DLFNLMNCVL QEVRFTDQQR FKQFVSQSRA RMENRLRGSG
QGIAAARMDA MLNVAGWMSE QMGGLSYLEF LHTLEQKVDQ DWEGISSSLE EIRRSFLSRN
GCIVNMTADG KSLTNTEKYV GKFLDLLPEN PSGELVTWDA RLPLRNEAIV IPTQVNYVGK
AGNIYSSGYK LDGSSYVISK HISNTWLWDR VRVSGGAYGG SCDFDSHSGV FSFLSYRDPN
LLKTLDIYDG TGDFLRGLDV DEDTLTKAII GTIGDVDSYQ LPDAKGYTSL LRHLLNVTDE
ERQIRREEIL STSLKDFKEF AEAIDSVSDK GVAVAVASQE DIDAANRERS NFFEVKKAAL
