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Protein

Presequence protease 2, chloroplastic/mitochondrial

Gene

PREP2

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

ATP-independent protease that degrades both mitochondrial and chloroplastic transit peptides after their cleavage. Also degrades other unstructured peptides. Specific for peptides in the range of 10 to 65 residues. Shows a preference for cleavage after small polar residues and before basic residues, but without any positional preference.1 Publication

Cofactori

Protein has several cofactor binding sites:
  • Zn2+Note: Binds 1 zinc ion per subunit.
  • Mg2+By similarityNote: Binds 2 Magnesium ions per subunit.By similarity

Enzyme regulationi

Completely inhibited by the metal chelator orthophenanthroline.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi161 – 1611ZincBy similarity
Active sitei164 – 1641Proton acceptorBy similarity
Metal bindingi165 – 1651ZincBy similarity
Metal bindingi261 – 2611ZincBy similarity

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. metallopeptidase activity Source: UniProtKB-KW

GO - Biological processi

  1. protein processing Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Magnesium, Metal-binding, Zinc

Enzyme and pathway databases

BioCyciARA:GQT-933-MONOMER.
ARA:GQT-934-MONOMER.
ARA:GQT-935-MONOMER.

Protein family/group databases

MEROPSiM16.018.

Names & Taxonomyi

Protein namesi
Recommended name:
Presequence protease 2, chloroplastic/mitochondrial (EC:3.4.24.-)
Short name:
AtPreP2
Short name:
PreP 2
Alternative name(s):
Zinc metalloprotease 2
Short name:
AtZnMP2
Gene namesi
Name:PREP2
Synonyms:ZNMP2
Ordered Locus Names:At1g49630
ORF Names:F14J22.13
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 1

Organism-specific databases

TAIRiAT1G49630.

Subcellular locationi

  1. Plastidchloroplast stroma 1 Publication
  2. Mitochondrion matrix 1 Publication

GO - Cellular componenti

  1. chloroplast Source: TAIR
  2. chloroplast stroma Source: UniProtKB-SubCell
  3. mitochondrial matrix Source: UniProtKB-SubCell
  4. mitochondrion Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Mitochondrion, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 8484Chloroplast and mitochondrionSequence AnalysisAdd
BLAST
Chaini85 – 1080996Presequence protease 2, chloroplastic/mitochondrialPRO_0000249939Add
BLAST

Proteomic databases

PaxDbiQ8VY06.
PRIDEiQ8VY06.

Expressioni

Tissue specificityi

Expressed in leaves, flowers and roots, but not detected in siliques and shoots.1 Publication

Gene expression databases

GenevestigatoriQ8VY06.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi3702.AT1G49630.1-P.

Structurei

3D structure databases

ProteinModelPortaliQ8VY06.
SMRiQ8VY06. Positions 99-1077.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M16 family. PreP subfamily.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG1026.
HOGENOMiHOG000008829.
InParanoidiQ8VY06.
KOiK06972.
OMAiFTNDILY.
PhylomeDBiQ8VY06.

Family and domain databases

Gene3Di3.30.830.10. 1 hit.
InterProiIPR011249. Metalloenz_LuxS/M16.
IPR011237. Pept_M16_dom.
IPR011765. Pept_M16_N.
IPR007863. Peptidase_M16_C.
IPR013578. Peptidase_M16C_assoc.
[Graphical view]
PfamiPF08367. M16C_assoc. 1 hit.
PF00675. Peptidase_M16. 1 hit.
PF05193. Peptidase_M16_C. 1 hit.
[Graphical view]
SUPFAMiSSF63411. SSF63411. 4 hits.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8VY06-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLRSLTCSST ITSTSLFFRS FRQLPRSYLS PSSSTTVVGA SGRNIRRLST
60 70 80 90 100
LEAAGRRLFL RRGLKLLSAA SRGLNGQFSR LSIRAVATQS APSSYPGQDE
110 120 130 140 150
AEKLGFEKVS EEFISECKSK AVLFKHKKTG CEVMSVSNDD ENKVFGIVFR
160 170 180 190 200
TPPKDSTGIP HILEHSVLCG SRKYPMKEPF VELLKGSLHT FLNAFTYPDR
210 220 230 240 250
TCYPVASTNK KDFYNLVDVY LDAVFFPKCV DDVHTFQQEG WHYELNDPSE
260 270 280 290 300
DISYKGVVFN EMKGVYSQPD NILGRVTQQA LCPENTYGVD SGGDPKDIPK
310 320 330 340 350
LTFEKFKEFH RQYYHPSNAR IWFYGDDDPV HRLRVLSEYL DMFDASPARD
360 370 380 390 400
SSKVEPQKLF SRPRRIVEKY PAGEDGDLKK KHMVCLNWLL SDKPLDLQTQ
410 420 430 440 450
LALGFLDHLM LGTPASPLRK ILLESGLGEA LVNSGMEDEL LQPQFSIGLK
460 470 480 490 500
GVSDDNVQKV EELVMNTLRK LADEGFDTDA VEASMNTIEF SLRENNTGSS
510 520 530 540 550
PRGLSLMLQS IAKWIYDMDP FEPLKYEEPL KSLKARIAEK GSKSVFSPLI
560 570 580 590 600
EEYILNNPHC VTIEMQPDPE KASLEEAEEK SILEKVKASM TEEDLTELAR
610 620 630 640 650
ATEELRLKQE TPDPPDALKC VPSLNLSDIP KEPIYVPTEV GDINGVKVLR
660 670 680 690 700
NDLFTNNILY TEVVFDMGSV KHELLQLIPL FCQSLLEMGT QDLTFVQLNQ
710 720 730 740 750
LIGRKTGGIS VYPLTSSVYG RDDPCSKIIV RGKSMVGRAE DLFNLMNCVL
760 770 780 790 800
QEVRFTDQQR FKQFVSQSRA RMENRLRGSG QGIAAARMDA MLNVAGWMSE
810 820 830 840 850
QMGGLSYLEF LHTLEQKVDQ DWEGISSSLE EIRRSFLSRN GCIVNMTADG
860 870 880 890 900
KSLTNTEKYV GKFLDLLPEN PSGELVTWDA RLPLRNEAIV IPTQVNYVGK
910 920 930 940 950
AGNIYSSGYK LDGSSYVISK HISNTWLWDR VRVSGGAYGG SCDFDSHSGV
960 970 980 990 1000
FSFLSYRDPN LLKTLDIYDG TGDFLRGLDV DEDTLTKAII GTIGDVDSYQ
1010 1020 1030 1040 1050
LPDAKGYTSL LRHLLNVTDE ERQIRREEIL STSLKDFKEF AEAIDSVSDK
1060 1070 1080
GVAVAVASQE DIDAANRERS NFFEVKKAAL
Length:1,080
Mass (Da):121,131
Last modified:March 1, 2002 - v1
Checksum:i23425D0E7376E39E
GO

Sequence cautioni

The sequence AAG13049.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC011807 Genomic DNA. Translation: AAG13049.1. Sequence problems.
CP002684 Genomic DNA. Translation: AEE32451.1.
CP002684 Genomic DNA. Translation: AEE32452.1.
CP002684 Genomic DNA. Translation: AEE32453.1.
AY074305 mRNA. Translation: AAL67002.1.
BT004376 mRNA. Translation: AAO42370.1.
PIRiA96533.
RefSeqiNP_175386.2. NM_103851.3.
NP_850961.1. NM_180630.1.
NP_850962.1. NM_180631.1.
UniGeneiAt.27723.

Genome annotation databases

EnsemblPlantsiAT1G49630.1; AT1G49630.1; AT1G49630.
AT1G49630.2; AT1G49630.2; AT1G49630.
AT1G49630.3; AT1G49630.3; AT1G49630.
GeneIDi841387.
KEGGiath:AT1G49630.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC011807 Genomic DNA. Translation: AAG13049.1. Sequence problems.
CP002684 Genomic DNA. Translation: AEE32451.1.
CP002684 Genomic DNA. Translation: AEE32452.1.
CP002684 Genomic DNA. Translation: AEE32453.1.
AY074305 mRNA. Translation: AAL67002.1.
BT004376 mRNA. Translation: AAO42370.1.
PIRiA96533.
RefSeqiNP_175386.2. NM_103851.3.
NP_850961.1. NM_180630.1.
NP_850962.1. NM_180631.1.
UniGeneiAt.27723.

3D structure databases

ProteinModelPortaliQ8VY06.
SMRiQ8VY06. Positions 99-1077.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3702.AT1G49630.1-P.

Protein family/group databases

MEROPSiM16.018.

Proteomic databases

PaxDbiQ8VY06.
PRIDEiQ8VY06.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT1G49630.1; AT1G49630.1; AT1G49630.
AT1G49630.2; AT1G49630.2; AT1G49630.
AT1G49630.3; AT1G49630.3; AT1G49630.
GeneIDi841387.
KEGGiath:AT1G49630.

Organism-specific databases

GeneFarmi2580. 225.
TAIRiAT1G49630.

Phylogenomic databases

eggNOGiCOG1026.
HOGENOMiHOG000008829.
InParanoidiQ8VY06.
KOiK06972.
OMAiFTNDILY.
PhylomeDBiQ8VY06.

Enzyme and pathway databases

BioCyciARA:GQT-933-MONOMER.
ARA:GQT-934-MONOMER.
ARA:GQT-935-MONOMER.

Miscellaneous databases

PROiQ8VY06.

Gene expression databases

GenevestigatoriQ8VY06.

Family and domain databases

Gene3Di3.30.830.10. 1 hit.
InterProiIPR011249. Metalloenz_LuxS/M16.
IPR011237. Pept_M16_dom.
IPR011765. Pept_M16_N.
IPR007863. Peptidase_M16_C.
IPR013578. Peptidase_M16C_assoc.
[Graphical view]
PfamiPF08367. M16C_assoc. 1 hit.
PF00675. Peptidase_M16. 1 hit.
PF05193. Peptidase_M16_C. 1 hit.
[Graphical view]
SUPFAMiSSF63411. SSF63411. 4 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
    Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K.
    , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
    Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  2. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  3. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  4. "Isolation and identification of a novel mitochondrial metalloprotease (PreP) that degrades targeting presequences in plants."
    Staahl A., Moberg P., Ytterberg J., Panfilov O., Brockenhuus Von Lowenhielm H., Nilsson F., Glaser E.
    J. Biol. Chem. 277:41931-41939(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION.
  5. "Catalysis, subcellular localization, expression and evolution of the targeting peptides degrading protease, AtPreP2."
    Bhushan S., Staahl A., Nilsson S., Lefebvre B., Seki M., Roth C., McWilliam D., Wright S.J., Liberles D.A., Shinozaki K., Bruce B.D., Boutry M., Glaser E.
    Plant Cell Physiol. 46:985-996(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION, IDENTIFICATION BY MASS SPECTROMETRY, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
  6. "Two novel targeting peptide degrading proteases, PrePs, in mitochondria and chloroplasts, so similar and still different."
    Staahl A., Nilsson S., Lundberg P., Bhushan S., Biverstaahl H., Moberg P., Morisset M., Vener A., Maeler L., Langel U., Glaser E.
    J. Mol. Biol. 349:847-860(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: CLEAVAGE SPECIFICITY.

Entry informationi

Entry nameiPREP2_ARATH
AccessioniPrimary (citable) accession number: Q8VY06
Secondary accession number(s): Q9FX91
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2006
Last sequence update: March 1, 2002
Last modified: April 29, 2015
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.