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Q8VY06 (PREP2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 83. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Presequence protease 2, chloroplastic/mitochondrial

Short name=AtPreP2
Short name=PreP 2
EC=3.4.24.-
Alternative name(s):
Zinc metalloprotease 2
Short name=AtZnMP2
Gene names
Name:PREP2
Synonyms:ZNMP2
Ordered Locus Names:At1g49630
ORF Names:F14J22.13
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length1080 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.4

Cofactor

Binds 1 zinc ion per subunit.

Binds 2 Magnesium ions per subunit By similarity.

Enzyme regulation

Completely inhibited by the metal chelator orthophenanthroline.

Subunit structure

Homodimer By similarity.

Subcellular location

Plastidchloroplast stroma. Mitochondrion matrix Ref.5.

Tissue specificity

Expressed in leaves, flowers and roots, but not detected in siliques and shoots. Ref.5

Sequence similarities

Belongs to the peptidase M16 family. PreP subfamily.

Sequence caution

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 8484Chloroplast and mitochondrion Potential
Chain85 – 1080996Presequence protease 2, chloroplastic/mitochondrial
PRO_0000249939

Sites

Active site1641Proton acceptor By similarity
Metal binding1611Zinc By similarity
Metal binding1651Zinc By similarity
Metal binding2611Zinc By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8VY06 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: 23425D0E7376E39E

FASTA1,080121,131
        10         20         30         40         50         60 
MLRSLTCSST ITSTSLFFRS FRQLPRSYLS PSSSTTVVGA SGRNIRRLST LEAAGRRLFL 

        70         80         90        100        110        120 
RRGLKLLSAA SRGLNGQFSR LSIRAVATQS APSSYPGQDE AEKLGFEKVS EEFISECKSK 

       130        140        150        160        170        180 
AVLFKHKKTG CEVMSVSNDD ENKVFGIVFR TPPKDSTGIP HILEHSVLCG SRKYPMKEPF 

       190        200        210        220        230        240 
VELLKGSLHT FLNAFTYPDR TCYPVASTNK KDFYNLVDVY LDAVFFPKCV DDVHTFQQEG 

       250        260        270        280        290        300 
WHYELNDPSE DISYKGVVFN EMKGVYSQPD NILGRVTQQA LCPENTYGVD SGGDPKDIPK 

       310        320        330        340        350        360 
LTFEKFKEFH RQYYHPSNAR IWFYGDDDPV HRLRVLSEYL DMFDASPARD SSKVEPQKLF 

       370        380        390        400        410        420 
SRPRRIVEKY PAGEDGDLKK KHMVCLNWLL SDKPLDLQTQ LALGFLDHLM LGTPASPLRK 

       430        440        450        460        470        480 
ILLESGLGEA LVNSGMEDEL LQPQFSIGLK GVSDDNVQKV EELVMNTLRK LADEGFDTDA 

       490        500        510        520        530        540 
VEASMNTIEF SLRENNTGSS PRGLSLMLQS IAKWIYDMDP FEPLKYEEPL KSLKARIAEK 

       550        560        570        580        590        600 
GSKSVFSPLI EEYILNNPHC VTIEMQPDPE KASLEEAEEK SILEKVKASM TEEDLTELAR 

       610        620        630        640        650        660 
ATEELRLKQE TPDPPDALKC VPSLNLSDIP KEPIYVPTEV GDINGVKVLR NDLFTNNILY 

       670        680        690        700        710        720 
TEVVFDMGSV KHELLQLIPL FCQSLLEMGT QDLTFVQLNQ LIGRKTGGIS VYPLTSSVYG 

       730        740        750        760        770        780 
RDDPCSKIIV RGKSMVGRAE DLFNLMNCVL QEVRFTDQQR FKQFVSQSRA RMENRLRGSG 

       790        800        810        820        830        840 
QGIAAARMDA MLNVAGWMSE QMGGLSYLEF LHTLEQKVDQ DWEGISSSLE EIRRSFLSRN 

       850        860        870        880        890        900 
GCIVNMTADG KSLTNTEKYV GKFLDLLPEN PSGELVTWDA RLPLRNEAIV IPTQVNYVGK 

       910        920        930        940        950        960 
AGNIYSSGYK LDGSSYVISK HISNTWLWDR VRVSGGAYGG SCDFDSHSGV FSFLSYRDPN 

       970        980        990       1000       1010       1020 
LLKTLDIYDG TGDFLRGLDV DEDTLTKAII GTIGDVDSYQ LPDAKGYTSL LRHLLNVTDE 

      1030       1040       1050       1060       1070       1080 
ERQIRREEIL STSLKDFKEF AEAIDSVSDK GVAVAVASQE DIDAANRERS NFFEVKKAAL 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRA96533.
RefSeqNP_175386.2. NM_103851.3.
NP_850961.1. NM_180630.1.
NP_850962.1. NM_180631.1.
UniGeneAt.27723.

3D structure databases

ProteinModelPortalQ8VY06.
SMRQ8VY06. Positions 99-1077.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING3702.AT1G49630.1-P.

Protein family/group databases

MEROPSM16.018.

Proteomic databases

PaxDbQ8VY06.
PRIDEQ8VY06.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G49630.1; AT1G49630.1; AT1G49630.
AT1G49630.2; AT1G49630.2; AT1G49630.
AT1G49630.3; AT1G49630.3; AT1G49630.
GeneID841387.
KEGGath:AT1G49630.

Organism-specific databases

GeneFarm2580. 225.
TAIRAT1G49630.

Phylogenomic databases

eggNOGCOG1026.
HOGENOMHOG000008829.
InParanoidQ8VY06.
KOK06972.
OMAKGSKAVF.
PhylomeDBQ8VY06.

Enzyme and pathway databases

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

Gene expression databases

GenevestigatorQ8VY06.

Family and domain databases

Gene3D3.30.830.10. 1 hit.
InterProIPR011249. Metalloenz_LuxS/M16.
IPR011237. Pept_M16_dom.
IPR011765. Pept_M16_N.
IPR007863. Peptidase_M16_C.
IPR013578. Peptidase_M16C_assoc.
[Graphical view]
PfamPF08367. M16C_assoc. 1 hit.
PF00675. Peptidase_M16. 1 hit.
PF05193. Peptidase_M16_C. 1 hit.
[Graphical view]
SUPFAMSSF63411. SSF63411. 4 hits.
ProtoNetSearch...

Entry information

Entry namePREP2_ARATH
AccessionPrimary (citable) accession number: Q8VY06
Secondary accession number(s): Q9FX91
Entry history
Integrated into UniProtKB/Swiss-Prot: September 19, 2006
Last sequence update: March 1, 2002
Last modified: May 14, 2014
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names