Reviewed, UniProtKB/Swiss-Prot Q8VY06 (PREP2_ARATH)

Names and origin

Protein names

Recommended name:
    Presequence protease 2, chloroplastic/mitochondrial
      Short name=PreP 2
      Short name=AtPreP2
    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

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	1080 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.3
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	Plastid › chloroplast stroma. Mitochondrion matrix.
Tissue specificity	Expressed in leaves, flowers and roots, but not detected in siliques and shoots. Ref.4
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.

Ontologies

Keywords
Cellular component	Chloroplast Mitochondrion Plastid
Domain	Transit peptide
Ligand	Magnesium Metal-binding Zinc
Molecular function	Hydrolase Metalloprotease Protease
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	protein maturation by peptide bond cleavage Ref.4 Inferred from direct assay. Source: TAIR proteolysis Inferred from electronic annotation. Source: InterPro
Cellular component	chloroplast stroma Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW metalloendopeptidase activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 84	84	Chloroplast and mitochondrion Potential
	Chain	85 – 1080	996	Presequence protease 2, chloroplastic/mitochondrial		PRO_0000249939
Sites
	Active site	164	1	Proton acceptor By similarity
	Metal binding	161	1	Zinc By similarity
	Metal binding	165	1	Zinc By similarity
	Metal binding	261	1	Zinc By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8VY06-1 [UniParc]. Last modified March 1, 2002. Version 1. Checksum: 23425D0E7376E39E	FASTA	1,080	121,131
	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

References

	« Hide 'large scale' referencesShow '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. , 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: 11130712] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[2]	"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: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[3]	"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: 12138166] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION.
[4]	"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: 15827031] [Abstract] Cited for: CHARACTERIZATION, IDENTIFICATION BY MASS SPECTROMETRY, TISSUE SPECIFICITY, SUBCELLULAR LOCALIZATION.
[5]	"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: 15893767] [Abstract] Cited for: CLEAVAGE SPECIFICITY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AC011807 Genomic DNA. Translation: AAG13049.1. Sequence problems. AY074305 mRNA. Translation: AAL67002.1. BT004376 mRNA. Translation: AAO42370.1.
IPI	IPI00544499.
PIR	A96533.
RefSeq	NP_175386.2. NP_850961.1. NP_850962.1.
UniGene	At.27723
3D structure databases
SMR	Q8VY06. Positions 99-1077.
ModBase	Search...
Protein family/group databases
MEROPS	M16.018.
Proteomic databases
PRIDE	Q8VY06.
ProMEX	Q8VY06.
Genome annotation databases
GeneID	841387.
GenomeReviews	Gene locus AT1G49630 in contig CT485782_GR.
KEGG	ath:AT1G49630.
NMPDR	fig|3702.1.peg.4435.
Organism-specific databases
GeneFarm	2580. 225.
TAIR	At1g49630.
Phylogenomic databases
OMA	Q8VY06. WLYDGDP.
Gene expression databases
ArrayExpress	Q8VY06.
GermOnline	AT1G49630. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR011237. Pept_M16_core. IPR011765. Pept_M16_N. IPR001431. Pept_M16_Zn_BS. IPR007863. Peptidase_M16_C. IPR013578. Peptidase_M16C_assoc. [Graphical view]
Gene3D	G3DSA:3.30.830.10. Pept_M16_core. 1 hit.
Pfam	PF08367. M16C_assoc. 1 hit. PF00675. Peptidase_M16. 1 hit. PF05193. Peptidase_M16_C. 2 hits. [Graphical view]
PROSITE	PS00143. INSULINASE. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PREP2_ARATH

Accession

Primary (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:	June 16, 2009
This is version 41 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)