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Reviewed, UniProtKB/Swiss-Prot Q8RX72 (AMPL2_ARATH)

Last modified February 9, 2010. Version 52. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Leucine aminopeptidase 2, chloroplastic
    EC=3.4.11.1
Alternative name(s):
    Leucyl aminopeptidase 2
      Short name=LAP 2
    Proline aminopeptidase 2
    EC=3.4.11.5
    Prolyl aminopeptidase 2
Gene names
Ordered Locus Names: At4g30910
ORF Names: F6I18.180
OrganismArabidopsis thaliana (Mouse-ear cress) [Complete proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Arabidopsis

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Protein attributes

Sequence length581 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

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General annotation (Comments)

Function

Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides By similarity.

Catalytic activity

Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low.

Release of N-terminal proline from a peptide.

Cofactor

Binds 2 zinc ions per subunit By similarity.

Subunit structure

Homohexamer Probable.

Subcellular location

Plastid › chloroplast Potential.

Sequence similarities

Belongs to the peptidase M17 family.

Sequence caution

The sequence CAA18202.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAB79809.1 differs from that shown. Reason: Erroneous gene model prediction.

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Ontologies

Keywords
   Cellular componentChloroplast
Plastid
   DomainTransit peptide
   LigandMetal-binding
Zinc
   Molecular functionAminopeptidase
Hydrolase
Protease
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processproteolysis

Inferred from electronic annotation. Source: InterPro

   Cellular componentchloroplast

Inferred from direct assay. Source: TAIR

   Molecular functionaminopeptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

manganese ion binding

Inferred from electronic annotation. Source: InterPro

metalloexopeptidase activity

Inferred from electronic annotation. Source: InterPro

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 5050Chloroplast Potential
Chain51 – 581531Leucine aminopeptidase 2, chloroplastic
PRO_0000045811

Regions

Compositional bias178 – 1858Poly-Ala

Sites

Active site3621 Potential
Active site4391 Potential
Metal binding3501Zinc 2 By similarity
Metal binding3551Zinc 1 By similarity
Metal binding3551Zinc 2 By similarity
Metal binding3751Zinc 2 By similarity
Metal binding4351Zinc 1 By similarity
Metal binding4371Zinc 1 By similarity
Metal binding4371Zinc 2 By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q8RX72-1 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: C4B674CFF40F1DC0

FASTA58161,290
        10         20         30         40         50         60 
MAVTLVTSCA SSSRFHFRSF SSSPSSLSSC FVRFQLLSRL RVSFAITPLY CSSKATAHTI 

        70         80         90        100        110        120 
AHATLGLTQA NSVDHPKISF SGKEIDVTEW KGDILAVGVT EKDMAKDANS KFENPILKKL 

       130        140        150        160        170        180 
DAHLGGLLAD VSAEEDFSGK PGQSTVLRLP GLGSKRVGLI GLGKSASTPS AFQSLGEAVA 

       190        200        210        220        230        240 
AAAKASQASS VAVVLASSES FSDESKLSSA SDIASGTVLG LFEDSRYKSE SKKPSLKSVV 

       250        260        270        280        290        300 
FIGFGTGPEL ENKLKYAEHV SYGVIFTKEL VNSPANVLSP AVLAEEASNL ASMYSNVMTA 

       310        320        330        340        350        360 
NILKEEQCKE LKMGSYLAVA AASANPPHFI HLIYKPSSGP VKTKLALVGK GLTFDSGGYN 

       370        380        390        400        410        420 
IKIGPELIIE LMKIDVGGSA AVLGAAKAIG EIKPPGVEVH FIVAACENMI SGTGMRPGDV 

       430        440        450        460        470        480 
ITASNGKTIE VNDTDSEGRL TLADALVYAC NQGVDKIVDI ATLTGEIIVA LGPSMAGMYT 

       490        500        510        520        530        540 
ASDELAKEVI AASQRSGEKL WRMPMEESYW EMMKSGVADM VNFGGRAGGS ITAALFLKRF 

       550        560        570        580 
VSENVEWLHI DMAGRVWNEK KKAATGFGVA TLVEWVQNNS S

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References

[1]"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. expand/collapse author list , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
Nature 402:769-777(1999) [PubMed: 10617198] [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. 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: 14593172] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
+Additional computationally mapped references.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AL022198 Genomic DNA. Translation: CAA18202.1. Sequence problems.
AL161577 Genomic DNA. Translation: CAB79809.1. Sequence problems.
AY090346 mRNA. Translation: AAL91252.1.
AY125537 mRNA. Translation: AAM78047.1.
IPIIPI00539733.
PIRH85361.
RefSeqNP_194820.1.
UniGeneAt.31791

3D structure databases

SMRQ8RX72. Positions 80-580.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ8RX72.

Protein family/group databases

MEROPSM17.A02.

Proteomic databases

PRIDEQ8RX72.

Genome annotation databases

GeneID829215.
GenomeReviewsGene locus AT4G30910 in contig CT486007_GR.
KEGGath:AT4G30910.
NMPDRfig|3702.1.peg.21081.

Organism-specific databases

GeneFarm2141. 195.
TAIRAt4g30910.

Phylogenomic databases

eggNOGKOG2597.
HOGENOMHBG742580.
InParanoidQ8RX72.
OMAHTIAHAT.
PhylomeDBQ8RX72.

Enzyme and pathway databases

BRENDA3.4.11.1. 302.
3.4.11.5. 302.

Gene expression databases

GenevestigatorQ8RX72.
GermOnlineAT4G30910. Arabidopsis thaliana.

Family and domain databases

InterProIPR011356. Peptidase_M17.
IPR000819. Peptidase_M17_C.
IPR008283. Peptidase_M17_N.
[Graphical view]
PANTHERPTHR11963:SF3. Peptidase_M17. 1 hit.
PfamPF00883. Peptidase_M17. 1 hit.
PF02789. Peptidase_M17_N. 1 hit.
[Graphical view]
PRINTSPR00481. LAMNOPPTDASE.
PROSITEPS00631. CYTOSOL_AP. False negative.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameAMPL2_ARATH
AccessionPrimary (citable) accession number: Q8RX72
Secondary accession number(s): O65558
Entry history
Integrated into UniProtKB/Swiss-Prot: January 24, 2006
Last sequence update: June 1, 2002
Last modified: February 9, 2010
This is version 52 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

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Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents