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Reviewed, UniProtKB/Swiss-Prot Q944P7 (AMPL3_ARATH)

Last modified November 3, 2009. Version 53. 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 3, chloroplastic
    EC=3.4.11.1
Alternative name(s):
    Leucyl aminopeptidase 3
      Short name=LAP 3
    Proline aminopeptidase 3
    EC=3.4.11.5
    Prolyl aminopeptidase 3
Gene names
Ordered Locus Names: At4g30920
ORF Names: F6I18.170
OrganismArabidopsis thaliana (Mouse-ear cress) [Complete proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

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Protein attributes

Sequence length583 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 CAA18201.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAB79810.1 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

vacuole

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 – 7070Chloroplast Potential
Chain71 – 583513Leucine aminopeptidase 3, chloroplastic
PRO_0000045812

Regions

Compositional bias179 – 1868Poly-Ala

Sites

Active site3631 Potential
Active site4401 Potential
Metal binding3511Zinc 2 By similarity
Metal binding3561Zinc 1 By similarity
Metal binding3561Zinc 2 By similarity
Metal binding3761Zinc 2 By similarity
Metal binding4361Zinc 1 By similarity
Metal binding4381Zinc 1 By similarity
Metal binding4381Zinc 2 By similarity

Experimental info

Sequence conflict911W → G in AAL11627. Ref.2
Sequence conflict911W → G in AAO11568. Ref.2
Sequence conflict5451D → G in AAL11627. Ref.2
Sequence conflict5451D → G in AAO11568. Ref.2

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Sequences

Sequence LengthMass (Da)Tools
Q944P7-1 [UniParc].

Last modified January 24, 2006. Version 2.
Checksum: 1045CC6F326644AB

FASTA58361,307
        10         20         30         40         50         60 
MAVTLVTSFA SSSSRFHFRS FSSSPSSLSS CFVRFQFPSR LRLAFAVTPL YSSSRAMAHT 

        70         80         90        100        110        120 
ISHATLGLTQ ANSVDHPKIS FSGKEIDVTE WKGDILAVGV TEKDMAKDVN SKFENPILKK 

       130        140        150        160        170        180 
LDAHLGGLLA DVSSEEDFSG KPGQSTVLRL PGLGSKRVGL IGLGKSASTP SAFQSLGEAV 

       190        200        210        220        230        240 
AAAAKASQAS SVAVVLASSE SVSNESKLCS ASAIASGTVL GLFEDSRYKS ESKKPSLKSV 

       250        260        270        280        290        300 
DIIGFGSGPE LEKKLKYAEH VSYGVIFGKE LVNSPANVLT PAVLAEEALN LASMYSDVMT 

       310        320        330        340        350        360 
ANILNEEQCK ELKMGSYLAV AAASANPPHF IHLIYKPSSG PVKTKLALVG KGLTFDSGGY 

       370        380        390        400        410        420 
NIKTGPGCLI ELMKFDMGGS AAVLGAAKAI GQIKPPGVEV HFIVAACENM ISGTGMRPGD 

       430        440        450        460        470        480 
VLTASNGKTI EVNNTDAEGR LTLADALVYA CNQGVDKVVD LATLTGACII ALGTSMAGIY 

       490        500        510        520        530        540 
TPSDKLAKEV IAASERSGEK LWRMPMEESY WEMMKSGVAD MVNTGGRAGG SITAALFLKQ 

       550        560        570        580 
FVSEDVEWMH IDMAGPVWNE KKKAATGFGV ATLVEWVQNH SSS

« Hide

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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

AL022198 Genomic DNA. Translation: CAA18201.1. Sequence problems.
AL161577 Genomic DNA. Translation: CAB79810.1. Sequence problems.
AF424634 mRNA. Translation: AAL11627.1.
BT002652 mRNA. Translation: AAO11568.1.
IPIIPI00544667.
PIRA85362.
RefSeqNP_194821.1.
UniGeneAt.2156

3D structure databases

HSSPHSSP built from PDB template 1GYT based on UniProtKB P11648.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ944P7.

Protein family/group databases

MEROPSM17.A01.

Proteomic databases

PRIDEQ944P7.

Genome annotation databases

GeneID829216.
GenomeReviewsGene locus AT4G30920 in contig CT486007_GR.
KEGGath:AT4G30920.
NMPDRfig|3702.1.peg.21082.

Organism-specific databases

GeneFarm2142. 195.
TAIRAt4g30920.

Phylogenomic databases

OMAHTISHAT.

Enzyme and pathway databases

BRENDA3.4.11.1. 302.
3.4.11.5. 302.

Gene expression databases

GenevestigatorQ944P7.
GermOnlineAT4G30920. 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. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameAMPL3_ARATH
AccessionPrimary (citable) accession number: Q944P7
Secondary accession number(s): O65557
Entry history
Integrated into UniProtKB/Swiss-Prot: January 24, 2006
Last sequence update: January 24, 2006
Last modified: November 3, 2009
This is version 53 of the entry and version 2 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