Reviewed, UniProtKB/Swiss-Prot P30184 (AMPL1_ARATH)

Names and origin

Protein names

Recommended name:
    Leucine aminopeptidase 1
    EC=3.4.11.1
Alternative name(s):
    Leucyl aminopeptidase 1
      Short name=LAP 1
    Proline aminopeptidase 1
    EC=3.4.11.5
    Prolyl aminopeptidase 1

Gene names

Name:	PM25
Ordered Locus Names:	At2g24200
ORF Names:	F27D4.11

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	520 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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.
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	Cytoplasm.
Sequence similarities	Belongs to the peptidase M17 family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Metal-binding Zinc
Molecular function	Aminopeptidase Hydrolase Protease
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	proteolysis Inferred from electronic annotation. Source: InterPro response to cadmium ion Inferred from expression pattern. Source: TAIR
Cellular component	vacuole Inferred from direct assay. Source: TAIR
Molecular function	aminopeptidase 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...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 520	520	Leucine aminopeptidase 1		PRO_0000165823
Sites
	Active site	300	1	Potential
	Active site	377	1	Potential
	Metal binding	288	1	Zinc 2 By similarity
	Metal binding	293	1	Zinc 1 By similarity
	Metal binding	293	1	Zinc 2 By similarity
	Metal binding	313	1	Zinc 2 By similarity
	Metal binding	373	1	Zinc 1 By similarity
	Metal binding	375	1	Zinc 1 By similarity
	Metal binding	375	1	Zinc 2 By similarity

Sequences

	Sequence		Length	Mass (Da)
	P30184-1 [UniParc]. Last modified April 1, 1993. Version 1. Checksum: D3FA9CCCD312AA92	FASTA	520	54,509
	10 20 30 40 50 60 MAHTLGLTQP NSTEPHKISF TAKEIDVIEW KGDILVVGVT EKDLAKDGNS KFENPILSKV 70 80 90 100 110 120 DAHLSGLLAQ VSSEEDFTGK PGQSTVLRLP GLGSKRIALI GLGQSVSSPV AFHSLGEAVA 130 140 150 160 170 180 TVSKASQSTS AAIVLASSVS DESKLSSVSA LASGIVLGLF EDGRYKSESK KPSLKAVDII 190 200 210 220 230 240 GFGTGAEVEK KLKYAEDVSY GVIFGRELIN SPANVLTPAV LAEEAAKVAS TYSDVFTANI 250 260 270 280 290 300 LNEEQCKELK MGSYLAVAAA SANPPHFIHL VYKPPNGSVK TKLALVGKGL TFDSGGYNIK 310 320 330 340 350 360 TGPGCSIELM KFDMGGSAAV LGAAKAIGEI KPPGVEVHFI VAACENMISG TGMRPGDVIT 370 380 390 400 410 420 ASNGKTIEVN NTDAEGRLTL ADALVYACNQ GVDKIVDLAT LTGACVIALG TSMAGIYTPS 430 440 450 460 470 480 DELAKEVIAA SERSGEKLWR MPLEESYWEM MKSGVADMVN TGGRAGGSIT AALFLKQFVS 490 500 510 520 EKVQWMHIDM AGPVWNEKKK SGTGFGVATL VEWVQKNSSS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Leucine aminopeptidase from Arabidopsis thaliana. Molecular evidence for a phylogenetically conserved enzyme of protein turnover in higher plants." Bartling D., Weiler E.W. Eur. J. Biochem. 205:425-431(1992) [PubMed: 1555602] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Landsberg erecta. Tissue: Leaf.
[2]	"Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana." Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., Cronin L.A. , Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C. Nature 402:761-768(1999) [PubMed: 10617197] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 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: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X63444 mRNA. Translation: CAA45040.1. AC005967 Genomic DNA. Translation: AAD03381.1. AY062105 mRNA. Translation: AAL32980.1. BT006345 mRNA. Translation: AAP21153.1.
IPI	IPI00538374.
PIR	S22399.
RefSeq	NP_001118375.1. NP_179997.1.
UniGene	At.24655
3D structure databases
HSSP	HSSP built from PDB template 1GYT based on UniProtKB P11648.
ModBase	Search...
Protein-protein interaction databases
STRING	P30184.
Protein family/group databases
MEROPS	M17.A03.
Proteomic databases
PRIDE	P30184.
ProMEX	P30184.
Genome annotation databases
GeneID	816954.
GenomeReviews	Gene locus AT2G24200 in contig CT485783_GR.
KEGG	ath:AT2G24200.
NMPDR	fig|3702.1.peg.9442.
Organism-specific databases
GeneFarm	1931. 195.
TAIR	At2g24200.
Phylogenomic databases
OMA	AMALQKA.
Enzyme and pathway databases
BRENDA	3.4.11.1. 302. 3.4.11.5. 302.
Gene expression databases
ArrayExpress	P30184.
Genevestigator	P30184.
GermOnline	AT2G24200. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR011356. Peptidase_M17. IPR000819. Peptidase_M17_C. IPR008283. Peptidase_M17_N. [Graphical view]
PANTHER	PTHR11963:SF3. Peptidase_M17. 1 hit.
Pfam	PF00883. Peptidase_M17. 1 hit. PF02789. Peptidase_M17_N. 1 hit. [Graphical view]
PRINTS	PR00481. LAMNOPPTDASE.
PROSITE	PS00631. CYTOSOL_AP. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

AMPL1_ARATH

Accession

Primary (citable) accession number: P30184

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	April 1, 1993
Last modified:	November 3, 2009
This is version 86 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)