P31427 (AMPL_SOLTU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Leucine aminopeptidase, chloroplastic
EC=3.4.11.1

Alternative name(s):
Leucyl aminopeptidase
Short name=LAP
Proline aminopeptidase
EC=3.4.11.5
Prolyl aminopeptidase

Gene names

Name:

LAP

Organism

Solanum tuberosum (Potato)

Taxonomic identifier

4113 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › lamiids › Solanales › Solanaceae › Solanoideae › Solaneae › Solanum

Protein attributes

Sequence length	573 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Presumably involved in the processing and regular turnover of intracellular proteins.
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 By similarity.
Tissue specificity	In tubers and floral buds of untreated plants. After abscisic acid (ABA) treatment or mechanical wounding is mostly accumulated in leaves, to a lesser extent in stems, but not in roots.
Induction	By abscisic acid (ABA), jasmonic acid (JA) and wounding.
Sequence similarities	Belongs to the peptidase M17 family.

Ontologies

Keywords
Biological process	Stress response
Cellular component	Chloroplast Plastid
Domain	Transit peptide
Ligand	Metal-binding Zinc
Molecular function	Aminopeptidase Hydrolase Protease
Gene Ontology (GO)
Biological process	proteolysis Inferred from electronic annotation. Source: UniProtKB-KW response to stress Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	chloroplast Inferred from electronic annotation. Source: UniProtKB-SubCell
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
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 53	53	Chloroplast Potential
	Chain	54 – 573	520	Leucine aminopeptidase, chloroplastic		PRO_0000026805
Regions
	Compositional bias	169 – 174	6	Poly-Ala
Sites
	Active site	354	1	Potential
	Active site	431	1	Potential
	Metal binding	342	1	Zinc 2 By similarity
	Metal binding	347	1	Zinc 1 By similarity
	Metal binding	347	1	Zinc 2 By similarity
	Metal binding	367	1	Zinc 2 By similarity
	Metal binding	427	1	Zinc 1 By similarity
	Metal binding	429	1	Zinc 1 By similarity
	Metal binding	429	1	Zinc 2 By similarity

Sequences

	Sequence		Length	Mass (Da)
	P31427 [UniParc]. Last modified October 1, 1996. Version 2. Checksum: 3152145A4A7FB291	FASTA	573	60,122
	10 20 30 40 50 60 MATLRVSSLL ASSPSSLHCN PSVFTKCQSS PRWAFSFSVT PLCSRRSKRI VHCIAGDTLG 70 80 90 100 110 120 LTRPNESDAP KISIGAKDTD VVQWQGDLLA IGATENDLAR DDNSKFKNPL LQRLDSKLNG 130 140 150 160 170 180 LLSAASSEED FSGKSGQSIN LRLPGGRITL VGLGSSASSP TSYHSLGEAA AAAAKSAQAR 190 200 210 220 230 240 NIAVSLASTD GLSAESKINS ASAIATGVML GIFEDNRFRS ESKTPALESL DILGLGTGPE 250 260 270 280 290 300 IESKIKYAEH VCAGVILGRE LVNAPANIVT PGALAEEAKK IASTYSDVIT VNILDAEQCK 310 320 330 340 350 360 ELKMGAYLGV AAAATENPPY FIHLCFKTNS RERKTKIALV GKGLTFDSGG YNLKTGAGSK 370 380 390 400 410 420 IELMKNDMGG AAAVLGAAKA LGEIKPRGVE VHFIVAACEN MISGAGMRPG DIVTASNGKT 430 440 450 460 470 480 IEVNNTDAEG RLTLADALIY ACNQGVEKII DLATLTGAIV TALGPSVAGA FTPSDGLARE 490 500 510 520 530 540 VVVAAEASGE KLWRMPMEES YWESMKSGVA DMINTGPRDG GAITGALFLK QFVDEKVQWL 550 560 570 HLDIAGPVWS DEKKNATGYG VSTLVEWVLR NSL

References

[1]	"Functional analysis of a leucine aminopeptidase from Solanum tuberosum L." Herbers K., Prat S., Willmitzer L. Planta 194:230-240(1994) [PubMed: 7765119] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Desiree.
[2]	"General roles of abscisic and jasmonic acids in gene activation as a result of mechanical wounding." Hildmann T., Ebneth M., Pena-Cortes H., Sanchez-Serrano J.J., Willmitzer L., Prat S. Plant Cell 4:1157-1170(1992) [PubMed: 1392612] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 19-573. Strain: cv. Desiree. Tissue: Leaf.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X77015 mRNA. Translation: CAA54314.1. X67845 mRNA. Translation: CAA48038.1.
PIR	S41376.
3D structure databases
ProteinModelPortal	P31427.
ModBase	Search...
Protein family/group databases
MEROPS	M17.002.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR011356. Peptidase_M17. IPR000819. Peptidase_M17_C. IPR023042. Peptidase_M17_cytosol_amino. IPR008283. Peptidase_M17_N. [Graphical view]
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

AMPL_SOLTU

Accession

Primary (citable) accession number: P31427

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	October 1, 1996
Last modified:	November 16, 2011
This is version 77 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program