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Q10712 (AMPL1_SOLLC) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Leucine aminopeptidase 1, chloroplastic
EC=3.4.11.1
Alternative name(s):
DR57
Leucyl aminopeptidase 1
Short name=LAP 1
Proline aminopeptidase 1
EC=3.4.11.5
Prolyl aminopeptidase 1
Gene names
Name:LAPA1
Synonyms:LAP, LAP2
OrganismSolanum lycopersicum (Tomato) (Lycopersicon esculentum)
Taxonomic identifier4081 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › lamiids › Solanales › Solanaceae › Solanoideae › Solaneae › Solanum › Lycopersicon

Protein attributes

Sequence length571 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.

Subcellular location

Plastid › chloroplast.

Induction

By wounding.

Sequence similarities

Belongs to the peptidase M17 family.

Ontologies

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

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentchloroplast

Inferred from electronic annotation. Source: UniProtKB-SubCell

   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

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 5353Chloroplast Potential
Chain54 – 571518Leucine aminopeptidase 1, chloroplastic
PRO_0000026803

Regions

Compositional bias169 – 1746Poly-Ala

Sites

Active site3541 Potential
Active site4311 Potential
Metal binding3421Zinc 2 By similarity
Metal binding3471Zinc 1 By similarity
Metal binding3471Zinc 2 By similarity
Metal binding3671Zinc 2 By similarity
Metal binding4271Zinc 1 By similarity
Metal binding4291Zinc 1 By similarity
Metal binding4291Zinc 2 By similarity

Natural variations

Natural variant3581R → G. Ref.2

Experimental info

Sequence conflict2711P → N in AAA80498. Ref.2
Sequence conflict3151T → S Ref.3
Sequence conflict5151T → L in AAC49457. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q10712 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: C7A224837E73939D

FASTA57160,279
        10         20         30         40         50         60 
MATLRVSSLF ASSSSSLHSN PSVFTKYQSS PKWAFSFPVT PLCSKRSKRI VHCIAGDTLG 

        70         80         90        100        110        120 
LTRPNESDAP KISIGAKDTA VVQWQGDLLA IGATENDMAR DENSKFKNPL LQQLDSELNG 

       130        140        150        160        170        180 
LLSAASSEED FSGKSGQSVN LRFPGGRITL VGLGSSASSP TSYHSLGQAA AAAAKSSQAR 

       190        200        210        220        230        240 
NIAVALASTD GLSAESKINS ASAIATGVVL GSFEDNRFRS ESKKSTLESL DILGLGTGPE 

       250        260        270        280        290        300 
IERKIKYAEH VCAGVILGRE LVNAPANIVT PAVLAEEAKK IASTYSDVIS VNILDAEQCK 

       310        320        330        340        350        360 
ELKMGAYLAV AAAATENPPY FIHLCFKTPT KERKTKLALV GKGLTFDSGG YNLKVGARSR 

       370        380        390        400        410        420 
IELMKNDMGG AAAVLGAAKA LGEIRPSRVE VHFIVAACEN MISAEGMRPG DIVTASNGKT 

       430        440        450        460        470        480 
IEVNNTDAEG RLTLADALIY ACNQGVEKII DLATLTGAIM VALGPSVAGA FTPNDDLARE 

       490        500        510        520        530        540 
VVEAAEASGE KLWRMPMEES YWESMKSGVA DMINTGPGNG GAITGALFLK QFVDEKVQWL 

       550        560        570 
HLDVAGPVWS DEKKNATGYG VSTLVEWVLR N

« Hide

References

[1]"Localization and post-translational processing of the wound-induced leucine aminopeptidase proteins of tomato."
Gu Y.Q., Chao W.S., Walling L.L.
J. Biol. Chem. 271:25880-25887(1996) [PubMed: 8824220] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Peto 238R.
Tissue: Leaf.
[2]"Nature and regulation of pistil-expressed genes in tomato."
Milligan S.B., Gasser C.S.
Plant Mol. Biol. 28:691-711(1995) [PubMed: 7647301] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 49-571, VARIANT GLY-358.
Strain: cv. VF36.
Tissue: Pistil.
[3]"Leucine aminopeptidase: an inducible component of the defense response in Lycopersicon esculentum (tomato)."
Pautot V., Holzer F.M., Reisch B., Walling L.L.
Proc. Natl. Acad. Sci. U.S.A. 90:9906-9910(1993) [PubMed: 8234334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 103-571.
Strain: cv. Peto 238R.
Tissue: Leaf.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U50151 mRNA. Translation: AAC49456.1.
U50152 mRNA. Translation: AAC49457.1.
U20593 mRNA. Translation: AAA80498.1.
PIRS57811.
T07849.
T07850.
RefSeqNP_001233862.1. NM_001246933.1.
UniGeneLes.84.

3D structure databases

ProteinModelPortalQ10712.
ModBaseSearch...

Protein family/group databases

MEROPSM17.002.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID544017.

Family and domain databases

InterProIPR011356. Peptidase_M17.
IPR000819. Peptidase_M17_C.
IPR023042. Peptidase_M17_cytosol_amino.
IPR008283. Peptidase_M17_N.
[Graphical view]
PfamPF00883. Peptidase_M17. 1 hit.
PF02789. Peptidase_M17_N. 1 hit.
[Graphical view]
PRINTSPR00481. LAMNOPPTDASE.
PROSITEPS00631. CYTOSOL_AP. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAMPL1_SOLLC
AccessionPrimary (citable) accession number: Q10712
Secondary accession number(s): Q9S9A3
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: December 14, 2011
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

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