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Q42876 (AMPL2_SOLLC) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 74. 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 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
Name:LAPA2
OrganismSolanum lycopersicum (Tomato) (Lycopersicon esculentum)
Taxonomic identifier4081 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsasteridslamiidsSolanalesSolanaceaeSolanoideaeSolaneaeSolanumLycopersicon

Protein attributes

Sequence length569 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

Plastidchloroplast.

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 – 4848Chloroplast Potential
Chain49 – 569521Leucine aminopeptidase 2, chloroplastic
PRO_0000026804

Regions

Compositional bias167 – 1726Poly-Ala

Sites

Active site3511 Potential
Active site4281 Potential
Metal binding3391Zinc 2 By similarity
Metal binding3441Zinc 1 By similarity
Metal binding3441Zinc 2 By similarity
Metal binding3641Zinc 2 By similarity
Metal binding4241Zinc 1 By similarity
Metal binding4261Zinc 1 By similarity
Metal binding4261Zinc 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q42876 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: E8DADAC26A3DC47B

FASTA56959,549
        10         20         30         40         50         60 
MNGVLCSSSS SFHSYPSIFT KFQSSPIWSF SISVTPLCSR RAKRMAHSIA RDTLGLTHTN 

        70         80         90        100        110        120 
QSDAPKISFA AKEIDLVEWK GDILTVGATE KDLARDGNSK FQNPLLQKLD SKLSGLLSEA 

       130        140        150        160        170        180 
SSEEDFSGKA GQSTILRLPG LGSKRIALVG LGSPTSSTAA YRCLGEAAAA AAKSAQASNI 

       190        200        210        220        230        240 
AIALASTDGL SAELKLSSAS AITTGAVLGT FEDNRFKSES KKPTLKSLDI LGLGTGPEIE 

       250        260        270        280        290        300 
KKIKYAADVC AGVILGRELV NAPANVLTPA VLAEEAKKIA STYSDVFSAN ILDVEQCKEL 

       310        320        330        340        350        360 
KMGSYLRVAA ASANPAHFIH LCYKPSSGEI KKKIALVGKG LTFDSGGYNI KTGPGCSIEL 

       370        380        390        400        410        420 
MKFDMGGAAA VLGAAKALGQ IKPAGVEVHF IVAACENMIS GTGMRPGDII TASNGKTIEV 

       430        440        450        460        470        480 
NNTDAEGRLT LSVGISCNQG VEKIVDLATL TGACVVALGP SIAGIFTPSD DLAKEVVAAS 

       490        500        510        520        530        540 
EVSGEKLWRL PMEDSYWDSM KSGVADMVNT GGRPGGAITA ALFLKQFVNE KVQWMHIDLA 

       550        560 
GPVWSDKKKN ATGFGVSTLV EWVLKNSTN 

« Hide

References

[1]"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].
Strain: cv. VF36.
Tissue: Pistil.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U20594 mRNA. Translation: AAA80499.1.
PIRS57812.
RefSeqNP_001233884.1. NM_001246955.1.
UniGeneLes.307.

3D structure databases

ProteinModelPortalQ42876.
ModBaseSearch...

Protein family/group databases

MEROPSM17.002.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID544277.

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 nameAMPL2_SOLLC
AccessionPrimary (citable) accession number: Q42876
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: December 14, 2011
This is version 74 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