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Q5XGB9 (AMPL_XENTR) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 54. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cytosol aminopeptidase

EC=3.4.11.1
Alternative name(s):
Leucine aminopeptidase 3
Short name=LAP-3
Leucyl aminopeptidase
Proline aminopeptidase
EC=3.4.11.5
Prolyl aminopeptidase
Gene names
Name:lap3
OrganismXenopus tropicalis (Western clawed frog) (Silurana tropicalis)
Taxonomic identifier8364 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraMesobatrachiaPipoideaPipidaeXenopodinaeXenopusSilurana

Protein attributes

Sequence length520 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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 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. One zinc ion is tightly bound and essential for enzyme activity, while the second metal coordination site can be occupied by zinc, magnesium or manganese to give enzymes of different activities By similarity.

Subunit structure

Homohexamer By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the peptidase M17 family.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandMagnesium
Manganese
Metal-binding
Zinc
   Molecular functionAminopeptidase
Hydrolase
Protease
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processproteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

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

Chain1 – 520520Cytosol aminopeptidase
PRO_0000274147

Sites

Active site2921 By similarity
Active site3661 By similarity
Metal binding2801Zinc 2 By similarity
Metal binding2851Zinc 1 By similarity
Metal binding2851Zinc 2 By similarity
Metal binding3031Zinc 2 By similarity
Metal binding3621Zinc 1 By similarity
Metal binding3641Zinc 1 By similarity
Metal binding3641Zinc 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5XGB9 [UniParc].

Last modified November 23, 2004. Version 1.
Checksum: 33ADD5840F6E7837

FASTA52056,333
        10         20         30         40         50         60 
MLPFRTLLKW SVNRNCCRGF AVSQQNYNSV KKGLVLGVYE KEKEEESLTL TNAGDAVDNA 

        70         80         90        100        110        120 
VLGKLRDQLA RSGPSLKKGK SRIFYGLHED FPSIVVVGLG KKSAGVNQHE LWNEAKENIR 

       130        140        150        160        170        180 
AAVSVGCRQM QDMEIVQVEV DPCGDAQAAA EGAVLGLFEY NEMKKKKKKA VTTHLHGSSE 

       190        200        210        220        230        240 
ITAWEKGVLY AEGQNLARHL MEAPANYITP TKFAETFEQR LANMGSNVKV FTRSKQWIEE 

       250        260        270        280        290        300 
QQMGAFLSVA KGSEEPPVFL EIHYSGSSDA SQPPLVFVGK GVTFDSGGIS LKPSSGMDAM 

       310        320        330        340        350        360 
RGDMGGAATV CSAITTAAKL KLPINIISLA PLCENMPNGR ANKPGDVVKA KNGKTIQVDN 

       370        380        390        400        410        420 
TDAEGRLLLA DALCYAHSFN PRAIVNAATL TGAMDVALGS AAAGVFTNSS WLWTHLQEAS 

       430        440        450        460        470        480 
VVTGDRVWRM PLFEHYSKQV TESALADLNN IGKYSRSGGA CTAAAFLKEF VTAPHWAHLD 

       490        500        510        520 
IAGVMSNKDE VPYLRKGMSG RPTRTLIEFA ARLSEDKQTI 

« Hide

References

[1]NIH - Xenopus Gene Collection (XGC) project
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Embryo.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC084523 mRNA. Translation: AAH84523.1.
RefSeqNP_001011124.1. NM_001011124.1.
UniGeneStr.9934.

3D structure databases

HSSPHSSP built from PDB template 2EWB based on UniProtKB P00727.
ProteinModelPortalQ5XGB9.
SMRQ5XGB9. Positions 32-516.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ5XGB9.

Protein family/group databases

MEROPSM17.001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID496537.
KEGGxtr:496537.

Organism-specific databases

CTD51056.
XenbaseXB-GENE-1006711. lap3.

Phylogenomic databases

eggNOGveNOG10515.
GeneTreeENSGT00530000063255.
HOGENOMHBG742580.
HOVERGENHBG003320.
InParanoidQ5XGB9.
OMAKLFEASV.
OrthoDBEOG4P2Q21.

Gene expression databases

BgeeQ5XGB9.

Family and domain databases

InterProIPR011356. Peptidase_M17.
IPR000819. Peptidase_M17_C.
IPR023042. Peptidase_M17_cytosol_amino.
IPR008283. Peptidase_M17_N.
[Graphical view]
KOK11142.
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...

Entry information

Entry nameAMPL_XENTR
AccessionPrimary (citable) accession number: Q5XGB9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: November 23, 2004
Last modified: November 16, 2011
This is version 54 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families