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Reviewed, UniProtKB/Swiss-Prot Q5V9F0 (AMPL_DICDI)

Last modified November 3, 2009. Version 32. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Cytosol aminopeptidase
    EC=3.4.11.1
Alternative name(s):
    Leucine aminopeptidase
    Leucyl aminopeptidase
      Short name=LAP
    Proline aminopeptidase
    EC=3.4.11.5
    Prolyl aminopeptidase
Gene names
Name: lap
ORF Names: DDB_G0279793
OrganismDictyostelium discoideum (Slime mold) [Complete proteome]
Taxonomic identifier44689 [NCBI]
Taxonomic lineageEukaryotaAmoebozoaMycetozoaDictyosteliidaDictyostelium

Protein attributes

Sequence length520 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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 By similarity.

Subunit structure

Homohexamer By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the peptidase M17 family.

Ontologies

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

Inferred from electronic annotation. Source: InterPro

   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

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 520520Cytosol aminopeptidase
PRO_0000328614

Sites

Active site2981 By similarity
Active site3721 By similarity
Metal binding2861Zinc 2 By similarity
Metal binding2911Zinc 1 By similarity
Metal binding2911Zinc 2 By similarity
Metal binding3091Zinc 2 By similarity
Metal binding3681Zinc 1 By similarity
Metal binding3701Zinc 1 By similarity
Metal binding3701Zinc 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5V9F0-1 [UniParc].

Last modified December 7, 2004. Version 1.
Checksum: EE9ECBB8B54C0E85

FASTA52056,410
        10         20         30         40         50         60 
MLKNIINKKN LFINNQQNIF QIIKRNKMTD STVDNKGYIV GIYENEEFTP LGQQLNEKTN 

        70         80         90        100        110        120 
GHLLKSIKLS DTKGKVGDNL VLYNVTPEVS RVAIVGLGKK ENNNSTTYEK NENTRKAIGS 

       130        140        150        160        170        180 
GVKALKSKNA THLTIDSNIG DAKQTAEGAF LSNFKFDFKT GTSGKTANST NESIQVQLSP 

       190        200        210        220        230        240 
SPSSEECFKE GKILAESQNF ARVLMETPAN LLTPTNFVQH VSSQMKELID SGKVEMIVRE 

       250        260        270        280        290        300 
EQWVKDQKMG MFWGVAKGSD EPLKFLELHY RGASADGKDS IVYVGKGITF DSGGISIKPS 

       310        320        330        340        350        360 
ANMGLMKGDM GGAATAVSAM FGVASLGLKV NLITITPLCE NMPSGKATKP GDILTAANGK 

       370        380        390        400        410        420 
TVEVDNTDAE GRLILGDALH YACSFKPTHI IDIATLTGAI DVALGQHYAG CFTTTDSLWD 

       430        440        450        460        470        480 
QLNECGNISG ERLWRMPLIP EYRKQMETSK VADLINSAGR SGGACCAAGF LKEFITADQS 

       490        500        510        520 
WSHLDIAGVM SSSEDGPYIR KGMTGKPTRT LIEFAKKNQQ 

« Hide

References

« Hide 'large scale' references
[1]Huang J., Mullapudi N., Lancto C., Scott M., Abrahamsen M., Kissinger J.C.
Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The genome of the social amoeba Dictyostelium discoideum."
Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N. expand/collapse author list , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.
Nature 435:43-57(2005) [PubMed: 15875012] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AX4.

Cross-references

Sequence databases

AY581145 Genomic DNA. Translation: AAT92029.1.
AAFI02000032 Genomic DNA. Translation: EAL67576.1.
RefSeqXP_641537.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ5V9F0.

Protein family/group databases

MEROPSM17.001.

Genome annotation databases

GeneID3392643.
GenomeReviewsGene locus lap in contig CM000152_GR.
KEGGddi:DDB_0231024.

Organism-specific databases

dictyBaseDDB_G0279793. lap.

Phylogenomic databases

OMAPPLLLEC.

Enzyme and pathway databases

BRENDA3.4.11.1. 424.
3.4.11.5. 424.

Family and domain databases

InterProIPR011356. Peptidase_M17.
IPR000819. Peptidase_M17_C.
IPR008283. Peptidase_M17_N.
[Graphical view]
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_DICDI
AccessionPrimary (citable) accession number: Q5V9F0
Secondary accession number(s): Q54WC1
Entry history
Integrated into UniProtKB/Swiss-Prot: April 8, 2008
Last sequence update: December 7, 2004
Last modified: November 3, 2009
This is version 32 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

Dictyostelium discoideum

Dictyostelium discoideum: entries, gene names and cross-references to dictyBase

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents