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P00727 (AMPL_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 139. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·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
Peptidase S
Proline aminopeptidase
EC=3.4.11.5
Prolyl aminopeptidase
Gene names
Name:LAP3
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length519 AA.
Sequence statusComplete.
Protein existenceEvidence at protein 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. HAMAP-Rule MF_00181

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. HAMAP-Rule MF_00181

Release of N-terminal proline from a peptide. HAMAP-Rule MF_00181

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.

Enzyme regulation

Inhibited by bestatin. HAMAP-Rule MF_00181

Subunit structure

Homohexamer.

Subcellular location

Cytoplasm HAMAP-Rule MF_00181.

Sequence similarities

Belongs to the peptidase M17 family.

Sequence caution

The sequence AAB28170.1 differs from that shown. Reason: Erroneous initiation.

Alternative products

This entry describes 2 isoforms produced by alternative initiation. [Align] [Select]
Isoform 1 (identifier: P00727-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Note: No experimental confirmation available.
Isoform 2 (identifier: P00727-2)

The sequence of this isoform differs from the canonical sequence as follows:
     11-31: Missing.
Note: Initiator Met-1 is removed.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 519519Cytosol aminopeptidase HAMAP-Rule MF_00181
PRO_0000165824

Sites

Active site2941
Active site3681
Metal binding2821Zinc 2
Metal binding2871Zinc 1
Metal binding2871Zinc 2
Metal binding3051Zinc 2
Metal binding3641Zinc 1
Metal binding3661Zinc 1
Metal binding3661Zinc 2

Amino acid modifications

Modified residue331N-acetylthreonine HAMAP-Rule MF_00181
Modified residue451N6-succinyllysine By similarity
Modified residue611N6-succinyllysine By similarity
Modified residue1031N6-succinyllysine By similarity
Modified residue1801Phosphoserine By similarity
Modified residue2381Phosphoserine By similarity
Modified residue4551N6-acetyllysine; alternate By similarity
Modified residue4551N6-succinyllysine; alternate By similarity
Modified residue4761N6-succinyllysine By similarity
Modified residue4891N6-acetyllysine; alternate By similarity
Modified residue4891N6-succinyllysine; alternate By similarity

Natural variations

Alternative sequence11 – 3121Missing in isoform 2.
VSP_022634

Experimental info

Sequence conflict771P → S in AAB28170. Ref.2
Sequence conflict414 – 4152LW → M AA sequence Ref.4
Sequence conflict414 – 4152LW → M AA sequence Ref.5
Sequence conflict506 – 5138Missing AA sequence Ref.4
Sequence conflict506 – 5138Missing AA sequence Ref.5

Secondary structure

..................................................................................... 519
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: CDA6AED4D937F624

FASTA51956,289
        10         20         30         40         50         60 
MFLLPLPAAA RVAVRHLSVK RLWAPGPAAA DMTKGLVLGI YSKEKEEDEP QFTSAGENFN 

        70         80         90        100        110        120 
KLVSGKLREI LNISGPPLKA GKTRTFYGLH EDFPSVVVVG LGKKTAGIDE QENWHEGKEN 

       130        140        150        160        170        180 
IRAAVAAGCR QIQDLEIPSV EVDPCGDAQA AAEGAVLGLY EYDDLKQKRK VVVSAKLHGS 

       190        200        210        220        230        240 
EDQEAWQRGV LFASGQNLAR RLMETPANEM TPTKFAEIVE ENLKSASIKT DVFIRPKSWI 

       250        260        270        280        290        300 
EEQEMGSFLS VAKGSEEPPV FLEIHYKGSP NASEPPLVFV GKGITFDSGG ISIKAAANMD 

       310        320        330        340        350        360 
LMRADMGGAA TICSAIVSAA KLDLPINIVG LAPLCENMPS GKANKPGDVV RARNGKTIQV 

       370        380        390        400        410        420 
DNTDAEGRLI LADALCYAHT FNPKVIINAA TLTGAMDIAL GSGATGVFTN SSWLWNKLFE 

       430        440        450        460        470        480 
ASIETGDRVW RMPLFEHYTR QVIDCQLADV NNIGKYRSAG ACTAAAFLKE FVTHPKWAHL 

       490        500        510 
DIAGVMTNKD EVPYLRKGMA GRPTRTLIEF LFRFSQDSA 

« Hide

Isoform 2 [UniParc].

Checksum: 70766756087AB1FD
Show »

FASTA49854,037

References

« Hide 'large scale' references
[1]"The genome sequence of taurine cattle: a window to ruminant biology and evolution."
The bovine genome sequencing and analysis consortium
Science 324:522-528(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Hereford.
[2]"Isolation of bovine kidney leucine aminopeptidase cDNA: comparison with the lens enzyme and tissue-specific expression of two mRNAs."
Wallner B.P., Hession C., Tizard R., Frey A.Z., Zuliani A., Mura C., Jahngen-Hodge J., Taylor A.
Biochemistry 32:9296-9301(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: Kidney.
[3]NIH - Mammalian Gene Collection (MGC) project
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 11-519 (ISOFORM 1).
Strain: Hereford.
Tissue: Hypothalamus.
[4]"The primary structure of leucine aminopeptidase from bovine eye lens."
Cuypers H.T., van Loon-Klaassen L.A.H., Vree Egberts W.T.M., de Jong W.W., Bloemendal H.
J. Biol. Chem. 257:7077-7085(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 33-519.
Tissue: Lens.
[5]"Sulfhydryl content of bovine eye lens leucine aminopeptidase. Determination of the reactivity of the sulfhydryl groups of the zinc metalloenzyme, of the enzyme activated by Mg2+, Mn2+, and Co2+, and of the metal-free apoenzyme."
Cuypers H.T., van Loon-Klaassen L.A.H., Vree Egberts W.T.M., de Jong W.W., Bloemendal H.
J. Biol. Chem. 257:7086-7091(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 33-519.
[6]Seroussi E.
Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 431-478.
Strain: Holstein.
[7]"Molecular structure of leucine aminopeptidase at 2.7-A resolution."
Burley S.K., David P.R., Taylor A., Lipscomb W.N.
Proc. Natl. Acad. Sci. U.S.A. 87:6878-6882(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 33-519.
[8]"Structure determination and refinement of bovine lens leucine aminopeptidase and its complex with bestatin."
Burley S.K., David P.R., Sweet R.M., Taylor A., Lipscomb W.N.
J. Mol. Biol. 224:113-140(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 33-519.
[9]"Two-metal ion mechanism of bovine lens leucine aminopeptidase: active site solvent structure and binding mode of L-leucinal, a gem-diolate transition state analogue, by X-ray crystallography."
Straeter N., Lipscomb W.N.
Biochemistry 34:14792-14800(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 33-519.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
S65367 mRNA. Translation: AAB28170.1. Different initiation.
BC105385 mRNA. Translation: AAI05386.1.
AJ871963 Genomic DNA. Translation: CAI44744.1.
PIRAPBOL. A54338.
RefSeqNP_776523.2. NM_174098.3.
UniGeneBt.56962.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BLLX-ray2.40E33-519[»]
1BPMX-ray2.90A33-519[»]
1BPNX-ray2.90A33-519[»]
1LAMX-ray1.60A33-516[»]
1LANX-ray1.90A33-516[»]
1LAPX-ray2.70A33-519[»]
1LCPX-ray1.65A/B33-516[»]
2EWBX-ray1.85A33-518[»]
2J9AX-ray1.73A33-519[»]
ProteinModelPortalP00727.
SMRP00727. Positions 33-518.
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBP00727.
ChEMBLCHEMBL1671610.

Protein family/group databases

MEROPSM17.001.

Proteomic databases

PaxDbP00727.
PRIDEP00727.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000007860; ENSBTAP00000007860; ENSBTAG00000005989. [P00727-1]
GeneID781648.
KEGGbta:781648.

Organism-specific databases

CTD51056.

Phylogenomic databases

eggNOGCOG0260.
GeneTreeENSGT00530000063255.
HOGENOMHOG000243129.
HOVERGENHBG003320.
InParanoidP00727.
KOK11142.
OMAGMDAMRA.
OrthoDBEOG7F24SG.
TreeFamTF314954.

Enzyme and pathway databases

BRENDA3.4.11.1. 908.
SABIO-RKP00727.

Family and domain databases

HAMAPMF_00181. Cytosol_peptidase_M17.
InterProIPR011356. Leucine_aapep/pepB.
IPR000819. Peptidase_M17_C.
IPR023042. Peptidase_M17_leu_NH2_pept.
IPR008283. Peptidase_M17_N.
[Graphical view]
PANTHERPTHR11963:SF3. PTHR11963:SF3. 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...

Other

EvolutionaryTraceP00727.
NextBio20924951.

Entry information

Entry nameAMPL_BOVIN
AccessionPrimary (citable) accession number: P00727
Secondary accession number(s): Q2HJH5, Q2PC24
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 139 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references