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P00727

- AMPL_BOVIN

UniProt

P00727 - AMPL_BOVIN

Protein

Cytosol aminopeptidase

Gene

LAP3

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 142 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides.

    Catalytic activityi

    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.

    Cofactori

    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 regulationi

    Inhibited by bestatin.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi282 – 2821Zinc 2
    Metal bindingi287 – 2871Zinc 1
    Metal bindingi287 – 2871Zinc 2
    Active sitei294 – 2941
    Metal bindingi305 – 3051Zinc 2
    Metal bindingi364 – 3641Zinc 1
    Metal bindingi366 – 3661Zinc 1
    Metal bindingi366 – 3661Zinc 2
    Active sitei368 – 3681

    GO - Molecular functioni

    1. aminopeptidase activity Source: UniProtKB-KW
    2. manganese ion binding Source: InterPro
    3. metalloexopeptidase activity Source: InterPro
    4. peptidase activity Source: AgBase

    Keywords - Molecular functioni

    Aminopeptidase, Hydrolase, Protease

    Keywords - Ligandi

    Magnesium, Manganese, Metal-binding, Zinc

    Enzyme and pathway databases

    BRENDAi3.4.11.1. 908.
    SABIO-RKP00727.

    Protein family/group databases

    MEROPSiM17.001.

    Names & Taxonomyi

    Protein namesi
    Recommended 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 namesi
    Name:LAP3
    OrganismiBos taurus (Bovine)
    Taxonomic identifieri9913 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
    ProteomesiUP000009136: Chromosome 6

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrion Source: AgBase
    2. nucleus Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 519519Cytosol aminopeptidasePRO_0000165824Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei33 – 331N-acetylthreonine
    Modified residuei45 – 451N6-succinyllysineBy similarity
    Modified residuei61 – 611N6-succinyllysineBy similarity
    Modified residuei103 – 1031N6-succinyllysineBy similarity
    Modified residuei180 – 1801PhosphoserineBy similarity
    Modified residuei238 – 2381PhosphoserineBy similarity
    Modified residuei455 – 4551N6-acetyllysine; alternateBy similarity
    Modified residuei455 – 4551N6-succinyllysine; alternateBy similarity
    Modified residuei476 – 4761N6-succinyllysineBy similarity
    Modified residuei489 – 4891N6-acetyllysine; alternateBy similarity
    Modified residuei489 – 4891N6-succinyllysine; alternateBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    PaxDbiP00727.
    PRIDEiP00727.

    Interactioni

    Subunit structurei

    Homohexamer.

    Structurei

    Secondary structure

    1
    519
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi34 – 407
    Beta strandi47 – 493
    Helixi54 – 629
    Turni63 – 653
    Helixi66 – 738
    Beta strandi83 – 908
    Beta strandi93 – 1008
    Turni110 – 1134
    Helixi116 – 13419
    Beta strandi138 – 1425
    Helixi148 – 15912
    Beta strandi174 – 1818
    Helixi183 – 20422
    Turni207 – 2093
    Helixi212 – 22615
    Beta strandi228 – 2358
    Helixi237 – 2426
    Helixi246 – 2527
    Beta strandi255 – 2573
    Beta strandi260 – 2678
    Beta strandi269 – 2713
    Beta strandi277 – 2815
    Beta strandi283 – 2875
    Helixi299 – 3046
    Helixi307 – 32115
    Beta strandi325 – 33713
    Beta strandi348 – 3514
    Beta strandi357 – 3615
    Turni363 – 3664
    Helixi367 – 37913
    Beta strandi384 – 3907
    Helixi394 – 4007
    Beta strandi405 – 4106
    Helixi412 – 42514
    Beta strandi429 – 4313
    Helixi436 – 4438
    Beta strandi446 – 4538
    Beta strandi455 – 4573
    Helixi460 – 46910
    Beta strandi475 – 4817
    Helixi483 – 4853
    Beta strandi486 – 4927
    Beta strandi497 – 4993
    Helixi504 – 51512

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    ProteinModelPortaliP00727.
    SMRiP00727. Positions 33-518.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00727.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase M17 family.Curated

    Phylogenomic databases

    eggNOGiCOG0260.
    GeneTreeiENSGT00530000063255.
    HOGENOMiHOG000243129.
    HOVERGENiHBG003320.
    InParanoidiP00727.
    KOiK11142.
    OMAiGMDAMRA.
    OrthoDBiEOG7F24SG.
    TreeFamiTF314954.

    Family and domain databases

    HAMAPiMF_00181. Cytosol_peptidase_M17.
    InterProiIPR011356. Leucine_aapep/pepB.
    IPR000819. Peptidase_M17_C.
    IPR023042. Peptidase_M17_leu_NH2_pept.
    IPR008283. Peptidase_M17_N.
    [Graphical view]
    PfamiPF00883. Peptidase_M17. 1 hit.
    PF02789. Peptidase_M17_N. 1 hit.
    [Graphical view]
    PRINTSiPR00481. LAMNOPPTDASE.
    PROSITEiPS00631. CYTOSOL_AP. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative initiation. Align

    Isoform 1 (identifier: P00727-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MFLLPLPAAA RVAVRHLSVK RLWAPGPAAA DMTKGLVLGI YSKEKEEDEP    50
    QFTSAGENFN KLVSGKLREI LNISGPPLKA GKTRTFYGLH EDFPSVVVVG 100
    LGKKTAGIDE QENWHEGKEN IRAAVAAGCR QIQDLEIPSV EVDPCGDAQA 150
    AAEGAVLGLY EYDDLKQKRK VVVSAKLHGS EDQEAWQRGV LFASGQNLAR 200
    RLMETPANEM TPTKFAEIVE ENLKSASIKT DVFIRPKSWI EEQEMGSFLS 250
    VAKGSEEPPV FLEIHYKGSP NASEPPLVFV GKGITFDSGG ISIKAAANMD 300
    LMRADMGGAA TICSAIVSAA KLDLPINIVG LAPLCENMPS GKANKPGDVV 350
    RARNGKTIQV DNTDAEGRLI LADALCYAHT FNPKVIINAA TLTGAMDIAL 400
    GSGATGVFTN SSWLWNKLFE ASIETGDRVW RMPLFEHYTR QVIDCQLADV 450
    NNIGKYRSAG ACTAAAFLKE FVTHPKWAHL DIAGVMTNKD EVPYLRKGMA 500
    GRPTRTLIEF LFRFSQDSA 519

    Note: No experimental confirmation available.

    Length:519
    Mass (Da):56,289
    Last modified:January 23, 2007 - v3
    Checksum:iCDA6AED4D937F624
    GO
    Isoform 2 (identifier: P00727-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         11-31: Missing.

    Note: Initiator Met-1 is removed.

    Show »
    Length:498
    Mass (Da):54,037
    Checksum:i70766756087AB1FD
    GO

    Sequence cautioni

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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti77 – 771P → S in AAB28170. (PubMed:8369298)Curated
    Sequence conflicti414 – 4152LW → M AA sequence (PubMed:7085616)Curated
    Sequence conflicti414 – 4152LW → M AA sequence (PubMed:7085617)Curated
    Sequence conflicti506 – 5138Missing AA sequence (PubMed:7085616)Curated
    Sequence conflicti506 – 5138Missing AA sequence (PubMed:7085617)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei11 – 3121Missing in isoform 2. 1 PublicationVSP_022634Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S65367 mRNA. Translation: AAB28170.1. Different initiation.
    BC105385 mRNA. Translation: AAI05386.1.
    AJ871963 Genomic DNA. Translation: CAI44744.1.
    PIRiA54338. APBOL.
    RefSeqiNP_776523.2. NM_174098.3. [P00727-1]
    UniGeneiBt.56962.

    Genome annotation databases

    EnsembliENSBTAT00000007860; ENSBTAP00000007860; ENSBTAG00000005989. [P00727-1]
    GeneIDi781648.
    KEGGibta:781648.

    Keywords - Coding sequence diversityi

    Alternative initiation

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S65367 mRNA. Translation: AAB28170.1 . Different initiation.
    BC105385 mRNA. Translation: AAI05386.1 .
    AJ871963 Genomic DNA. Translation: CAI44744.1 .
    PIRi A54338. APBOL.
    RefSeqi NP_776523.2. NM_174098.3. [P00727-1 ]
    UniGenei Bt.56962.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1BLL X-ray 2.40 E 33-519 [» ]
    1BPM X-ray 2.90 A 33-519 [» ]
    1BPN X-ray 2.90 A 33-519 [» ]
    1LAM X-ray 1.60 A 33-516 [» ]
    1LAN X-ray 1.90 A 33-516 [» ]
    1LAP X-ray 2.70 A 33-519 [» ]
    1LCP X-ray 1.65 A/B 33-516 [» ]
    2EWB X-ray 1.85 A 33-518 [» ]
    2J9A X-ray 1.73 A 33-519 [» ]
    ProteinModelPortali P00727.
    SMRi P00727. Positions 33-518.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    BindingDBi P00727.
    ChEMBLi CHEMBL1671610.

    Protein family/group databases

    MEROPSi M17.001.

    Proteomic databases

    PaxDbi P00727.
    PRIDEi P00727.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSBTAT00000007860 ; ENSBTAP00000007860 ; ENSBTAG00000005989 . [P00727-1 ]
    GeneIDi 781648.
    KEGGi bta:781648.

    Organism-specific databases

    CTDi 51056.

    Phylogenomic databases

    eggNOGi COG0260.
    GeneTreei ENSGT00530000063255.
    HOGENOMi HOG000243129.
    HOVERGENi HBG003320.
    InParanoidi P00727.
    KOi K11142.
    OMAi GMDAMRA.
    OrthoDBi EOG7F24SG.
    TreeFami TF314954.

    Enzyme and pathway databases

    BRENDAi 3.4.11.1. 908.
    SABIO-RK P00727.

    Miscellaneous databases

    EvolutionaryTracei P00727.
    NextBioi 20924951.

    Family and domain databases

    HAMAPi MF_00181. Cytosol_peptidase_M17.
    InterProi IPR011356. Leucine_aapep/pepB.
    IPR000819. Peptidase_M17_C.
    IPR023042. Peptidase_M17_leu_NH2_pept.
    IPR008283. Peptidase_M17_N.
    [Graphical view ]
    Pfami PF00883. Peptidase_M17. 1 hit.
    PF02789. Peptidase_M17_N. 1 hit.
    [Graphical view ]
    PRINTSi PR00481. LAMNOPPTDASE.
    PROSITEi PS00631. CYTOSOL_AP. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.

    Entry informationi

    Entry nameiAMPL_BOVIN
    AccessioniPrimary (citable) accession number: P00727
    Secondary accession number(s): Q2HJH5, Q2PC24
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 142 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3