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P00727

- AMPL_BOVIN

UniProt

P00727 - AMPL_BOVIN

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Protein

Cytosol aminopeptidase

Gene

LAP3

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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
Complete GO annotation...

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. extracellular vesicular exosome Source: Ensembl
  2. mitochondrion Source: AgBase
  3. nucleus Source: Ensembl
Complete GO annotation...

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.

Expressioni

Gene expression databases

ExpressionAtlasiP00727. baseline and differential.

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

        10         20         30         40         50
MFLLPLPAAA RVAVRHLSVK RLWAPGPAAA DMTKGLVLGI YSKEKEEDEP
60 70 80 90 100
QFTSAGENFN KLVSGKLREI LNISGPPLKA GKTRTFYGLH EDFPSVVVVG
110 120 130 140 150
LGKKTAGIDE QENWHEGKEN IRAAVAAGCR QIQDLEIPSV EVDPCGDAQA
160 170 180 190 200
AAEGAVLGLY EYDDLKQKRK VVVSAKLHGS EDQEAWQRGV LFASGQNLAR
210 220 230 240 250
RLMETPANEM TPTKFAEIVE ENLKSASIKT DVFIRPKSWI EEQEMGSFLS
260 270 280 290 300
VAKGSEEPPV FLEIHYKGSP NASEPPLVFV GKGITFDSGG ISIKAAANMD
310 320 330 340 350
LMRADMGGAA TICSAIVSAA KLDLPINIVG LAPLCENMPS GKANKPGDVV
360 370 380 390 400
RARNGKTIQV DNTDAEGRLI LADALCYAHT FNPKVIINAA TLTGAMDIAL
410 420 430 440 450
GSGATGVFTN SSWLWNKLFE ASIETGDRVW RMPLFEHYTR QVIDCQLADV
460 470 480 490 500
NNIGKYRSAG ACTAAAFLKE FVTHPKWAHL DIAGVMTNKD EVPYLRKGMA
510
GRPTRTLIEF LFRFSQDSA

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.

Gene expression databases

ExpressionAtlasi P00727. baseline and differential.

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

« Hide 'large scale' publications
  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 29, 2014
This is version 143 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