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Protein

Cytosol aminopeptidase

Gene

LAP3

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: -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

Note: 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)DescriptionActionsGraphical viewLength
Metal bindingi282Zinc 21
Metal bindingi287Zinc 11
Metal bindingi287Zinc 21
Active sitei2941
Metal bindingi305Zinc 21
Metal bindingi364Zinc 11
Metal bindingi366Zinc 11
Metal bindingi366Zinc 21
Active sitei3681

GO - Molecular functioni

Keywordsi

Molecular functionAminopeptidase, Hydrolase, Protease
LigandMagnesium, 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
Proteomesi
  • UP000009136 Componenti: Chromosome 6

Organism-specific databases

VGNCiVGNC:30786 LAP3

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL1671610

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001658241 – 519Cytosol aminopeptidaseAdd BLAST519
Isoform 3 (identifier: P00727-3)
Initiator methionineiRemoved5 Publications

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei42PhosphoserineBy similarity1
Modified residuei45N6-succinyllysineBy similarity1
Modified residuei54PhosphoserineBy similarity1
Modified residuei61N6-succinyllysineBy similarity1
Modified residuei103N6-succinyllysineBy similarity1
Modified residuei180PhosphoserineBy similarity1
Modified residuei194PhosphoserineBy similarity1
Modified residuei238PhosphoserineBy similarity1
Modified residuei455N6-acetyllysine; alternateBy similarity1
Modified residuei455N6-succinyllysine; alternateBy similarity1
Modified residuei476N6-succinyllysineBy similarity1
Modified residuei489N6-acetyllysine; alternateBy similarity1
Modified residuei489N6-succinyllysine; alternateBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP00727
PeptideAtlasiP00727
PRIDEiP00727

Expressioni

Gene expression databases

BgeeiENSBTAG00000005989
ExpressionAtlasiP00727 baseline and differential

Interactioni

Subunit structurei

Homohexamer.

GO - Molecular functioni

  • disordered domain specific binding Source: CAFA

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000007860

Chemistry databases

BindingDBiP00727

Structurei

Secondary structure

1519
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi34 – 40Combined sources7
Beta strandi47 – 49Combined sources3
Helixi54 – 62Combined sources9
Turni63 – 65Combined sources3
Helixi66 – 73Combined sources8
Beta strandi83 – 90Combined sources8
Beta strandi93 – 100Combined sources8
Turni110 – 113Combined sources4
Helixi116 – 134Combined sources19
Beta strandi138 – 142Combined sources5
Helixi148 – 159Combined sources12
Beta strandi174 – 181Combined sources8
Helixi183 – 204Combined sources22
Turni207 – 209Combined sources3
Helixi212 – 226Combined sources15
Beta strandi228 – 235Combined sources8
Helixi237 – 242Combined sources6
Helixi246 – 252Combined sources7
Beta strandi255 – 257Combined sources3
Beta strandi260 – 267Combined sources8
Beta strandi269 – 271Combined sources3
Beta strandi277 – 281Combined sources5
Beta strandi283 – 287Combined sources5
Helixi299 – 304Combined sources6
Helixi307 – 321Combined sources15
Beta strandi325 – 337Combined sources13
Beta strandi348 – 351Combined sources4
Beta strandi357 – 361Combined sources5
Turni363 – 366Combined sources4
Helixi367 – 379Combined sources13
Beta strandi384 – 390Combined sources7
Helixi394 – 400Combined sources7
Beta strandi405 – 410Combined sources6
Helixi412 – 425Combined sources14
Beta strandi429 – 431Combined sources3
Helixi436 – 443Combined sources8
Beta strandi446 – 453Combined sources8
Beta strandi455 – 457Combined sources3
Helixi460 – 469Combined sources10
Beta strandi475 – 481Combined sources7
Helixi483 – 485Combined sources3
Beta strandi486 – 492Combined sources7
Beta strandi497 – 499Combined sources3
Helixi504 – 515Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00727

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M17 family.Curated

Phylogenomic databases

eggNOGiKOG2597 Eukaryota
COG0260 LUCA
GeneTreeiENSGT00530000063255
HOGENOMiHOG000243129
HOVERGENiHBG003320
InParanoidiP00727
KOiK11142
OMAiMKNTGPR
OrthoDBiEOG091G0ERB
TreeFamiTF314954

Family and domain databases

CDDicd00433 Peptidase_M17, 1 hit
HAMAPiMF_00181 Cytosol_peptidase_M17, 1 hit
InterProiView protein in InterPro
IPR011356 Leucine_aapep/pepB
IPR000819 Peptidase_M17_C
IPR023042 Peptidase_M17_leu_NH2_pept
IPR008283 Peptidase_M17_N
PANTHERiPTHR11963 PTHR11963, 1 hit
PfamiView protein in Pfam
PF00883 Peptidase_M17, 1 hit
PF02789 Peptidase_M17_N, 1 hit
PRINTSiPR00481 LAMNOPPTDASE
PROSITEiView protein in PROSITE
PS00631 CYTOSOL_AP, 1 hit

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative initiation. AlignAdd to basket

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.

Show »
Length:498
Mass (Da):54,037
Checksum:i70766756087AB1FD
GO
Isoform 3 (identifier: P00727-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-31: Missing.

Show »
Length:488
Mass (Da):53,011
Checksum:i11B49D671A1FBD4D
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti77P → S in AAB28170 (PubMed:8369298).Curated1
Sequence conflicti414 – 415LW → M AA sequence (PubMed:7085616).Curated2
Sequence conflicti414 – 415LW → M AA sequence (PubMed:7085617).Curated2
Sequence conflicti506 – 513Missing AA sequence (PubMed:7085616).Curated8
Sequence conflicti506 – 513Missing AA sequence (PubMed:7085617).Curated8

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0581501 – 31Missing in isoform 3. CuratedAdd BLAST31
Alternative sequenceiVSP_02263411 – 31Missing in isoform 2. 1 PublicationAdd BLAST21

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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

Similar proteinsi

Entry informationi

Entry nameiAMPL_BOVIN
AccessioniPrimary (citable) accession number: P00727
Secondary accession number(s): Q2HJH5, Q2PC24
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: March 28, 2018
This is version 165 of the entry and version 3 of the sequence. See 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

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