UniProt Accession

 AMPL_MOUSE; Q9CPY7; Q3TFS5; Q4FJV1; Q4FK15; Q99P44; Q9CWN8 

Genbank Protein ID

 AF334160; CT010237; CT010301; AK002819; AK005334; AK008600; AK010502; AK011604; AK166958; AK169032; BC016536 

Genbank Nucleotide ID

 AAK13495.1; CAJ18445.1; CAJ18509.1; BAB23958.1; BAB25769.1; BAB26987.1; BAB27726.1; BAE39141.1; BAE40823.1; AAH16536.1 

Protein Name

 Cytosol aminopeptidase 

Protein Synonyms/Alias

 Leucine aminopeptidase 3; LAP-3; Leucyl aminopeptidase; Proline aminopeptidase; Prolyl aminopeptidase 

Gene Name

 Lap3 

Gene Synonyms/Alias

 Lapep 

Created Date

 July 27, 2013 

Organism

 Mus musculus (Mouse) 

NCBI Taxa ID

 10090 

Lysine Modification

Position	Peptide	Type	References
43	LVLGIYAKDKDDDLP	acetylation	[1]
45	LGIYAKDKDDDLPQF	acetylation	[1, 2, 3, 4]
45	LGIYAKDKDDDLPQF	succinylation	[4]
45	LGIYAKDKDDDLPQF	ubiquitination	[5]
61	SAGESFNKLVSGKLR	acetylation	[1, 4, 6, 7]
61	SAGESFNKLVSGKLR	succinylation	[4]
61	SAGESFNKLVSGKLR	ubiquitination	[5]
79	NISGPPLKAGKTRTF	acetylation	[4]
79	NISGPPLKAGKTRTF	succinylation	[4]
79	NISGPPLKAGKTRTF	ubiquitination	[5]
103	VVVVGLGKRSAGVDD	acetylation	[4, 7]
103	VVVVGLGKRSAGVDD	succinylation	[4]
103	VVVVGLGKRSAGVDD	ubiquitination	[5]
118	QENWHEGKENIRAAV	ubiquitination	[5]
188	GDLEAWEKGVLFASG	ubiquitination	[5]
221	RFAEIIEKNLKSASS	acetylation	[1, 3, 4, 6, 7, 8, 9]
221	RFAEIIEKNLKSASS	succinylation	[4]
221	RFAEIIEKNLKSASS	ubiquitination	[5]
231	KSASSKTKVHIRPKS	acetylation	[1]
342	CENMPSGKANKPGDV	ubiquitination	[5]
455	ADVNNLGKYRSAGAC	acetylation	[1, 2, 3, 4, 7, 9]
455	ADVNNLGKYRSAGAC	succinylation	[4]
455	ADVNNLGKYRSAGAC	ubiquitination	[5]
476	REFVTHTKWAHLDIA	acetylation	[1, 4]
476	REFVTHTKWAHLDIA	succinylation	[4]
489	IAGVMTNKDEIPYLR	acetylation	[1, 4, 6, 7]
489	IAGVMTNKDEIPYLR	succinylation	[4]

Reference

 [1] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
 Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
 J Biol Chem. 2013 Jul 17;. [PMID: 23864654]
 [2] Quantitative assessment of the impact of the gut microbiota on lysine epsilon-acetylation of host proteins using gnotobiotic mice.
 Simon GM, Cheng J, Gordon JI.
 Proc Natl Acad Sci U S A. 2012 Jul 10;109(28):11133-8. [PMID: 22733758]
 [3] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
 [4] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [5] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [6] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [7] Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways.
 Rardin MJ, Newman JC, Held JM, Cusack MP, Sorensen DJ, Li B, Schilling B, Mooney SD, Kahn CR, Verdin E, Gibson BW.
 Proc Natl Acad Sci U S A. 2013 Apr 16;110(16):6601-6. [PMID: 23576753]
 [8] Mitochondrial acetylome analysis in a mouse model of alcohol-induced liver injury utilizing SIRT3 knockout mice.
 Fritz KS, Galligan JJ, Hirschey MD, Verdin E, Petersen DR.
 J Proteome Res. 2012 Mar 2;11(3):1633-43. [PMID: 22309199]
 [9] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441] 

Functional Description

 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). 

Sequence Annotation

 ACT_SITE 294 294 By similarity.
 ACT_SITE 368 368 By similarity.
 METAL 282 282 Zinc 2 (By similarity).
 METAL 287 287 Zinc 1 (By similarity).
 METAL 287 287 Zinc 2 (By similarity).
 METAL 305 305 Zinc 2 (By similarity).
 METAL 364 364 Zinc 1 (By similarity).
 METAL 366 366 Zinc 1 (By similarity).
 METAL 366 366 Zinc 2 (By similarity).
 MOD_RES 221 221 N6-acetyllysine (By similarity).
 MOD_RES 238 238 Phosphoserine (By similarity).  

Keyword

 Acetylation; Alternative initiation; Aminopeptidase; Complete proteome; Cytoplasm; Direct protein sequencing; Hydrolase; Magnesium; Manganese; Metal-binding; Phosphoprotein; Protease; Reference proteome; Zinc. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 519 AA 

Protein Sequence

Gene Ontology

 GO:0005739; C:mitochondrion; IDA:MGI.
 GO:0005634; C:nucleus; IEA:Compara.
 GO:0005802; C:trans-Golgi network; ISO:MGI.
 GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
 GO:0030145; F:manganese ion binding; IEA:InterPro.
 GO:0008235; F:metalloexopeptidase activity; IEA:InterPro.
 GO:0008233; F:peptidase activity; IDA:MGI.
 GO:0006508; P:proteolysis; IEA:UniProtKB-KW. 

Interpro

 IPR011356; Leucine_aapep/pepB.
 IPR000819; Peptidase_M17_C.
 IPR023042; Peptidase_M17_leu_NH2_pept.
 IPR008283; Peptidase_M17_N. 

Pfam

 PF00883; Peptidase_M17
 PF02789; Peptidase_M17_N 

SMART

  

PROSITE

 PS00631; CYTOSOL_AP 

PRINTS

 PR00481; LAMNOPPTDASE.