CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-015128
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Xaa-Pro aminopeptidase 1 
Protein Synonyms/Alias
 Aminoacylproline aminopeptidase; Cytosolic aminopeptidase P; Soluble aminopeptidase P; sAmp; X-Pro aminopeptidase 1; X-prolyl aminopeptidase 1, soluble 
Gene Name
 Xpnpep1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
130IIPTDYWKKMAKVLRacetylation[1, 2, 3]
130IIPTDYWKKMAKVLRsuccinylation[3]
269RIQVLPYKSILSELKacetylation[4]
287ADLSPREKVWVSDKAacetylation[2, 3]
304AVSEAIPKDHRCCMPacetylation[2]
441GTPTAYEKECFTYVLacetylation[4]
441GTPTAYEKECFTYVLubiquitination[5]
546VVLVVPAKTKYNFNNubiquitination[5]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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]
 [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
Functional Description
 Contributes to the degradation of bradykinin. Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides, such as Arg-Pro-Pro (By similarity). 
Sequence Annotation
 METAL 415 415 Manganese 1 (By similarity).
 METAL 426 426 Manganese 1 (By similarity).
 METAL 426 426 Manganese 2 (By similarity).
 METAL 489 489 Manganese 2 (By similarity).
 METAL 523 523 Manganese 1 (By similarity).
 METAL 523 523 Manganese 2 (By similarity).
 METAL 537 537 Manganese 1 (By similarity).
 METAL 537 537 Manganese 2 (By similarity).
 MOD_RES 304 304 N6-acetyllysine (By similarity).  
Keyword
 Acetylation; Aminopeptidase; Complete proteome; Cytoplasm; Hydrolase; Manganese; Metal-binding; Metalloprotease; Protease; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 623 AA 
Protein Sequence
MAPKVTSELL RQLRQAMRNS EYVAEPIQAY IIPSGDAHQS EYIAPCDCRR AFVSGFDGSA 60
GTAIITEEHA AMWTDGRYFL QAAKQMDNNW TLMKMGLKDT PTQEDWLVSV LPEGSRVGVD 120
PLIIPTDYWK KMAKVLRSAG HHLVPVKENL VDKIWTDRPE RPCKPLLTLG LDYTGISWKE 180
KVADLRLKMA ERSIAWFVVT ALDEIAWLFN LRGSDVEHNP VFFSYAIVGL ETIMLFIDGD 240
RVDAPGVKQH LLLDLGLEAE YRIQVLPYKS ILSELKALCA DLSPREKVWV SDKASYAVSE 300
AIPKDHRCCM PYTPICIAKA VKNSAESDGM RRAHIKDAVA LCELFNWLEQ EVPKGGVTEI 360
SAADKAEEFR RQQADFVDLS FPTISSTGPN GAIIHYAPVP ETNRTLSLDE VYLIDSGAQY 420
KDGTTDVTRT MHFGTPTAYE KECFTYVLKG HIAVSAAVFP TGTKGHLLDS FARSALWDSG 480
LDYLHGTGHG VGSFLNVHEG PCGISYKTFS DEPLEAGMIV TDEPGYYEDG AFGIRIENVV 540
LVVPAKTKYN FNNRGSLTFE PLTLVPIQTK MIDVNALTDK ECDWLNSYHQ TCRDVVGKEL 600
QSQGRQEALE WLIRETEPVS RQH 623 
Gene Ontology
 GO:0005737; C:cytoplasm; ISS:UniProtKB.
 GO:0005829; C:cytosol; IEA:Compara.
 GO:0030145; F:manganese ion binding; ISS:UniProtKB.
 GO:0070006; F:metalloaminopeptidase activity; ISS:UniProtKB.
 GO:0010815; P:bradykinin catabolic process; ISS:UniProtKB.
 GO:0006508; P:proteolysis; ISS:UniProtKB. 
Interpro
 IPR000587; Creatinase.
 IPR000994; Pept_M24_structural-domain.
 IPR001131; Peptidase_M24B_aminopep-P_CS. 
Pfam
 PF01321; Creatinase_N
 PF00557; Peptidase_M24 
SMART
  
PROSITE
 PS00491; PROLINE_PEPTIDASE 
PRINTS