CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-017475
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Aminopeptidase O 
Protein Synonyms/Alias
 AP-O 
Gene Name
 AOPEP 
Gene Synonyms/Alias
 C9orf3; ONPEP 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
55EDGNRFKKQNSSIEEubiquitination[1]
169AAVPGLEKFTRSPELubiquitination[1]
231TWSLQIRKTGAQTATubiquitination[1]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961
Functional Description
 Aminopeptidases catalyze the hydrolysis of amino acid residues from the N-terminus of peptide or protein substrates. Able to cleave angiotensin III to generate angiotensin IV, a bioactive peptide of the renin-angiotensin pathway. Not able to cleave angiotensin I and angiotensin II. May play a role in the proteolytic processing of bioactive peptides in tissues such as testis and heart. 
Sequence Annotation
 ACT_SITE 480 480 Proton acceptor (By similarity).
 METAL 479 479 Zinc; catalytic (By similarity).
 METAL 483 483 Zinc; catalytic (By similarity).
 METAL 502 502 Zinc; catalytic (By similarity).  
Keyword
 Alternative splicing; Aminopeptidase; Complete proteome; Cytoplasm; Hydrolase; Metal-binding; Metalloprotease; Polymorphism; Protease; Reference proteome; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 819 AA 
Protein Sequence
MDIQLDPARD DLPLMANTSH ILVKHYVLDL DVDFESQVIE GTIVLFLEDG NRFKKQNSSI 60
EEACQSESNK ACKFGMPEPC HIPVTNARTF SSEMEYNDFA ICSKGEKDTS DKDGNHDNQE 120
HASGISSSKY CCDTGNHGSE DFLLVLDCCD LSVLKVEEVD VAAVPGLEKF TRSPELTVVS 180
EEFRNQIVRE LVTLPANRWR EQLDYYARCS QAPGCGELLF DTDTWSLQIR KTGAQTATDF 240
PHAIRIWYKT KPEGRSVTWT SDQSGRPCVY TVGSPINNRA LFPCQEPPVA MSTWQATVRA 300
AASFVVLMSG ENSAKPTQLW EECSSWYYYV TMPMPASTFT IAVGCWTEMK METWSSNDLA 360
TERPFSPSEA NFRHVGVCSH MEYPCRFQNA SATTQEIIPH RVFAPVCLTG ACQETLLRLI 420
PPCLSAAHSV LGAHPFSRLD VLIVPANFPS LGMASPHIMF LSQSILTGGN HLCGTRLCHE 480
IAHAWFGLAI GARDWTEEWL SEGFATHLED VFWATAQQLA PYEAREQQEL RACLRWRRLQ 540
DEMQCSPEEM QVLRPSKDKT GHTSDSGASV IKHGLNPEKI FMQVHYLKGY FLLRFLAKRL 600
GDETYFSFLR KFVHTFHGQL ILSQDFLQML LENIPEEKRL ELSVENIYQD WLESSGIPKP 660
LQRERRAGAE CGLARQVRAE VTKWIGVNRR PRKRKRREKE EVFEKLLPDQ LVLLLEHLLE 720
QKTLSPRTLQ SLQRTYHLQD QDAEVRHRWC ELIVKHKFTK AYKSVERFLQ EDQAMGVYLY 780
GELMVSEDAR QQQLARRCFE RTKEQMDRSS AQVVAEMLF 819 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0004177; F:aminopeptidase activity; IDA:UniProtKB.
 GO:0008237; F:metallopeptidase activity; IDA:UniProtKB.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0019370; P:leukotriene biosynthetic process; IEA:InterPro.
 GO:0006508; P:proteolysis; IDA:UniProtKB. 
Interpro
 IPR016024; ARM-type_fold.
 IPR001930; Peptidase_M1.
 IPR015211; Peptidase_M1_C.
 IPR014782; Peptidase_M1_N. 
Pfam
 PF09127; Leuk-A4-hydro_C
 PF01433; Peptidase_M1 
SMART
  
PROSITE
 PS00142; ZINC_PROTEASE 
PRINTS