CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004363
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Aminopeptidase N 
Protein Synonyms/Alias
 AP-N; rAPN; Alanyl aminopeptidase; Aminopeptidase M; AP-M; Kidney Zn peptidase; KZP; Microsomal aminopeptidase; CD13 
Gene Name
 Anpep 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
826TLVNEADKLRSALACacetylation[1]
Reference
 [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405
Functional Description
 Broad specificity aminopeptidase. Plays a role in the final digestion of peptides generated from hydrolysis of proteins by gastric and pancreatic proteases. May be involved in the metabolism of regulatory peptides of diverse cell types, responsible for the processing of peptide hormones, such as angiotensin III and IV, neuropeptides, and chemokines and involved the cleavage of peptides bound to major histocompatibility complex class II molecules of antigen presenting cells. May have a role in angiogenesis (By similarity). 
Sequence Annotation
 REGION 33 68 Cytosolic Ser/Thr-rich junction.
 REGION 69 965 Metalloprotease.
 REGION 351 355 Substrate binding (By similarity).
 ACT_SITE 388 388 Proton acceptor (By similarity).
 METAL 387 387 Zinc; catalytic (By similarity).
 METAL 391 391 Zinc; catalytic (By similarity).
 METAL 410 410 Zinc; catalytic (By similarity).
 MOD_RES 176 176 Sulfotyrosine (Potential).
 MOD_RES 852 852 Phosphotyrosine (By similarity).
 CARBOHYD 114 114 N-linked (GlcNAc...) (Potential).
 CARBOHYD 128 128 N-linked (GlcNAc...) (Potential).
 CARBOHYD 234 234 N-linked (GlcNAc...) (Potential).
 CARBOHYD 242 242 N-linked (GlcNAc...) (Potential).
 CARBOHYD 264 264 N-linked (GlcNAc...) (Potential).
 CARBOHYD 555 555 N-linked (GlcNAc...) (Potential).
 CARBOHYD 606 606 N-linked (GlcNAc...) (Potential).
 CARBOHYD 624 624 N-linked (GlcNAc...) (Potential).
 CARBOHYD 780 780 N-linked (GlcNAc...) (Potential).
 DISULFID 760 767 By similarity.
 DISULFID 797 833 By similarity.  
Keyword
 Aminopeptidase; Angiogenesis; Complete proteome; Developmental protein; Differentiation; Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase; Membrane; Metal-binding; Metalloprotease; Phosphoprotein; Protease; Reference proteome; Signal-anchor; Sulfation; Transmembrane; Transmembrane helix; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 965 AA 
Protein Sequence
MAKGFYISKT LGILGILLGV AAVCTIIALS VVYAQEKNRN AENSAIAPTL PGSTSATTST 60
TNPAIDESKP WNQYRLPKTL IPDSYQVTLR PYLTPNEQGL YIFKGSSTVR FTCNETTNVI 120
IIHSKKLNYT NKGNHRVALR ALGDTPAPNI DTTELVERTE YLVVHLQGSL VKGHQYEMDS 180
EFQGELADDL AGFYRSEYME GGNKKVVATT QMQAADARKS FPCFDEPAMK ASFNITLIHP 240
NNLTALSNML PKDSRTLQED PSWNVTEFHP TPKMSTYLLA YIVSEFKYVE AVSPNRVQIR 300
IWARPSAIDE GHGDYALQVT GPILNFFAQH YNTAYPLEKS DQIALPDFNA GAMENWGLVT 360
YRESALVFDP QSSSISNKER VVTVIAHELA HQWFGNLVTV DWWNDLWLNE GFASYVEFLG 420
ADYAEPTWNL KDLIVLNDVY RVMAVDALAS SHPLSSPANE VNTPAQISEL FDSITYSKGA 480
SVLRMLSSFL TEDLFKKGLS SYLHTFQYSN TIYLDLWEHL QQAVDSQTAI KLPASVSTIM 540
DRWILQMGFP VITVNTSTGE IYQEHFLLDP TSKPTRPSDF NYLWIVPIPY LKNGKEDHYW 600
LETEKNQSAE FQTSSNEWLL LNINVTGYYQ VNYDENNWRK IQNQLQTDLS VIPVINRAQI 660
IHDSFNLASA GKLSITLPLS NTLFLASETE YMPWEAALSS LNYFKLMFDR SEVYGPMKRY 720
LKKQVTPLFA YFKIKTNNWL DRPPTLMEQY NEINAISTAC SSGLEECRDL VVGLYSQWMN 780
NSDNNPIHPN LRSTVYCNAI AFGGEEEWNF AWEQFRKATL VNEADKLRSA LACSNEVWIL 840
NRYLSYTLNP DYIRKQDATS TIVSIANNVV GQTLVWDFVR SNWKKLFEDY GGGSFSFANL 900
IQGVTRRFSS EFELQQLEQF KEDNSATGFG SGTRALEQAL EKTKANIKWV KENKDVVLKW 960
FTENS 965 
Gene Ontology
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0031983; C:vesicle lumen; IDA:RGD.
 GO:0012506; C:vesicle membrane; IDA:RGD.
 GO:0004177; F:aminopeptidase activity; IDA:RGD.
 GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
 GO:0042277; F:peptide binding; IDA:RGD.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
 GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
 GO:0006725; P:cellular aromatic compound metabolic process; IDA:RGD.
 GO:0035814; P:negative regulation of renal sodium excretion; IMP:RGD.
 GO:0006508; P:proteolysis; IDA:RGD. 
Interpro
 IPR024571; DUF3358.
 IPR001930; Peptidase_M1.
 IPR014782; Peptidase_M1_N. 
Pfam
 PF11838; DUF3358
 PF01433; Peptidase_M1 
SMART
  
PROSITE
 PS00142; ZINC_PROTEASE 
PRINTS
 PR00756; ALADIPTASE.