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P15684 (AMPN_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 136. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Aminopeptidase N

Short name=AP-N
Short name=rAPN
EC=3.4.11.2
Alternative name(s):
Alanyl aminopeptidase
Aminopeptidase M
Short name=AP-M
Kidney Zn peptidase
Short name=KZP
Microsomal aminopeptidase
CD_antigen=CD13
Gene names
Name:Anpep
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length965 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Catalytic activity

Release of an N-terminal amino acid, Xaa-|-Yaa- from a peptide, amide or arylamide. Xaa is preferably Ala, but may be most amino acids including Pro (slow action). When a terminal hydrophobic residue is followed by a prolyl residue, the two may be released as an intact Xaa-Pro dipeptide.

Cofactor

Binds 1 zinc ion per subunit By similarity.

Subunit structure

Homodimer By similarity.

Subcellular location

Membrane; Single-pass type II membrane protein.

Tissue specificity

Widely distributed throughout the CNS. Particularly abundant in kidney and intestinal microvilli, also detected in lung and liver. Weakly expressed in heart and aorta. Ref.5

Post-translational modification

Sulfated By similarity.

Sequence similarities

Belongs to the peptidase M1 family.

Ontologies

Keywords
   Biological processAngiogenesis
Differentiation
   Cellular componentMembrane
   DomainSignal-anchor
Transmembrane
Transmembrane helix
   LigandMetal-binding
Zinc
   Molecular functionAminopeptidase
Developmental protein
Hydrolase
Metalloprotease
Protease
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
Sulfation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processangiogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

cell differentiation

Inferred from electronic annotation. Source: UniProtKB-KW

cellular aromatic compound metabolic process

Inferred from direct assay PubMed 12110004. Source: RGD

negative regulation of renal sodium excretion

Inferred from mutant phenotype PubMed 19996063. Source: RGD

proteolysis

Inferred from direct assay PubMed 12110004PubMed 16537183. Source: RGD

   Cellular_componentintegral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

vesicle lumen

Inferred from direct assay PubMed 12110004. Source: RGD

vesicle membrane

Inferred from direct assay PubMed 12110004. Source: RGD

   Molecular_functionaminopeptidase activity

Inferred from direct assay PubMed 12110004PubMed 16537183PubMed 16619500. Source: RGD

metallopeptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

peptide binding

Inferred from direct assay PubMed 12110004PubMed 16537183PubMed 8702598. Source: RGD

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.4
Chain2 – 965964Aminopeptidase N
PRO_0000095085

Regions

Topological domain2 – 87Cytoplasmic
Transmembrane9 – 3224Helical; Signal-anchor for type II membrane protein; Potential
Topological domain33 – 965933Extracellular
Region33 – 6836Cytosolic Ser/Thr-rich junction
Region69 – 965897Metalloprotease
Region351 – 3555Substrate binding By similarity

Sites

Active site3881Proton acceptor By similarity
Metal binding3871Zinc; catalytic By similarity
Metal binding3911Zinc; catalytic By similarity
Metal binding4101Zinc; catalytic By similarity
Site4761Transition state stabilizer By similarity

Amino acid modifications

Modified residue1761Sulfotyrosine Potential
Modified residue8521Phosphotyrosine By similarity
Glycosylation1141N-linked (GlcNAc...) Potential
Glycosylation1281N-linked (GlcNAc...) Potential
Glycosylation2341N-linked (GlcNAc...) Potential
Glycosylation2421N-linked (GlcNAc...) Potential
Glycosylation2641N-linked (GlcNAc...) Potential
Glycosylation5551N-linked (GlcNAc...) Potential
Glycosylation6061N-linked (GlcNAc...) Potential
Glycosylation6241N-linked (GlcNAc...) Potential
Glycosylation7801N-linked (GlcNAc...) Potential
Disulfide bond760 ↔ 767 By similarity
Disulfide bond797 ↔ 833 By similarity

Experimental info

Sequence conflict5581T → A in CAB93958. Ref.3
Sequence conflict5821Y → L in CAB93958. Ref.3
Sequence conflict590 – 5989YLKNGKEDH → VSQKWKGGS in CAB93958. Ref.3
Sequence conflict802 – 8043FGG → SC Ref.2
Sequence conflict8071E → A Ref.2
Sequence conflict813 – 8186EQFRKA → ATVPER in AAA57129. Ref.2
Sequence conflict831 – 8333LAC → VGR in AAA57129. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P15684 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 03A9A14AEFCCE31C

FASTA965109,449
        10         20         30         40         50         60 
MAKGFYISKT LGILGILLGV AAVCTIIALS VVYAQEKNRN AENSAIAPTL PGSTSATTST 

        70         80         90        100        110        120 
TNPAIDESKP WNQYRLPKTL IPDSYQVTLR PYLTPNEQGL YIFKGSSTVR FTCNETTNVI 

       130        140        150        160        170        180 
IIHSKKLNYT NKGNHRVALR ALGDTPAPNI DTTELVERTE YLVVHLQGSL VKGHQYEMDS 

       190        200        210        220        230        240 
EFQGELADDL AGFYRSEYME GGNKKVVATT QMQAADARKS FPCFDEPAMK ASFNITLIHP 

       250        260        270        280        290        300 
NNLTALSNML PKDSRTLQED PSWNVTEFHP TPKMSTYLLA YIVSEFKYVE AVSPNRVQIR 

       310        320        330        340        350        360 
IWARPSAIDE GHGDYALQVT GPILNFFAQH YNTAYPLEKS DQIALPDFNA GAMENWGLVT 

       370        380        390        400        410        420 
YRESALVFDP QSSSISNKER VVTVIAHELA HQWFGNLVTV DWWNDLWLNE GFASYVEFLG 

       430        440        450        460        470        480 
ADYAEPTWNL KDLIVLNDVY RVMAVDALAS SHPLSSPANE VNTPAQISEL FDSITYSKGA 

       490        500        510        520        530        540 
SVLRMLSSFL TEDLFKKGLS SYLHTFQYSN TIYLDLWEHL QQAVDSQTAI KLPASVSTIM 

       550        560        570        580        590        600 
DRWILQMGFP VITVNTSTGE IYQEHFLLDP TSKPTRPSDF NYLWIVPIPY LKNGKEDHYW 

       610        620        630        640        650        660 
LETEKNQSAE FQTSSNEWLL LNINVTGYYQ VNYDENNWRK IQNQLQTDLS VIPVINRAQI 

       670        680        690        700        710        720 
IHDSFNLASA GKLSITLPLS NTLFLASETE YMPWEAALSS LNYFKLMFDR SEVYGPMKRY 

       730        740        750        760        770        780 
LKKQVTPLFA YFKIKTNNWL DRPPTLMEQY NEINAISTAC SSGLEECRDL VVGLYSQWMN 

       790        800        810        820        830        840 
NSDNNPIHPN LRSTVYCNAI AFGGEEEWNF AWEQFRKATL VNEADKLRSA LACSNEVWIL 

       850        860        870        880        890        900 
NRYLSYTLNP DYIRKQDATS TIVSIANNVV GQTLVWDFVR SNWKKLFEDY GGGSFSFANL 

       910        920        930        940        950        960 
IQGVTRRFSS EFELQQLEQF KEDNSATGFG SGTRALEQAL EKTKANIKWV KENKDVVLKW 


FTENS 

« Hide

References

[1]"Amino acid sequence deduced from a rat kidney cDNA suggests it encodes the Zn-peptidase aminopeptidase N."
Watt V.M., Yip C.C.
J. Biol. Chem. 264:5480-5487(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Kidney.
[2]"Molecular cloning and amino acid sequence of rat kidney aminopeptidase M: a member of a super family of zinc-metallohydrolases."
Malfroy B., Kado-Fong H., Gros C., Giros B., Schwartz J.C., Hellmiss R.
Biochem. Biophys. Res. Commun. 161:236-241(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Kidney.
[3]Gal-Gaber O.
Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 198-754.
[4]"p146 type II alveolar epithelial cell antigen is identical to aminopeptidase N."
Funkhouser J.D., Tangada S.D., Jones M., O S.J., Peterson R.D.
Am. J. Physiol. 260:L274-L279(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-19; 68-84; 206-215; 286-299 AND 364-371.
[5]"First discrete autoradiographic distribution of aminopeptidase N in various structures of rat brain and spinal cord using the selective iodinated inhibitor 125IRB 129."
Noble F., Banisadr G., Jardinaud F., Popovici T., Lai-Kuen R., Chen H., Bischoff L., Parsadaniantz S.M., Fournie-Zaluski M.-C., Roques B.P.
Neuroscience 105:479-488(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M25073 mRNA. Translation: AAA41502.1.
M26710 mRNA. Translation: AAA57129.1.
Y18765 mRNA. Translation: CAB93958.1.
PIRA32852.
RefSeqNP_112274.1. NM_031012.1.
UniGeneRn.11132.
Rn.179371.

3D structure databases

ProteinModelPortalP15684.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid249541. 2 interactions.
IntActP15684. 1 interaction.

Chemistry

BindingDBP15684.
ChEMBLCHEMBL3259.

Protein family/group databases

MEROPSM01.001.

Proteomic databases

PaxDbP15684.
PRIDEP15684.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID81641.
KEGGrno:81641.
UCSCRGD:2991. rat.

Organism-specific databases

CTD290.
RGD2991. Anpep.

Phylogenomic databases

eggNOGCOG0308.
HOGENOMHOG000106482.
HOVERGENHBG006616.
InParanoidP15684.
KOK11140.
PhylomeDBP15684.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-9982.
SABIO-RKP15684.

Gene expression databases

GenevestigatorP15684.

Family and domain databases

InterProIPR024571. ERAP1-like_C_dom.
IPR001930. Peptidase_M1.
IPR014782. Peptidase_M1_N.
[Graphical view]
PANTHERPTHR11533. PTHR11533. 1 hit.
PfamPF11838. ERAP1_C. 1 hit.
PF01433. Peptidase_M1. 1 hit.
[Graphical view]
PRINTSPR00756. ALADIPTASE.
PROSITEPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio615144.
PROP15684.

Entry information

Entry nameAMPN_RAT
AccessionPrimary (citable) accession number: P15684
Secondary accession number(s): Q9JHP4
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 136 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries