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Reviewed, UniProtKB/Swiss-Prot P15684 (AMPN_RAT)

Last modified October 13, 2009. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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
    Microsomal aminopeptidase
    Aminopeptidase M
      Short name=AP-M
    Kidney Zn peptidase
      Short name=KZP
    CD_antigen=CD13
Gene names
Name: Anpep
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

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Protein attributes

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

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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. Found to cleave antigen peptides bound to major histocompatibility complex class II molecules of 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.

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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 – 3224Signal-anchor for type II membrane protein Potential
Region33 – 6836Cytosolic Ser/Thr-rich junction
Region69 – 965897Metalloprotease

Sites

Active site3881 By similarity
Active site4761Proton donor Potential
Metal binding3871Zinc; catalytic By similarity
Metal binding3911Zinc; catalytic By similarity
Metal binding4101Zinc; catalytic By similarity

Amino acid modifications

Modified residue1761Sulfotyrosine Potential
Modified residue8521Phosphotyrosine By similarity
Modified residue9271Phosphothreonine 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

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

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Sequences

Sequence LengthMass (Da)Tools
P15684-1 [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

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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: 2564389] [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: 2567164] [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: 1673322] [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: 11672613] [Abstract]
Cited for: TISSUE SPECIFICITY.
+Additional computationally mapped references.

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Cross-references

Sequence databases

M25073 mRNA. Translation: AAA41502.1.
M26710 mRNA. Translation: AAA57129.1.
Y18765 mRNA. Translation: CAB93958.1.
IPIIPI00230862.
PIRA32852.
RefSeqNP_112274.1.
UniGeneRn.11132
Rn.179371

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGP15684.

Protein family/group databases

MEROPSM01.001.

Proteomic databases

PRIDEP15684.

Genome annotation databases

EnsemblENSRNOT00000020002; ENSRNOP00000020002; ENSRNOG00000014610; Rattus norvegicus. [Genome view]
GeneID81641.
KEGGrno:81641.

Organism-specific databases

CTD81641.
RGD2991. Anpep.

Phylogenomic databases

HOVERGENP15684.

Enzyme and pathway databases

BioCycMetaCyc:MON-9982.
BRENDA3.4.11.2. 248.

Gene expression databases

ArrayExpressP15684.
GenevestigatorP15684.
GermOnlineENSRNOG00000014610. Rattus norvegicus.

Family and domain databases

InterProIPR006025. Pept_M_Zn_BS.
IPR001930. Peptidase_M1.
IPR014782. Peptidase_M1_N.
[Graphical view]
PANTHERPTHR11533. Peptidase_M1. 1 hit.
PfamPF01433. Peptidase_M1. 1 hit.
[Graphical view]
PRINTSPR00756. ALADIPTASE.
PROSITEPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio615144.

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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: October 13, 2009
This is version 99 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents