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P97449 (AMPN_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 140. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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=mAPN
EC=3.4.11.2
Alternative name(s):
Alanyl aminopeptidase
Aminopeptidase M
Short name=AP-M
Membrane protein p161
Microsomal aminopeptidase
CD_antigen=CD13
Gene names
Name:Anpep
Synonyms:Lap-1, Lap1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length966 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. May have a role in angiogenesis By similarity. Found to cleave antigen peptides bound to major histocompatibility complex class II molecules of presenting cells. Ref.3

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.

Subcellular location

Membrane; Single-pass type II membrane protein.

Tissue specificity

Highly expressed in intestinal tract and kidney, present in liver, lymph node, spleen, and brain. Found as well in monocytes, macrophages, dendritic cells, veiled cells and B-cells but not on T-cells and thymocytes. Ref.1

Post-translational modification

Sulfated By similarity.

Sequence similarities

Belongs to the peptidase M1 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 966965Aminopeptidase N
PRO_0000095082

Regions

Topological domain2 – 87Cytoplasmic
Transmembrane9 – 3224Helical; Signal-anchor for type II membrane protein; Potential
Topological domain33 – 966934Extracellular
Region33 – 6836Cytosolic Ser/Thr-rich junction
Region69 – 966898Metalloprotease
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 residue4181Sulfotyrosine Potential
Modified residue4231Sulfotyrosine Potential
Modified residue8521Phosphotyrosine Ref.5
Glycosylation1061N-linked (GlcNAc...) Ref.6 Ref.7
Glycosylation1141N-linked (GlcNAc...) Ref.7
Glycosylation1281N-linked (GlcNAc...) Ref.6
Glycosylation2341N-linked (GlcNAc...) Potential
Glycosylation2881N-linked (GlcNAc...) Potential
Glycosylation3181N-linked (GlcNAc...) Potential
Glycosylation3321N-linked (GlcNAc...) Ref.7
Glycosylation5731N-linked (GlcNAc...) Potential
Glycosylation6061N-linked (GlcNAc...) Ref.6 Ref.7
Glycosylation6241N-linked (GlcNAc...) Potential
Glycosylation6661N-linked (GlcNAc...); atypical Ref.6
Glycosylation7341N-linked (GlcNAc...) Potential
Glycosylation7831N-linked (GlcNAc...); atypical Ref.6 Ref.7
Glycosylation7841N-linked (GlcNAc...) Ref.6 Ref.7
Glycosylation7851N-linked (GlcNAc...); atypical Ref.6 Ref.7
Glycosylation7901N-linked (GlcNAc...); atypical Ref.6
Glycosylation8171N-linked (GlcNAc...) Ref.6 Ref.7
Disulfide bond760 ↔ 767 By similarity
Disulfide bond797 ↔ 833 By similarity

Experimental info

Sequence conflict621T → TATTTATTT in AAH17011. Ref.2
Sequence conflict621T → TATTTATTT in AAH40792. Ref.2
Sequence conflict841S → A in AAB19065. Ref.1
Sequence conflict1061N → S in AAH17011. Ref.2
Sequence conflict1061N → S in AAH40792. Ref.2
Sequence conflict1811Q → E in AAH17011. Ref.2
Sequence conflict1811Q → E in AAH40792. Ref.2
Sequence conflict2021D → G in AAH17011. Ref.2
Sequence conflict2021D → G in AAH40792. Ref.2
Sequence conflict5321P → L in AAH17011. Ref.2
Sequence conflict5321P → L in AAH40792. Ref.2
Sequence conflict5571N → S in AAH17011. Ref.2
Sequence conflict5571N → S in AAH40792. Ref.2
Sequence conflict5571Missing AA sequence Ref.1
Sequence conflict6891A → T in AAH17011. Ref.2
Sequence conflict6891A → T in AAH40792. Ref.2
Sequence conflict7261T → M in AAH17011. Ref.2
Sequence conflict7261T → M in AAH40792. Ref.2
Sequence conflict9661S → G in AAH17011. Ref.2
Sequence conflict9661S → G in AAH40792. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P97449 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: FD837F7ACE705835

FASTA966109,651
        10         20         30         40         50         60 
MAKGFYISKT LGILGILLGV AAVCTIIALS VVYAQEKNRN AENSATAPTL PGSTSATTAT 

        70         80         90        100        110        120 
TTPAVDESKP WNQYRLPKTL IPDSYRVILR PYLTPNNQGL YIFQGNSTVR FTCNQTTDVI 

       130        140        150        160        170        180 
IIHSKKLNYT LKGNHRVVLR TLDGTPAPNI DKTELVERTE YLVVHLQGSL VEGRQYEMDS 

       190        200        210        220        230        240 
QFQGELADDL AGFYRSEYME GDVKKVVATT QMQAADARKS FPCFDEPAMK AMFNITLIYP 

       250        260        270        280        290        300 
NNLIALSNML PKESKPYPED PSCTMTEFHS TPKMSTYLLA YIVSEFKNIS SVSANGVQIG 

       310        320        330        340        350        360 
IWARPSAIDE GQGDYALNVT GPILNFFAQH YNTSYPLPKS DQIALPDFNA GAMENWGLVT 

       370        380        390        400        410        420 
YRESSLVFDS QSSSISNKER VVTVIAHELA HQWFGNLVTV AWWNDLWLNE GFASYVEYLG 

       430        440        450        460        470        480 
ADYAEPTWNL KDLMVLNDVY RVMAVDALAS SHPLSSPADE IKTPDQIMEL FDSITYSKGA 

       490        500        510        520        530        540 
SVIRMLSSFL TEDLFKKGLS SYLHTYQYSN TVYLDLWEHL QKAVNQQTAV QPPATVRTIM 

       550        560        570        580        590        600 
DRWILQMGFP VITVNTNTGE ISQKHFLLDS KSNVTRPSEF NYIWIAPIPF LKSGQEDHYW 

       610        620        630        640        650        660 
LDVEKNQSAK FQTSSNEWIL LNINVTGYYL VNYDENNWKK LQNQLQTDLS VIPVINRAQI 

       670        680        690        700        710        720 
IHDSFNLASA KMIPITLALD NTLFLVKEAE YMPWQAALSS LNYFTLMFDR SEVYGPMKRY 

       730        740        750        760        770        780 
LKKQVTPLFF YFQNRTNNWV NRPPTLMEQY NEINAISTAC SSGLKECRDL VVELYSQWMK 

       790        800        810        820        830        840 
NPNNNTIHPN LRSTVYCNAI AFGGEEEWNF AWEQFRNATL VNEADKLRSA LACSKDVWIL 

       850        860        870        880        890        900 
NRYLSYTLNP DYIRKQDTTS TIISIASNVA GHPLVWDFVR SNWKKLFENY GGGSFSFANL 

       910        920        930        940        950        960 
IQGVTRRFSS EFELQQLEQF KADNSATGFG TGTRALEQAL EKTRANIDWV KENKDAVFKW 


FTENSS 

« Hide

References

« Hide 'large scale' references
[1]"p161, a murine membrane protein expressed on mast cells and some macrophages, is mouse CD13/aminopeptidase N."
Chen H., Kinzer C.A., Paul W.E.
J. Immunol. 157:2593-2600(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 538-564; 886-908; 922-942 AND 961-965, TISSUE SPECIFICITY.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Czech II and FVB/N.
Tissue: Mammary tumor.
[3]"A mouse aminopeptidase N is a marker for antigen-presenting cells and appears to be co-expressed with major histocompatibility complex class II molecules."
Hansen A.S., Noren O., Sjostrom H., Werdelin O.
Eur. J. Immunol. 23:2358-2364(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ENZYMATIC CLEAVAGE OF ANTIGEN PEPTIDES BOUND TO CLASS II MHC.
[4]"T cell responses affected by aminopeptidase N (CD13)-mediated trimming of major histocompatibility complex class II-bound peptides."
Larsen S.L., Pedersen L.O., Buus S., Stryhn A.
J. Exp. Med. 184:183-189(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYMATIC CLEAVAGE OF ANTIGEN PEPTIDES BOUND TO CLASS II MHC.
[5]"Quantitative time-resolved phosphoproteomic analysis of mast cell signaling."
Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R.
J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-852, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Mast cell.
[6]"The mouse C2C12 myoblast cell surface N-linked glycoproteome: identification, glycosite occupancy, and membrane orientation."
Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B.
Mol. Cell. Proteomics 8:2555-2569(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-106; ASN-128; ASN-606; ASN-666; ASN-783; ASN-784; ASN-785; ASN-790 AND ASN-817.
Tissue: Myoblast.
[7]"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-106; ASN-114; ASN-332; ASN-606; ASN-783; ASN-784; ASN-785 AND ASN-817.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U77083 mRNA. Translation: AAB19065.1.
BC005431 mRNA. Translation: AAH05431.1.
BC017011 mRNA. Translation: AAH17011.1.
BC040792 mRNA. Translation: AAH40792.1.
RefSeqNP_032512.2. NM_008486.2.
XP_006540741.1. XM_006540678.1.
UniGeneMm.4487.

3D structure databases

ProteinModelPortalP97449.
SMRP97449. Positions 66-965.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP97449. 10 interactions.
MINTMINT-1870305.

Chemistry

ChEMBLCHEMBL2189140.

Protein family/group databases

MEROPSM01.001.

PTM databases

PhosphoSiteP97449.

Proteomic databases

PaxDbP97449.
PRIDEP97449.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000049004; ENSMUSP00000035943; ENSMUSG00000039062.
ENSMUST00000107392; ENSMUSP00000103015; ENSMUSG00000039062.
GeneID16790.
KEGGmmu:16790.
UCSCuc009hzd.1. mouse.

Organism-specific databases

CTD290.
MGIMGI:5000466. Anpep.

Phylogenomic databases

eggNOGCOG0308.
GeneTreeENSGT00740000114965.
HOGENOMHOG000106482.
HOVERGENHBG006616.
InParanoidP97449.
KOK11140.
OMAWVLLNLN.
OrthoDBEOG754HNR.
PhylomeDBP97449.
TreeFamTF300395.

Gene expression databases

ArrayExpressP97449.
BgeeP97449.
CleanExMM_ANPEP.
GenevestigatorP97449.

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

ChiTaRSANPEP. mouse.
NextBio290654.
PROP97449.
SOURCESearch...

Entry information

Entry nameAMPN_MOUSE
AccessionPrimary (citable) accession number: P97449
Secondary accession number(s): Q91YH8, Q99K63
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 140 of the entry and version 4 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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot