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P97449

- AMPN_MOUSE

UniProt

P97449 - AMPN_MOUSE

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Protein

Aminopeptidase N

Gene

Anpep

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.By similarity1 Publication

Catalytic activityi

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.

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi387 – 3871Zinc; catalyticPROSITE-ProRule annotation
Active sitei388 – 3881Proton acceptorPROSITE-ProRule annotation
Metal bindingi391 – 3911Zinc; catalyticPROSITE-ProRule annotation
Metal bindingi410 – 4101Zinc; catalyticPROSITE-ProRule annotation
Sitei476 – 4761Transition state stabilizerBy similarity

GO - Molecular functioni

  1. aminopeptidase activity Source: UniProtKB-KW
  2. metallopeptidase activity Source: UniProtKB-KW
  3. zinc ion binding Source: InterPro

GO - Biological processi

  1. angiogenesis Source: UniProtKB-KW
  2. cell differentiation Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Developmental protein, Hydrolase, Metalloprotease, Protease

Keywords - Biological processi

Angiogenesis, Differentiation

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_196539. Metabolism of Angiotensinogen to Angiotensins.

Protein family/group databases

MEROPSiM01.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Aminopeptidase N (EC:3.4.11.2)
Short name:
AP-N
Short name:
mAPN
Alternative name(s):
Alanyl aminopeptidase
Aminopeptidase M
Short name:
AP-M
Membrane protein p161
Microsomal aminopeptidase
CD_antigen: CD13
Gene namesi
Name:Anpep
Synonyms:Lap-1, Lap1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 7

Organism-specific databases

MGIiMGI:5000466. Anpep.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 87Cytoplasmic
Transmembranei9 – 3224Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini33 – 966934ExtracellularAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum-Golgi intermediate compartment Source: Ensembl
  2. external side of plasma membrane Source: MGI
  3. extracellular space Source: Ensembl
  4. extracellular vesicular exosome Source: Ensembl
  5. integral component of membrane Source: UniProtKB-KW
  6. lysosomal membrane Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 966965Aminopeptidase NPRO_0000095082Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi106 – 1061N-linked (GlcNAc...)2 Publications
Glycosylationi114 – 1141N-linked (GlcNAc...)1 Publication
Glycosylationi128 – 1281N-linked (GlcNAc...)1 Publication
Modified residuei176 – 1761SulfotyrosineSequence Analysis
Glycosylationi234 – 2341N-linked (GlcNAc...)Sequence Analysis
Glycosylationi288 – 2881N-linked (GlcNAc...)Sequence Analysis
Glycosylationi318 – 3181N-linked (GlcNAc...)Sequence Analysis
Glycosylationi332 – 3321N-linked (GlcNAc...)1 Publication
Modified residuei418 – 4181SulfotyrosineSequence Analysis
Modified residuei423 – 4231SulfotyrosineSequence Analysis
Glycosylationi573 – 5731N-linked (GlcNAc...)Sequence Analysis
Glycosylationi606 – 6061N-linked (GlcNAc...)2 Publications
Glycosylationi624 – 6241N-linked (GlcNAc...)Sequence Analysis
Glycosylationi666 – 6661N-linked (GlcNAc...); atypical1 Publication
Glycosylationi734 – 7341N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi760 ↔ 767By similarity
Glycosylationi783 – 7831N-linked (GlcNAc...); atypical2 Publications
Glycosylationi784 – 7841N-linked (GlcNAc...)2 Publications
Glycosylationi785 – 7851N-linked (GlcNAc...); atypical2 Publications
Glycosylationi790 – 7901N-linked (GlcNAc...); atypical1 Publication
Disulfide bondi797 ↔ 833By similarity
Glycosylationi817 – 8171N-linked (GlcNAc...)2 Publications
Modified residuei852 – 8521Phosphotyrosine1 Publication

Post-translational modificationi

Sulfated.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Sulfation

Proteomic databases

MaxQBiP97449.
PaxDbiP97449.
PRIDEiP97449.

PTM databases

PhosphoSiteiP97449.

Expressioni

Tissue specificityi

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.1 Publication

Gene expression databases

BgeeiP97449.
CleanExiMM_ANPEP.
ExpressionAtlasiP97449. baseline and differential.
GenevestigatoriP97449.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

IntActiP97449. 10 interactions.
MINTiMINT-1870305.

Structurei

3D structure databases

ProteinModelPortaliP97449.
SMRiP97449. Positions 66-965.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni33 – 6836Cytosolic Ser/Thr-rich junctionAdd
BLAST
Regioni69 – 966898MetalloproteaseAdd
BLAST
Regioni351 – 3555Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the peptidase M1 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0308.
GeneTreeiENSGT00760000119082.
HOGENOMiHOG000106482.
HOVERGENiHBG006616.
InParanoidiP97449.
KOiK11140.
OMAiWVLLNLN.
OrthoDBiEOG754HNR.
PhylomeDBiP97449.
TreeFamiTF300395.

Family and domain databases

InterProiIPR024571. ERAP1-like_C_dom.
IPR001930. Peptidase_M1.
IPR014782. Peptidase_M1_N.
[Graphical view]
PANTHERiPTHR11533. PTHR11533. 1 hit.
PfamiPF11838. ERAP1_C. 1 hit.
PF01433. Peptidase_M1. 1 hit.
[Graphical view]
PRINTSiPR00756. ALADIPTASE.
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P97449-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAKGFYISKT LGILGILLGV AAVCTIIALS VVYAQEKNRN AENSATAPTL
60 70 80 90 100
PGSTSATTAT TTPAVDESKP WNQYRLPKTL IPDSYRVILR PYLTPNNQGL
110 120 130 140 150
YIFQGNSTVR FTCNQTTDVI IIHSKKLNYT LKGNHRVVLR TLDGTPAPNI
160 170 180 190 200
DKTELVERTE YLVVHLQGSL VEGRQYEMDS QFQGELADDL AGFYRSEYME
210 220 230 240 250
GDVKKVVATT QMQAADARKS FPCFDEPAMK AMFNITLIYP NNLIALSNML
260 270 280 290 300
PKESKPYPED PSCTMTEFHS TPKMSTYLLA YIVSEFKNIS SVSANGVQIG
310 320 330 340 350
IWARPSAIDE GQGDYALNVT GPILNFFAQH YNTSYPLPKS DQIALPDFNA
360 370 380 390 400
GAMENWGLVT YRESSLVFDS QSSSISNKER VVTVIAHELA HQWFGNLVTV
410 420 430 440 450
AWWNDLWLNE GFASYVEYLG ADYAEPTWNL KDLMVLNDVY RVMAVDALAS
460 470 480 490 500
SHPLSSPADE IKTPDQIMEL FDSITYSKGA SVIRMLSSFL TEDLFKKGLS
510 520 530 540 550
SYLHTYQYSN TVYLDLWEHL QKAVNQQTAV QPPATVRTIM DRWILQMGFP
560 570 580 590 600
VITVNTNTGE ISQKHFLLDS KSNVTRPSEF NYIWIAPIPF LKSGQEDHYW
610 620 630 640 650
LDVEKNQSAK FQTSSNEWIL LNINVTGYYL VNYDENNWKK LQNQLQTDLS
660 670 680 690 700
VIPVINRAQI IHDSFNLASA KMIPITLALD NTLFLVKEAE YMPWQAALSS
710 720 730 740 750
LNYFTLMFDR SEVYGPMKRY LKKQVTPLFF YFQNRTNNWV NRPPTLMEQY
760 770 780 790 800
NEINAISTAC SSGLKECRDL VVELYSQWMK NPNNNTIHPN LRSTVYCNAI
810 820 830 840 850
AFGGEEEWNF AWEQFRNATL VNEADKLRSA LACSKDVWIL NRYLSYTLNP
860 870 880 890 900
DYIRKQDTTS TIISIASNVA GHPLVWDFVR SNWKKLFENY GGGSFSFANL
910 920 930 940 950
IQGVTRRFSS EFELQQLEQF KADNSATGFG TGTRALEQAL EKTRANIDWV
960
KENKDAVFKW FTENSS
Length:966
Mass (Da):109,651
Last modified:January 23, 2007 - v4
Checksum:iFD837F7ACE705835
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti62 – 621T → TATTTATTT in AAH17011. (PubMed:15489334)Curated
Sequence conflicti62 – 621T → TATTTATTT in AAH40792. (PubMed:15489334)Curated
Sequence conflicti84 – 841S → A in AAB19065. (PubMed:8805662)Curated
Sequence conflicti106 – 1061N → S in AAH17011. (PubMed:15489334)Curated
Sequence conflicti106 – 1061N → S in AAH40792. (PubMed:15489334)Curated
Sequence conflicti181 – 1811Q → E in AAH17011. (PubMed:15489334)Curated
Sequence conflicti181 – 1811Q → E in AAH40792. (PubMed:15489334)Curated
Sequence conflicti202 – 2021D → G in AAH17011. (PubMed:15489334)Curated
Sequence conflicti202 – 2021D → G in AAH40792. (PubMed:15489334)Curated
Sequence conflicti532 – 5321P → L in AAH17011. (PubMed:15489334)Curated
Sequence conflicti532 – 5321P → L in AAH40792. (PubMed:15489334)Curated
Sequence conflicti557 – 5571N → S in AAH17011. (PubMed:15489334)Curated
Sequence conflicti557 – 5571N → S in AAH40792. (PubMed:15489334)Curated
Sequence conflicti557 – 5571Missing AA sequence (PubMed:8805662)Curated
Sequence conflicti689 – 6891A → T in AAH17011. (PubMed:15489334)Curated
Sequence conflicti689 – 6891A → T in AAH40792. (PubMed:15489334)Curated
Sequence conflicti726 – 7261T → M in AAH17011. (PubMed:15489334)Curated
Sequence conflicti726 – 7261T → M in AAH40792. (PubMed:15489334)Curated
Sequence conflicti966 – 9661S → G in AAH17011. (PubMed:15489334)Curated
Sequence conflicti966 – 9661S → G in AAH40792. (PubMed:15489334)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U77083 mRNA. Translation: AAB19065.1.
BC005431 mRNA. Translation: AAH05431.1.
BC017011 mRNA. Translation: AAH17011.1.
BC040792 mRNA. Translation: AAH40792.1.
CCDSiCCDS21388.1.
RefSeqiNP_032512.2. NM_008486.2.
XP_006540741.1. XM_006540678.1.
UniGeneiMm.4487.

Genome annotation databases

EnsembliENSMUST00000049004; ENSMUSP00000035943; ENSMUSG00000039062.
ENSMUST00000107392; ENSMUSP00000103015; ENSMUSG00000039062.
GeneIDi16790.
KEGGimmu:16790.
UCSCiuc009hzd.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U77083 mRNA. Translation: AAB19065.1 .
BC005431 mRNA. Translation: AAH05431.1 .
BC017011 mRNA. Translation: AAH17011.1 .
BC040792 mRNA. Translation: AAH40792.1 .
CCDSi CCDS21388.1.
RefSeqi NP_032512.2. NM_008486.2.
XP_006540741.1. XM_006540678.1.
UniGenei Mm.4487.

3D structure databases

ProteinModelPortali P97449.
SMRi P97449. Positions 66-965.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P97449. 10 interactions.
MINTi MINT-1870305.

Chemistry

BindingDBi P97449.
ChEMBLi CHEMBL2189140.

Protein family/group databases

MEROPSi M01.001.

PTM databases

PhosphoSitei P97449.

Proteomic databases

MaxQBi P97449.
PaxDbi P97449.
PRIDEi P97449.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000049004 ; ENSMUSP00000035943 ; ENSMUSG00000039062 .
ENSMUST00000107392 ; ENSMUSP00000103015 ; ENSMUSG00000039062 .
GeneIDi 16790.
KEGGi mmu:16790.
UCSCi uc009hzd.1. mouse.

Organism-specific databases

CTDi 290.
MGIi MGI:5000466. Anpep.

Phylogenomic databases

eggNOGi COG0308.
GeneTreei ENSGT00760000119082.
HOGENOMi HOG000106482.
HOVERGENi HBG006616.
InParanoidi P97449.
KOi K11140.
OMAi WVLLNLN.
OrthoDBi EOG754HNR.
PhylomeDBi P97449.
TreeFami TF300395.

Enzyme and pathway databases

Reactomei REACT_196539. Metabolism of Angiotensinogen to Angiotensins.

Miscellaneous databases

ChiTaRSi Anpep. mouse.
NextBioi 290654.
PROi P97449.
SOURCEi Search...

Gene expression databases

Bgeei P97449.
CleanExi MM_ANPEP.
ExpressionAtlasi P97449. baseline and differential.
Genevestigatori P97449.

Family and domain databases

InterProi IPR024571. ERAP1-like_C_dom.
IPR001930. Peptidase_M1.
IPR014782. Peptidase_M1_N.
[Graphical view ]
PANTHERi PTHR11533. PTHR11533. 1 hit.
Pfami PF11838. ERAP1_C. 1 hit.
PF01433. Peptidase_M1. 1 hit.
[Graphical view ]
PRINTSi PR00756. ALADIPTASE.
PROSITEi PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiAMPN_MOUSE
AccessioniPrimary (citable) accession number: P97449
Secondary accession number(s): Q91YH8, Q99K63
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 146 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3