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UniProtKB - P97449 (AMPN_MOUSE)

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Protein

Aminopeptidase N

Gene

Anpep

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

Functioni

Broad specificity aminopeptidase which plays a role in the final digestion of peptides generated from hydrolysis of proteins by gastric and pancreatic proteases. Also involved in the processing of various peptides including peptide hormones, such as angiotensin III and IV, neuropeptides, and chemokines (By similarity). May also be involved the cleavage of peptides bound to major histocompatibility complex class II molecules of antigen presenting cells (PubMed:8691132). May have a role in angiogenesis and promote cholesterol crystallization (By similarity).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.1 Publication

Cofactori

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi387Zinc; catalyticPROSITE-ProRule annotation1
Active sitei388Proton acceptorPROSITE-ProRule annotation1
Metal bindingi391Zinc; catalyticPROSITE-ProRule annotation1
Metal bindingi410Zinc; catalyticPROSITE-ProRule annotation1
Sitei476Transition state stabilizerBy similarity1

GO - Molecular functioni

Complete GO annotation...

GO - Biological processi

Complete GO annotation...

Keywordsi

Molecular functionAminopeptidase, Developmental protein, Hydrolase, Metalloprotease, Protease
Biological processAngiogenesis, Differentiation
LigandMetal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-MMU-6798695. Neutrophil degranulation.

Protein family/group databases

MEROPSiM01.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Aminopeptidase NCurated (EC:3.4.11.21 Publication)
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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:5000466. Anpep.

Subcellular locationi

  • Cell membrane 1 Publication; Single-pass type II membrane protein By similarity

    • Note: Also found as a soluble form.By similarity

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini2 – 8CytoplasmicBy similarity7
Transmembranei9 – 32Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST24
Topological domaini33 – 966ExtracellularBy similarityAdd BLAST934

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL2189140.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000950822 – 966Aminopeptidase NAdd BLAST965

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi106N-linked (GlcNAc...) asparagine2 Publications1
Glycosylationi114N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi128N-linked (GlcNAc...) asparagine1 Publication1
Modified residuei176SulfotyrosineSequence analysis1
Glycosylationi234N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi288N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi318N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi332N-linked (GlcNAc...) asparagine1 Publication1
Modified residuei418SulfotyrosineSequence analysis1
Modified residuei423SulfotyrosineSequence analysis1
Glycosylationi573N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi606N-linked (GlcNAc...) asparagine2 Publications1
Glycosylationi624N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi666N-linked (GlcNAc...) asparagine; atypical1 Publication1
Glycosylationi734N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi760 ↔ 767By similarity
Glycosylationi783N-linked (GlcNAc...) asparagine; atypical2 Publications1
Glycosylationi784N-linked (GlcNAc...) asparagine2 Publications1
Glycosylationi785N-linked (GlcNAc...) asparagine; atypical2 Publications1
Glycosylationi790N-linked (GlcNAc...) asparagine; atypical1 Publication1
Disulfide bondi797 ↔ 833By similarity
Glycosylationi817N-linked (GlcNAc...) asparagine2 Publications1
Modified residuei852PhosphotyrosineCombined sources1

Post-translational modificationi

N- and O-glycosylated.1 Publication
Sulfated.By similarity
May undergo proteolysis and give rise to a soluble form.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Sulfation

Proteomic databases

MaxQBiP97449.
PaxDbiP97449.
PeptideAtlasiP97449.
PRIDEiP97449.

PTM databases

iPTMnetiP97449.
PhosphoSitePlusiP97449.

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.2 Publications

Gene expression databases

BgeeiENSMUSG00000039062.
CleanExiMM_ANPEP.
ExpressionAtlasiP97449. baseline and differential.
GenevisibleiP97449. MM.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

IntActiP97449. 10 interactors.
MINTiMINT-1870305.
STRINGi10090.ENSMUSP00000035943.

Chemistry databases

BindingDBiP97449.

Structurei

3D structure databases

ProteinModelPortaliP97449.
SMRiP97449.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni33 – 68Cytosolic Ser/Thr-rich junctionAdd BLAST36
Regioni69 – 966MetalloproteaseAdd BLAST898
Regioni351 – 355Substrate bindingBy similarity5

Sequence similaritiesi

Belongs to the peptidase M1 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1046. Eukaryota.
COG0308. LUCA.
GeneTreeiENSGT00760000119082.
HOGENOMiHOG000106482.
HOVERGENiHBG006616.
InParanoidiP97449.
KOiK11140.
OMAiPTWNLKD.
OrthoDBiEOG091G01GH.
PhylomeDBiP97449.
TreeFamiTF300395.

Family and domain databases

CDDicd09601. M1_APN_2. 1 hit.
InterProiView protein in InterPro
IPR024571. ERAP1-like_C_dom.
IPR034016. M1_APN-typ.
IPR001930. Peptidase_M1.
IPR014782. Peptidase_M1_N.
PANTHERiPTHR11533. PTHR11533. 1 hit.
PfamiView protein in Pfam
PF11838. ERAP1_C. 1 hit.
PF01433. Peptidase_M1. 1 hit.
PRINTSiPR00756. ALADIPTASE.
PROSITEiView protein in PROSITE
PS00142. ZINC_PROTEASE. 1 hit.

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)DescriptionActionsGraphical viewLength
Sequence conflicti62T → TATTTATTT in AAH17011 (PubMed:15489334).Curated1
Sequence conflicti62T → TATTTATTT in AAH40792 (PubMed:15489334).Curated1
Sequence conflicti84S → A in AAB19065 (PubMed:8805662).Curated1
Sequence conflicti106N → S in AAH17011 (PubMed:15489334).Curated1
Sequence conflicti106N → S in AAH40792 (PubMed:15489334).Curated1
Sequence conflicti181Q → E in AAH17011 (PubMed:15489334).Curated1
Sequence conflicti181Q → E in AAH40792 (PubMed:15489334).Curated1
Sequence conflicti202D → G in AAH17011 (PubMed:15489334).Curated1
Sequence conflicti202D → G in AAH40792 (PubMed:15489334).Curated1
Sequence conflicti532P → L in AAH17011 (PubMed:15489334).Curated1
Sequence conflicti532P → L in AAH40792 (PubMed:15489334).Curated1
Sequence conflicti557N → S in AAH17011 (PubMed:15489334).Curated1
Sequence conflicti557N → S in AAH40792 (PubMed:15489334).Curated1
Sequence conflicti557Missing AA sequence (PubMed:8805662).Curated1
Sequence conflicti689A → T in AAH17011 (PubMed:15489334).Curated1
Sequence conflicti689A → T in AAH40792 (PubMed:15489334).Curated1
Sequence conflicti726T → M in AAH17011 (PubMed:15489334).Curated1
Sequence conflicti726T → M in AAH40792 (PubMed:15489334).Curated1
Sequence conflicti966S → G in AAH17011 (PubMed:15489334).Curated1
Sequence conflicti966S → G in AAH40792 (PubMed:15489334).Curated1

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_006540678.3.
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.
CCDSiCCDS21388.1.
RefSeqiNP_032512.2. NM_008486.2.
XP_006540741.1. XM_006540678.3.
UniGeneiMm.4487.

3D structure databases

ProteinModelPortaliP97449.
SMRiP97449.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP97449. 10 interactors.
MINTiMINT-1870305.
STRINGi10090.ENSMUSP00000035943.

Chemistry databases

BindingDBiP97449.
ChEMBLiCHEMBL2189140.

Protein family/group databases

MEROPSiM01.001.

PTM databases

iPTMnetiP97449.
PhosphoSitePlusiP97449.

Proteomic databases

MaxQBiP97449.
PaxDbiP97449.
PeptideAtlasiP97449.
PRIDEiP97449.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi290.
MGIiMGI:5000466. Anpep.

Phylogenomic databases

eggNOGiKOG1046. Eukaryota.
COG0308. LUCA.
GeneTreeiENSGT00760000119082.
HOGENOMiHOG000106482.
HOVERGENiHBG006616.
InParanoidiP97449.
KOiK11140.
OMAiPTWNLKD.
OrthoDBiEOG091G01GH.
PhylomeDBiP97449.
TreeFamiTF300395.

Enzyme and pathway databases

ReactomeiR-MMU-6798695. Neutrophil degranulation.

Miscellaneous databases

ChiTaRSiAnpep. mouse.
PROiPR:P97449.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000039062.
CleanExiMM_ANPEP.
ExpressionAtlasiP97449. baseline and differential.
GenevisibleiP97449. MM.

Family and domain databases

CDDicd09601. M1_APN_2. 1 hit.
InterProiView protein in InterPro
IPR024571. ERAP1-like_C_dom.
IPR034016. M1_APN-typ.
IPR001930. Peptidase_M1.
IPR014782. Peptidase_M1_N.
PANTHERiPTHR11533. PTHR11533. 1 hit.
PfamiView protein in Pfam
PF11838. ERAP1_C. 1 hit.
PF01433. Peptidase_M1. 1 hit.
PRINTSiPR00756. ALADIPTASE.
PROSITEiView protein in PROSITE
PS00142. ZINC_PROTEASE. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiAMPN_MOUSE
AccessioniPrimary (citable) accession number: P97449
Secondary accession number(s): Q91YH8, Q99K63
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: June 7, 2017
This is version 169 of the entry and version 4 of the sequence. See 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.