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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: -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

View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

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

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 8CytoplasmicBy similarity8
Transmembranei9 – 32Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST24
Topological domaini33 – 966ExtracellularBy similarityAdd BLAST934

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL2189140
GuidetoPHARMACOLOGYi1560

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000950821 – 966Aminopeptidase NAdd BLAST966

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.
MINTiP97449
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
OMAiNNPIHPN
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.

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
Mm.488034

Genome annotation databases

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

Similar proteinsi

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: March 28, 2018
This is version 173 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