UniProtKB - P97449 (AMPN_MOUSE)
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Protein
Aminopeptidase N
Gene
Anpep
Organism
Mus musculus (Mouse)
Status
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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 387 | Zinc; catalyticPROSITE-ProRule annotation | 1 | |
Active sitei | 388 | Proton acceptorPROSITE-ProRule annotation | 1 | |
Metal bindingi | 391 | Zinc; catalyticPROSITE-ProRule annotation | 1 | |
Metal bindingi | 410 | Zinc; catalyticPROSITE-ProRule annotation | 1 | |
Sitei | 476 | Transition state stabilizerBy similarity | 1 |
GO - Molecular functioni
- metalloaminopeptidase activity Source: GO_Central
- peptide binding Source: GO_Central
- zinc ion binding Source: GO_Central
GO - Biological processi
- angiogenesis Source: UniProtKB-KW
- cell-cell signaling Source: GO_Central
- cell differentiation Source: UniProtKB-KW
- peptide catabolic process Source: GO_Central
- proteolysis Source: GO_Central
- regulation of blood pressure Source: GO_Central
- signal transduction Source: GO_Central
Keywordsi
Molecular function | Aminopeptidase, Developmental protein, Hydrolase, Metalloprotease, Protease |
Biological process | Angiogenesis, Differentiation |
Ligand | Metal-binding, Zinc |
Enzyme and pathway databases
Reactomei | R-MMU-6798695 Neutrophil degranulation |
Protein family/group databases
MEROPSi | M01.001 |
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 |
Organismi | Mus musculus (Mouse) |
Taxonomic identifieri | 10090 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus |
Proteomesi |
|
Organism-specific databases
MGIi | MGI:5000466 Anpep |
Subcellular locationi
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Topological domaini | 1 – 8 | CytoplasmicBy similarity | 8 | |
Transmembranei | 9 – 32 | Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST | 24 | |
Topological domaini | 33 – 966 | ExtracellularBy similarityAdd BLAST | 934 |
Keywords - Cellular componenti
Cell membrane, MembranePTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000095082 | 1 – 966 | Aminopeptidase NAdd BLAST | 966 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Glycosylationi | 106 | N-linked (GlcNAc...) asparagine2 Publications | 1 | |
Glycosylationi | 114 | N-linked (GlcNAc...) asparagine1 Publication | 1 | |
Glycosylationi | 128 | N-linked (GlcNAc...) asparagine1 Publication | 1 | |
Modified residuei | 176 | SulfotyrosineSequence analysis | 1 | |
Glycosylationi | 234 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 288 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 318 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 332 | N-linked (GlcNAc...) asparagine1 Publication | 1 | |
Modified residuei | 418 | SulfotyrosineSequence analysis | 1 | |
Modified residuei | 423 | SulfotyrosineSequence analysis | 1 | |
Glycosylationi | 573 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 606 | N-linked (GlcNAc...) asparagine2 Publications | 1 | |
Glycosylationi | 624 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 666 | N-linked (GlcNAc...) asparagine; atypical1 Publication | 1 | |
Glycosylationi | 734 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 760 ↔ 767 | By similarity | ||
Glycosylationi | 783 | N-linked (GlcNAc...) asparagine; atypical2 Publications | 1 | |
Glycosylationi | 784 | N-linked (GlcNAc...) asparagine2 Publications | 1 | |
Glycosylationi | 785 | N-linked (GlcNAc...) asparagine; atypical2 Publications | 1 | |
Glycosylationi | 790 | N-linked (GlcNAc...) asparagine; atypical1 Publication | 1 | |
Disulfide bondi | 797 ↔ 833 | By similarity | ||
Glycosylationi | 817 | N-linked (GlcNAc...) asparagine2 Publications | 1 | |
Modified residuei | 852 | PhosphotyrosineCombined sources | 1 |
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, SulfationProteomic databases
MaxQBi | P97449 |
PaxDbi | P97449 |
PeptideAtlasi | P97449 |
PRIDEi | P97449 |
PTM databases
iPTMneti | P97449 |
PhosphoSitePlusi | P97449 |
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
Bgeei | ENSMUSG00000039062 |
CleanExi | MM_ANPEP |
ExpressionAtlasi | P97449 baseline and differential |
Genevisiblei | P97449 MM |
Interactioni
Subunit structurei
Homodimer.By similarity
Protein-protein interaction databases
IntActi | P97449 10 interactors. |
MINTi | P97449 |
STRINGi | 10090.ENSMUSP00000035943 |
Chemistry databases
BindingDBi | P97449 |
Structurei
3D structure databases
ProteinModelPortali | P97449 |
SMRi | P97449 |
ModBasei | Search... |
MobiDBi | Search... |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 33 – 68 | Cytosolic Ser/Thr-rich junctionAdd BLAST | 36 | |
Regioni | 69 – 966 | MetalloproteaseAdd BLAST | 898 | |
Regioni | 351 – 355 | Substrate bindingBy similarity | 5 |
Sequence similaritiesi
Belongs to the peptidase M1 family.Curated
Keywords - Domaini
Signal-anchor, Transmembrane, Transmembrane helixPhylogenomic databases
eggNOGi | KOG1046 Eukaryota COG0308 LUCA |
GeneTreei | ENSGT00760000119082 |
HOGENOMi | HOG000106482 |
HOVERGENi | HBG006616 |
InParanoidi | P97449 |
KOi | K11140 |
OMAi | NNPIHPN |
OrthoDBi | EOG091G01GH |
PhylomeDBi | P97449 |
TreeFami | TF300395 |
Family and domain databases
CDDi | cd09601 M1_APN_2, 1 hit |
InterProi | View protein in InterPro IPR024571 ERAP1-like_C_dom IPR034016 M1_APN-typ IPR001930 Peptidase_M1 IPR014782 Peptidase_M1_N |
PANTHERi | PTHR11533 PTHR11533, 1 hit |
Pfami | View protein in Pfam PF11838 ERAP1_C, 1 hit PF01433 Peptidase_M1, 1 hit |
PRINTSi | PR00756 ALADIPTASE |
PROSITEi | View protein in PROSITE PS00142 ZINC_PROTEASE, 1 hit |
i Sequence
Sequence statusi: Complete.
P97449-1 [UniParc]FASTAAdd to basket
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
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 62 | T → TATTTATTT in AAH17011 (PubMed:15489334).Curated | 1 | |
Sequence conflicti | 62 | T → TATTTATTT in AAH40792 (PubMed:15489334).Curated | 1 | |
Sequence conflicti | 84 | S → A in AAB19065 (PubMed:8805662).Curated | 1 | |
Sequence conflicti | 106 | N → S in AAH17011 (PubMed:15489334).Curated | 1 | |
Sequence conflicti | 106 | N → S in AAH40792 (PubMed:15489334).Curated | 1 | |
Sequence conflicti | 181 | Q → E in AAH17011 (PubMed:15489334).Curated | 1 | |
Sequence conflicti | 181 | Q → E in AAH40792 (PubMed:15489334).Curated | 1 | |
Sequence conflicti | 202 | D → G in AAH17011 (PubMed:15489334).Curated | 1 | |
Sequence conflicti | 202 | D → G in AAH40792 (PubMed:15489334).Curated | 1 | |
Sequence conflicti | 532 | P → L in AAH17011 (PubMed:15489334).Curated | 1 | |
Sequence conflicti | 532 | P → L in AAH40792 (PubMed:15489334).Curated | 1 | |
Sequence conflicti | 557 | N → S in AAH17011 (PubMed:15489334).Curated | 1 | |
Sequence conflicti | 557 | N → S in AAH40792 (PubMed:15489334).Curated | 1 | |
Sequence conflicti | 557 | Missing AA sequence (PubMed:8805662).Curated | 1 | |
Sequence conflicti | 689 | A → T in AAH17011 (PubMed:15489334).Curated | 1 | |
Sequence conflicti | 689 | A → T in AAH40792 (PubMed:15489334).Curated | 1 | |
Sequence conflicti | 726 | T → M in AAH17011 (PubMed:15489334).Curated | 1 | |
Sequence conflicti | 726 | T → M in AAH40792 (PubMed:15489334).Curated | 1 | |
Sequence conflicti | 966 | S → G in AAH17011 (PubMed:15489334).Curated | 1 | |
Sequence conflicti | 966 | S → G in AAH40792 (PubMed:15489334).Curated | 1 |
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_006540678.3 |
UniGenei | Mm.4487 Mm.488034 |
Genome annotation databases
Ensembli | ENSMUST00000049004; ENSMUSP00000035943; ENSMUSG00000039062 ENSMUST00000107392; ENSMUSP00000103015; ENSMUSG00000039062 |
GeneIDi | 16790 |
KEGGi | mmu:16790 |
UCSCi | uc009hzd.1 mouse |
Similar proteinsi
Entry informationi
Entry namei | AMPN_MOUSE | |
Accessioni | P97449Primary (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: | March 28, 2018 | |
This is version 173 of the entry and version 4 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |