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Protein

Aminopeptidase N

Gene

Anpep

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: 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 and involved the cleavage of peptides bound to major histocompatibility complex class II molecules of antigen presenting cells. May have a role in angiogenesis (By similarity).By similarity

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)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

  • aminopeptidase activity Source: RGD
  • metalloaminopeptidase activity Source: GO_Central
  • peptide binding Source: RGD
  • zinc ion binding Source: GO_Central

GO - Biological processi

  • angiogenesis Source: UniProtKB-KW
  • cell differentiation Source: UniProtKB-KW
  • cellular aromatic compound metabolic process Source: RGD
  • negative regulation of renal sodium excretion Source: RGD
  • peptide catabolic process Source: GO_Central
  • proteolysis Source: RGD
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

BioCyciMetaCyc:MONOMER-9982.
SABIO-RKP15684.

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:
rAPN
Alternative name(s):
Alanyl aminopeptidase
Aminopeptidase M
Short name:
AP-M
Kidney Zn peptidase
Short name:
KZP
Microsomal aminopeptidase
CD_antigen: CD13
Gene namesi
Name:Anpep
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2991. Anpep.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini2 – 8Cytoplasmic7
Transmembranei9 – 32Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST24
Topological domaini33 – 965ExtracellularAdd BLAST933

GO - Cellular componenti

  • cytoplasm Source: GO_Central
  • integral component of membrane Source: UniProtKB-KW
  • plasma membrane Source: GO_Central
  • vesicle lumen Source: RGD
  • vesicle membrane Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL3259.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00000950852 – 965Aminopeptidase NAdd BLAST964

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi114N-linked (GlcNAc...)Sequence analysis1
Glycosylationi128N-linked (GlcNAc...)Sequence analysis1
Modified residuei176SulfotyrosineSequence analysis1
Glycosylationi234N-linked (GlcNAc...)Sequence analysis1
Glycosylationi242N-linked (GlcNAc...)Sequence analysis1
Glycosylationi264N-linked (GlcNAc...)Sequence analysis1
Glycosylationi555N-linked (GlcNAc...)Sequence analysis1
Glycosylationi606N-linked (GlcNAc...)Sequence analysis1
Glycosylationi624N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi760 ↔ 767By similarity
Glycosylationi780N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi797 ↔ 833By similarity
Modified residuei852PhosphotyrosineBy similarity1

Post-translational modificationi

Sulfated.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Sulfation

Proteomic databases

PaxDbiP15684.
PRIDEiP15684.

PTM databases

iPTMnetiP15684.
PhosphoSitePlusiP15684.

Expressioni

Tissue specificityi

Widely distributed throughout the CNS. Particularly abundant in kidney and intestinal microvilli, also detected in lung and liver. Weakly expressed in heart and aorta.1 Publication

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

BioGridi249541. 2 interactors.
IntActiP15684. 1 interactor.
STRINGi10116.ENSRNOP00000020002.

Chemistry databases

BindingDBiP15684.

Structurei

3D structure databases

ProteinModelPortaliP15684.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni33 – 68Cytosolic Ser/Thr-rich junctionAdd BLAST36
Regioni69 – 965MetalloproteaseAdd BLAST897
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.
HOGENOMiHOG000106482.
HOVERGENiHBG006616.
InParanoidiP15684.
KOiK11140.
PhylomeDBiP15684.

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.

P15684-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKGFYISKT LGILGILLGV AAVCTIIALS VVYAQEKNRN AENSAIAPTL
60 70 80 90 100
PGSTSATTST TNPAIDESKP WNQYRLPKTL IPDSYQVTLR PYLTPNEQGL
110 120 130 140 150
YIFKGSSTVR FTCNETTNVI IIHSKKLNYT NKGNHRVALR ALGDTPAPNI
160 170 180 190 200
DTTELVERTE YLVVHLQGSL VKGHQYEMDS EFQGELADDL AGFYRSEYME
210 220 230 240 250
GGNKKVVATT QMQAADARKS FPCFDEPAMK ASFNITLIHP NNLTALSNML
260 270 280 290 300
PKDSRTLQED PSWNVTEFHP TPKMSTYLLA YIVSEFKYVE AVSPNRVQIR
310 320 330 340 350
IWARPSAIDE GHGDYALQVT GPILNFFAQH YNTAYPLEKS DQIALPDFNA
360 370 380 390 400
GAMENWGLVT YRESALVFDP QSSSISNKER VVTVIAHELA HQWFGNLVTV
410 420 430 440 450
DWWNDLWLNE GFASYVEFLG ADYAEPTWNL KDLIVLNDVY RVMAVDALAS
460 470 480 490 500
SHPLSSPANE VNTPAQISEL FDSITYSKGA SVLRMLSSFL TEDLFKKGLS
510 520 530 540 550
SYLHTFQYSN TIYLDLWEHL QQAVDSQTAI KLPASVSTIM DRWILQMGFP
560 570 580 590 600
VITVNTSTGE IYQEHFLLDP TSKPTRPSDF NYLWIVPIPY LKNGKEDHYW
610 620 630 640 650
LETEKNQSAE FQTSSNEWLL LNINVTGYYQ VNYDENNWRK IQNQLQTDLS
660 670 680 690 700
VIPVINRAQI IHDSFNLASA GKLSITLPLS NTLFLASETE YMPWEAALSS
710 720 730 740 750
LNYFKLMFDR SEVYGPMKRY LKKQVTPLFA YFKIKTNNWL DRPPTLMEQY
760 770 780 790 800
NEINAISTAC SSGLEECRDL VVGLYSQWMN NSDNNPIHPN LRSTVYCNAI
810 820 830 840 850
AFGGEEEWNF AWEQFRKATL VNEADKLRSA LACSNEVWIL NRYLSYTLNP
860 870 880 890 900
DYIRKQDATS TIVSIANNVV GQTLVWDFVR SNWKKLFEDY GGGSFSFANL
910 920 930 940 950
IQGVTRRFSS EFELQQLEQF KEDNSATGFG SGTRALEQAL EKTKANIKWV
960
KENKDVVLKW FTENS
Length:965
Mass (Da):109,449
Last modified:January 23, 2007 - v2
Checksum:i03A9A14AEFCCE31C
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti558T → A in CAB93958 (Ref. 3) Curated1
Sequence conflicti582Y → L in CAB93958 (Ref. 3) Curated1
Sequence conflicti590 – 598YLKNGKEDH → VSQKWKGGS in CAB93958 (Ref. 3) Curated9
Sequence conflicti802 – 804FGG → SC (PubMed:2567164).Curated3
Sequence conflicti807E → A (PubMed:2567164).Curated1
Sequence conflicti813 – 818EQFRKA → ATVPER in AAA57129 (PubMed:2567164).Curated6
Sequence conflicti831 – 833LAC → VGR in AAA57129 (PubMed:2567164).Curated3

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M25073 mRNA. Translation: AAA41502.1.
M26710 mRNA. Translation: AAA57129.1.
Y18765 mRNA. Translation: CAB93958.1.
PIRiA32852.
RefSeqiNP_112274.1. NM_031012.1.
UniGeneiRn.11132.
Rn.179371.

Genome annotation databases

GeneIDi81641.
KEGGirno:81641.
UCSCiRGD:2991. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M25073 mRNA. Translation: AAA41502.1.
M26710 mRNA. Translation: AAA57129.1.
Y18765 mRNA. Translation: CAB93958.1.
PIRiA32852.
RefSeqiNP_112274.1. NM_031012.1.
UniGeneiRn.11132.
Rn.179371.

3D structure databases

ProteinModelPortaliP15684.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi249541. 2 interactors.
IntActiP15684. 1 interactor.
STRINGi10116.ENSRNOP00000020002.

Chemistry databases

BindingDBiP15684.
ChEMBLiCHEMBL3259.

Protein family/group databases

MEROPSiM01.001.

PTM databases

iPTMnetiP15684.
PhosphoSitePlusiP15684.

Proteomic databases

PaxDbiP15684.
PRIDEiP15684.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi81641.
KEGGirno:81641.
UCSCiRGD:2991. rat.

Organism-specific databases

CTDi290.
RGDi2991. Anpep.

Phylogenomic databases

eggNOGiKOG1046. Eukaryota.
COG0308. LUCA.
HOGENOMiHOG000106482.
HOVERGENiHBG006616.
InParanoidiP15684.
KOiK11140.
PhylomeDBiP15684.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-9982.
SABIO-RKP15684.

Miscellaneous databases

PROiP15684.

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]
ProtoNetiSearch...

Entry informationi

Entry nameiAMPN_RAT
AccessioniPrimary (citable) accession number: P15684
Secondary accession number(s): Q9JHP4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 152 of the entry and version 2 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. Peptidase families
    Classification of peptidase families and list of entries
  2. 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.