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P15684

- AMPN_RAT

UniProt

P15684 - AMPN_RAT

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Protein

Aminopeptidase N

Gene

Anpep

Organism
Rattus norvegicus (Rat)
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 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

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: RGD
  2. metallopeptidase activity Source: UniProtKB-KW
  3. peptide binding Source: RGD
  4. zinc ion binding Source: InterPro

GO - Biological processi

  1. angiogenesis Source: UniProtKB-KW
  2. cell differentiation Source: UniProtKB-KW
  3. cellular aromatic compound metabolic process Source: RGD
  4. negative regulation of renal sodium excretion Source: RGD
  5. 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
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi2991. Anpep.

Subcellular locationi

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. vesicle lumen Source: RGD
  3. vesicle membrane Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 965964Aminopeptidase NPRO_0000095085Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi114 – 1141N-linked (GlcNAc...)Sequence Analysis
Glycosylationi128 – 1281N-linked (GlcNAc...)Sequence Analysis
Modified residuei176 – 1761SulfotyrosineSequence Analysis
Glycosylationi234 – 2341N-linked (GlcNAc...)Sequence Analysis
Glycosylationi242 – 2421N-linked (GlcNAc...)Sequence Analysis
Glycosylationi264 – 2641N-linked (GlcNAc...)Sequence Analysis
Glycosylationi555 – 5551N-linked (GlcNAc...)Sequence Analysis
Glycosylationi606 – 6061N-linked (GlcNAc...)Sequence Analysis
Glycosylationi624 – 6241N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi760 ↔ 767By similarity
Glycosylationi780 – 7801N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi797 ↔ 833By similarity
Modified residuei852 – 8521PhosphotyrosineBy similarity

Post-translational modificationi

Sulfated.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Sulfation

Proteomic databases

PaxDbiP15684.
PRIDEiP15684.

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

Gene expression databases

GenevestigatoriP15684.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

BioGridi249541. 2 interactions.
IntActiP15684. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliP15684.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 87Cytoplasmic
Topological domaini33 – 965933ExtracellularAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei9 – 3224Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni33 – 6836Cytosolic Ser/Thr-rich junctionAdd
BLAST
Regioni69 – 965897MetalloproteaseAdd
BLAST
Regioni351 – 3555Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the peptidase M1 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0308.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti558 – 5581T → A in CAB93958. 1 PublicationCurated
Sequence conflicti582 – 5821Y → L in CAB93958. 1 PublicationCurated
Sequence conflicti590 – 5989YLKNGKEDH → VSQKWKGGS in CAB93958. 1 PublicationCurated
Sequence conflicti802 – 8043FGG → SC(PubMed:2567164)Curated
Sequence conflicti807 – 8071E → A(PubMed:2567164)Curated
Sequence conflicti813 – 8186EQFRKA → ATVPER in AAA57129. (PubMed:2567164)Curated
Sequence conflicti831 – 8333LAC → VGR in AAA57129. (PubMed:2567164)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
M25073 mRNA. Translation: AAA41502.1 .
M26710 mRNA. Translation: AAA57129.1 .
Y18765 mRNA. Translation: CAB93958.1 .
PIRi A32852.
RefSeqi NP_112274.1. NM_031012.1.
UniGenei Rn.11132.
Rn.179371.

3D structure databases

ProteinModelPortali P15684.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 249541. 2 interactions.
IntActi P15684. 1 interaction.

Chemistry

BindingDBi P15684.
ChEMBLi CHEMBL3259.

Protein family/group databases

MEROPSi M01.001.

Proteomic databases

PaxDbi P15684.
PRIDEi P15684.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 81641.
KEGGi rno:81641.
UCSCi RGD:2991. rat.

Organism-specific databases

CTDi 290.
RGDi 2991. Anpep.

Phylogenomic databases

eggNOGi COG0308.
HOGENOMi HOG000106482.
HOVERGENi HBG006616.
InParanoidi P15684.
KOi K11140.
PhylomeDBi P15684.

Enzyme and pathway databases

BioCyci MetaCyc:MONOMER-9982.
SABIO-RK P15684.

Miscellaneous databases

NextBioi 615144.
PROi P15684.

Gene expression databases

Genevestigatori P15684.

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

  1. "Amino acid sequence deduced from a rat kidney cDNA suggests it encodes the Zn-peptidase aminopeptidase N."
    Watt V.M., Yip C.C.
    J. Biol. Chem. 264:5480-5487(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Kidney.
  2. "Molecular cloning and amino acid sequence of rat kidney aminopeptidase M: a member of a super family of zinc-metallohydrolases."
    Malfroy B., Kado-Fong H., Gros C., Giros B., Schwartz J.C., Hellmiss R.
    Biochem. Biophys. Res. Commun. 161:236-241(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Kidney.
  3. Gal-Gaber O.
    Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 198-754.
  4. "p146 type II alveolar epithelial cell antigen is identical to aminopeptidase N."
    Funkhouser J.D., Tangada S.D., Jones M., O S.J., Peterson R.D.
    Am. J. Physiol. 260:L274-L279(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-19; 68-84; 206-215; 286-299 AND 364-371.
  5. "First discrete autoradiographic distribution of aminopeptidase N in various structures of rat brain and spinal cord using the selective iodinated inhibitor 125IRB 129."
    Noble F., Banisadr G., Jardinaud F., Popovici T., Lai-Kuen R., Chen H., Bischoff L., Parsadaniantz S.M., Fournie-Zaluski M.-C., Roques B.P.
    Neuroscience 105:479-488(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.

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: October 1, 2014
This is version 137 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

External Data

Dasty 3