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P15145 (AMPN_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Aminopeptidase N

Short name=AP-N
Short name=pAPN
EC=3.4.11.2
Alternative name(s):
Alanyl aminopeptidase
Aminopeptidase M
Short name=AP-M
Microsomal aminopeptidase
gp130
CD_antigen=CD13
Gene names
Name:ANPEP
OrganismSus scrofa (Pig) [Reference proteome]
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus

Protein attributes

Sequence length963 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. It is able to degrade Leu-enkephalin and Met-enkephalin but not cholecystokinin CCK8, neuromedin C (GRP-10), somatostatin-14, substance P and vasoactive intestinal peptide. In case of porcine transmissible gastroenteritis coronavirus (TGEV) and porcine respiratory coronavirus (PRCoV) infections, serves as a receptor for TGEV and PRCoV spike glycoprotein in a species-specific manner. Ref.1 Ref.5 Ref.6 Ref.8 Ref.9

Catalytic activity

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.

Cofactor

Binds 1 zinc ion per subunit. Ref.12

Subunit structure

Homodimer. Interacts with TGEV and PRCoV spike glycoprotein. Ref.10 Ref.12

Subcellular location

Membrane; Single-pass type II membrane protein.

Post-translational modification

Sulfated.

Sequence similarities

Belongs to the peptidase M1 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.3
Chain2 – 963962Aminopeptidase N
PRO_0000095083

Regions

Topological domain2 – 87Cytoplasmic
Transmembrane9 – 3224Helical; Signal-anchor for type II membrane protein; Potential
Topological domain33 – 963931Extracellular
Region33 – 6432Cytosolic Ser/Thr-rich junction
Region65 – 963899Metalloprotease
Region347 – 3515Substrate binding By similarity
Region717 – 81397Interaction with TGEV spike glycoprotein

Sites

Active site3841Proton acceptor By similarity
Metal binding3831Zinc; catalytic
Metal binding3871Zinc; catalytic
Metal binding4061Zinc; catalytic
Site4721Transition state stabilizer By similarity

Amino acid modifications

Modified residue1711Sulfotyrosine Potential
Glycosylation821N-linked (GlcNAc...) Ref.12
Glycosylation1241N-linked (GlcNAc...) Ref.12
Glycosylation2291N-linked (GlcNAc...) Ref.12
Glycosylation2371N-linked (GlcNAc...) Ref.12
Glycosylation2581N-linked (GlcNAc...) Potential
Glycosylation2861N-linked (GlcNAc...) Potential
Glycosylation3141N-linked (GlcNAc...) Ref.12
Glycosylation3281N-linked (GlcNAc...) Ref.12
Glycosylation5061N-linked (GlcNAc...) Ref.12
Glycosylation5561N-linked (GlcNAc...) Potential
Glycosylation5691N-linked (GlcNAc...) Potential
Glycosylation6221N-linked (GlcNAc...) Ref.12
Glycosylation6461N-linked (GlcNAc...) Ref.12
Glycosylation7361N-linked (GlcNAc...) Ref.12
Disulfide bond758 ↔ 765 Ref.12
Disulfide bond795 ↔ 831 Ref.12

Experimental info

Sequence conflict821N → F in CAA82641. Ref.1
Sequence conflict821N → F in CAA34216. Ref.2
Sequence conflict107 – 1082LL → FI in CAA23291. Ref.4
Sequence conflict1111E → G in CAA23291. Ref.4
Sequence conflict1261T → N in CAA23291. Ref.4
Sequence conflict1401S → F in CAA23291. Ref.4

Secondary structure

..................................................................................................................................................................... 963
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P15145 [UniParc].

Last modified February 6, 2013. Version 4.
Checksum: 0C55FDD2CE1F3E10

FASTA963108,832
        10         20         30         40         50         60 
MAKGFYISKA LGILGILLGV AAVATIIALS VVYAQEKNKN AEHVPQAPTS PTITTTAAIT 

        70         80         90        100        110        120 
LDQSKPWNRY RLPTTLLPDS YNVTLRPYLT PNADGLYIFK GKSIVRLLCQ EPTDVIIIHS 

       130        140        150        160        170        180 
KKLNYTTQGH MVVLRGVGDS QVPEIDRTEL VELTEYLVVH LKGSLQPGHM YEMESEFQGE 

       190        200        210        220        230        240 
LADDLAGFYR SEYMEGNVKK VLATTQMQST DARKSFPCFD EPAMKATFNI TLIHPNNLTA 

       250        260        270        280        290        300 
LSNMPPKGSS TPLAEDPNWS VTEFETTPVM STYLLAYIVS EFQSVNETAQ NGVLIRIWAR 

       310        320        330        340        350        360 
PNAIAEGHGM YALNVTGPIL NFFANHYNTS YPLPKSDQIA LPDFNAGAME NWGLVTYREN 

       370        380        390        400        410        420 
ALLFDPQSSS ISNKERVVTV IAHELAHQWF GNLVTLAWWN DLWLNEGFAS YVEYLGADHA 

       430        440        450        460        470        480 
EPTWNLKDLI VPGDVYRVMA VDALASSHPL TTPAEEVNTP AQISEMFDSI SYSKGASVIR 

       490        500        510        520        530        540 
MLSNFLTEDL FKEGLASYLH AFAYQNTTYL DLWEHLQKAV DAQTSIRLPD TVRAIMDRWT 

       550        560        570        580        590        600 
LQMGFPVITV DTKTGNISQK HFLLDSESNV TRSSAFDYLW IVPISSIKNG VMQDHYWLRD 

       610        620        630        640        650        660 
VSQAQNDLFK TASDDWVLLN VNVTGYFQVN YDEDNWRMIQ HQLQTNLSVI PVINRAQVIY 

       670        680        690        700        710        720 
DSFNLATAHM VPVTLALDNT LFLNGEKEYM PWQAALSSLS YFSLMFDRSE VYGPMKKYLR 

       730        740        750        760        770        780 
KQVEPLFQHF ETLTKNWTER PENLMDQYSE INAISTACSN GLPQCENLAK TLFDQWMSDP 

       790        800        810        820        830        840 
ENNPIHPNLR STIYCNAIAQ GGQDQWDFAW GQLQQAQLVN EADKLRSALA CSNEVWLLNR 

       850        860        870        880        890        900 
YLGYTLNPDL IRKQDATSTI NSIASNVIGQ PLAWDFVQSN WKKLFQDYGG GSFSFSNLIQ 

       910        920        930        940        950        960 
GVTRRFSSEF ELQQLEQFKK NNMDVGFGSG TRALEQALEK TKANIKWVKE NKEVVLNWFI 


EHS 

« Hide

References

« Hide 'large scale' references
[1]"Determinants essential for the transmissible gastroenteritis virus-receptor interaction reside within a domain of aminopeptidase-N that is distinct from the enzymatic site."
Delmas B., Gelfi J., Kut E., Sjoestroem H., Noren O., Laude H.
J. Virol. 68:5216-5224(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION OF RECEPTOR FUNCTIONAL DOMAINS FOR TGEV INFECTION.
[2]"Cloning of the pig aminopeptidase N gene. Identification of possible regulatory elements and the exon distribution in relation to the membrane-spanning region."
Olsen J., Sjoestroem H., Noren O.
FEBS Lett. 251:275-281(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-294.
[3]"Identification and characterization of the major stilbene-disulphonate- and concanavalin A-binding protein of the porcine renal brush-border membrane as aminopeptidase N."
See H., Reithmeier R.A.F.
Biochem. J. 271:147-155(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-40.
[4]"Evaluation and characterization of a porcine small intestine cDNA library: analysis of 839 clones."
Winteroe A.K., Fredholm M., Davies W.
Mamm. Genome 7:509-517(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-144.
Tissue: Small intestine.
[5]"Aminopeptidase N is a major receptor for the entero-pathogenic coronavirus TGEV."
Delmas B., Gelfi J., L'Haridon R., Vogel L.K., Sjostrom H., Noren O., Laude H.
Nature 357:417-420(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF TGEV RECEPTOR FUNCTION.
[6]"Further characterization of aminopeptidase-N as a receptor for coronaviruses."
Delmas B., Gelfi J., Sjostrom H., Noren O., Laude H.
Adv. Exp. Med. Biol. 342:293-298(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF PRCOV RECEPTOR FUNCTION.
[7]"Purification and characterization of aminopeptidase M from muscle and mucosa of the pig intestine."
Terashima H., Bunnett N.W.
J. Gastroenterol. 30:696-704(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[8]"Interspecies aminopeptidase-N chimeras reveal species-specific receptor recognition by canine coronavirus, feline infectious peritonitis virus, and transmissible gastroenteritis virus."
Benbacer L., Kut E., Besnardeau L., Laude H., Delmas B.
J. Virol. 71:734-737(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION OF RECEPTOR FUNCTIONAL DOMAINS FOR TGEV INFECTION.
[9]"Characterization of determinants involved in the feline infectious peritonitis virus receptor function of feline aminopeptidase N."
Hegyi A., Kolb A.F.
J. Gen. Virol. 79:1387-1391(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION OF RECEPTOR FUNCTIONAL DOMAINS FOR TGEV INFECTION.
[10]"Subunit structured of pig small-intestinal brush-border aminopeptidase N."
Benajiba A., Maroux S.
Biochem. J. 197:573-580(1981) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT.
[11]"Tyrosine sulfation, a post-translational modification of microvillar enzymes in the small intestinal enterocyte."
Danielsen E.M.
EMBO J. 6:2891-2896(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: SULFATION.
[12]"Structural bases of coronavirus attachment to host aminopeptidase N and its inhibition by neutralizing antibodies."
Reguera J., Santiago C., Mudgal G., Ordono D., Enjuanes L., Casasnovas J.M.
PLoS Pathog. 8:E1002859-E1002859(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 36-963 IN COMPLEX WITH PORCINE RESPIRATORY CORONAVIRUS S PROTEIN, SUBUNIT, COFACTOR, ZINC-BINDING SITES, DISULFIDE BONDS, GLYCOSYLATION AT ASN-82; ASN-124; ASN-229; ASN-237; ASN-314; ASN-328; ASN-506; ASN-622; ASN-646 AND ASN-736.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z29522 mRNA. Translation: CAA82641.1.
X16088 Genomic DNA. Translation: CAA34216.1. Different termination.
F14846 mRNA. Translation: CAA23291.1.
PIRA53984.
RefSeqNP_999442.1. NM_214277.1.
UniGeneSsc.820.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4F5CX-ray3.20A/B36-963[»]
4FKEX-ray1.85A62-963[»]
4FKHX-ray2.05A62-963[»]
4FKKX-ray2.60A62-963[»]
4HOMX-ray1.90A63-963[»]
4NAQX-ray2.10A64-963[»]
4NZ8X-ray2.00A64-963[»]
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBP15145.
ChEMBLCHEMBL2590.

Protein family/group databases

MEROPSM01.001.

Proteomic databases

PaxDbP15145.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID397520.
KEGGssc:397520.

Organism-specific databases

CTD290.

Phylogenomic databases

eggNOGCOG0308.
HOGENOMHOG000106482.
HOVERGENHBG006616.
KOK11140.

Family and domain databases

InterProIPR024571. ERAP1-like_C_dom.
IPR001930. Peptidase_M1.
IPR014782. Peptidase_M1_N.
[Graphical view]
PANTHERPTHR11533. PTHR11533. 1 hit.
PfamPF11838. ERAP1_C. 1 hit.
PF01433. Peptidase_M1. 1 hit.
[Graphical view]
PRINTSPR00756. ALADIPTASE.
PROSITEPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PMAP-CutDBP15145.

Entry information

Entry nameAMPN_PIG
AccessionPrimary (citable) accession number: P15145
Secondary accession number(s): Q29242
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: February 6, 2013
Last modified: July 9, 2014
This is version 126 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references