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UniProtKB/Swiss-Prot entry P15145


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name AMPN_PIG
Primary accession number P15145
Secondary accession number Q29242
Integrated into Swiss-Prot on April 1, 1990
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    September 2, 2008 (Entry version 81)
Name and origin of the protein
Protein name Aminopeptidase N
Synonyms EC 3.4.11.2
pAPN
Alanyl aminopeptidase
Microsomal aminopeptidase
Aminopeptidase M
gp130
CD13 antigen
Gene name
Name: ANPEP
From
Sus scrofa (Pig) [TaxID: 9823] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae; Sus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND IDENTIFICATION OF RECEPTOR FUNCTIONAL DOMAINS FOR TGEV INFECTION.
PubMed=7913510 [NCBI, ExPASy, EBI, Israel, Japan]
Delmas B., Gelfi J., Kut E., Sjoestroem H., Noren O., Laude H.;
"Determinants essential for the transmissible gastroenteritis virus-receptor interaction reside within a domain of aminopeptidase-N that is distinct from the enzymatic site.";
J. Virol. 68:5216-5224(1994).
[2]
NUCLEOTIDE SEQUENCE OF 1-294.
DOI=10.1016/0014-5793(89)81470-X; PubMed=2568950 [NCBI, ExPASy, EBI, Israel, Japan]
Olsen J., Sjoestroem H., Noren O.;
"Cloning of the pig aminopeptidase N gene. Identification of possible regulatory elements and the exon distribution in relation to the membrane-spanning region.";
FEBS Lett. 251:275-281(1989).
[3]
PROTEIN SEQUENCE OF 2-40.
PubMed=1977382 [NCBI, ExPASy, EBI, Israel, Japan]
See H., Reithmeier R.A.F.;
"Identification and characterization of the major stilbene-disulphonate- and concanavalin A-binding protein of the porcine renal brush-border membrane as aminopeptidase N.";
Biochem. J. 271:147-155(1990).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-144.
TISSUE=Small intestine;
DOI=10.1007/s003359900153; PubMed=8672129 [NCBI, ExPASy, EBI, Israel, Japan]
Winteroe A.K., Fredholm M., Davies W.;
"Evaluation and characterization of a porcine small intestine cDNA library: analysis of 839 clones.";
Mamm. Genome 7:509-517(1996).
[5]
CHARACTERIZATION OF TGEV RECEPTOR FUNCTION.
DOI=10.1038/357417a0; PubMed=1350661 [NCBI, ExPASy, EBI, Israel, Japan]
Delmas B., Gelfi J., L'Haridon R., Vogel L.K., Sjostrom H., Noren O., Laude H.;
"Aminopeptidase N is a major receptor for the entero-pathogenic coronavirus TGEV.";
Nature 357:417-420(1992).
[6]
CHARACTERIZATION OF PRCOV RECEPTOR FUNCTION.
PubMed=7911642 [NCBI, ExPASy, EBI, Israel, Japan]
Delmas B., Gelfi J., Sjostrom H., Noren O., Laude H.;
"Further characterization of aminopeptidase-N as a receptor for coronaviruses.";
Adv. Exp. Med. Biol. 342:293-298(1993).
[7]
CHARACTERIZATION.
DOI=10.1007/BF02349634; PubMed=8963385 [NCBI, ExPASy, EBI, Israel, Japan]
Terashima H., Bunnett N.W.;
"Purification and characterization of aminopeptidase M from muscle and mucosa of the pig intestine.";
J. Gastroenterol. 30:696-704(1995).
[8]
IDENTIFICATION OF RECEPTOR FUNCTIONAL DOMAINS FOR TGEV INFECTION.
PubMed=8985407 [NCBI, ExPASy, EBI, Israel, Japan]
Benbacer L., Kut E., Besnardeau L., Laude H., Delmas B.;
"Interspecies aminopeptidase-N chimeras reveal species-specific receptor recognition by canine coronavirus, feline infectious peritonitis virus, and transmissible gastroenteritis virus.";
J. Virol. 71:734-737(1997).
[9]
IDENTIFICATION OF RECEPTOR FUNCTIONAL DOMAINS FOR TGEV INFECTION.
PubMed=9634079 [NCBI, ExPASy, EBI, Israel, Japan]
Hegyi A., Kolb A.F.;
"Characterization of determinants involved in the feline infectious peritonitis virus receptor function of feline aminopeptidase N.";
J. Gen. Virol. 79:1387-1391(1998).
[10]
SUBUNIT.
PubMed=6119979 [NCBI, ExPASy, EBI, Israel, Japan]
Benajiba A., Maroux S.;
"Subunit structured of pig small-intestinal brush-border aminopeptidase N.";
Biochem. J. 197:573-580(1981).
[11]
SULFATION.
PubMed=3121301 [NCBI, ExPASy, EBI, Israel, Japan]
Danielsen E.M.;
"Tyrosine sulfation, a post-translational modification of microvillar enzymes in the small intestinal enterocyte.";
EMBO J. 6:2891-2896(1987).
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 and in 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.
  • 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 (By similarity).
  • SUBUNIT: Homodimer. Interacts with TGEV and PRCoV spike glycoprotein.
  • SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein.
  • PTM: Sulfated.
  • SIMILARITY: Belongs to the peptidase M1 family [view classification].
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
Z29522; CAA82641.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X16088; CAA34216.1; ALT_TERM; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
F14846; CAA23291.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A53984; A53984.
RefSeq NP_999442.1; -.
UniGene Ssc.820
3D structure databases
ModBase P15145.
Protein family/group databases
MEROPS M01.001; -.
Family and domain databases
InterPro IPR006025; Pept_M_Zn_BS.
IPR001930; Peptidase_M1.
IPR014782; Peptidase_M1_N.
Graphical view of domain structure.
PANTHER PTHR11533; Peptidase_M1; 1.
Pfam PF01433; Peptidase_M1; 1.
Pfam graphical view of domain structure.
PRINTS PR00756; ALADIPTASE.
PROSITE PS00142; ZINC_PROTEASE; 1.
BLOCKS P15145.
Genome annotation databases
GeneID 397520; -.
KEGG ssc:397520; -.
Phylogenomic databases
HOVERGEN P15145; -.
Other
ProtoNet P15145.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Aminopeptidase; Angiogenesis; Developmental protein; Differentiation; Direct protein sequencing; Glycoprotein; Host-virus interaction; Hydrolase; Membrane; Metal-binding; Metalloprotease; Protease; Signal-anchor; Sulfation; Transmembrane; Zinc.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   963  962     Aminopeptidase N. PRO_0000095083
TOPO_DOM   2     8  7     Cytoplasmic. 
TRANSMEM   9    32  24     Signal-anchor for type II membrane protein (Potential). 
REGION   33    64  32     Cytosolic Ser/Thr-rich junction. 
REGION   65   963  899     Metalloprotease. 
REGION   717   813  97     Interaction with TGEV spike glycoprotein. 
ACT_SITE   384   384        By similarity. 
ACT_SITE   472   472        Proton donor (Potential). 
METAL   383   383        Zinc; catalytic (By similarity). 
METAL   387   387        Zinc; catalytic (By similarity). 
METAL   406   406        Zinc; catalytic (By similarity). 
MOD_RES   171   171        Sulfotyrosine (Potential). 
CARBOHYD   124   124        N-linked (GlcNAc...) (Potential). 
CARBOHYD   229   229        N-linked (GlcNAc...) (Potential). 
CARBOHYD   237   237        N-linked (GlcNAc...) (Potential). 
CARBOHYD   258   258        N-linked (GlcNAc...) (Potential). 
CARBOHYD   286   286        N-linked (GlcNAc...) (Potential). 
CARBOHYD   314   314        N-linked (GlcNAc...) (Potential). 
CARBOHYD   328   328        N-linked (GlcNAc...) (Potential). 
CARBOHYD   506   506        N-linked (GlcNAc...) (Potential). 
CARBOHYD   556   556        N-linked (GlcNAc...) (Potential). 
CARBOHYD   569   569        N-linked (GlcNAc...) (Potential). 
CARBOHYD   622   622        N-linked (GlcNAc...) (Potential). 
CARBOHYD   646   646        N-linked (GlcNAc...) (Potential). 
CARBOHYD   736   736        N-linked (GlcNAc...) (Potential). 
CONFLICT   82    82        F -> N (in Ref. 4; CAA23291). 
CONFLICT   107   108        LL -> FI (in Ref. 4; CAA23291). 
CONFLICT   111   111        E -> G (in Ref. 4; CAA23291). 
CONFLICT   126   126        T -> N (in Ref. 4; CAA23291). 
CONFLICT   140   140        S -> F (in Ref. 4; CAA23291). 
Sequence information
Length: 963 AA [This is the length of the unprocessed precursor] Molecular weight: 108865 Da [This is the MW of the unprocessed precursor] CRC64: 45751498F84CE899 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAKGFYISKA LGILGILLGV AAVATIIALS VVYAQEKNKN AEHVPQAPTS PTITTTAAIT 

        70         80         90        100        110        120 
LDQSKPWNRY RLPTTLLPDS YFVTLRPYLT 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 

P15145 in FASTA format

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