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P15145

- AMPN_PIG

UniProt

P15145 - AMPN_PIG

Protein

Aminopeptidase N

Gene

ANPEP

Organism
Sus scrofa (Pig)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 127 (01 Oct 2014)
      Sequence version 4 (06 Feb 2013)
      Previous versions | rss
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    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. 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.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.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi383 – 3831Zinc; catalytic
    Active sitei384 – 3841Proton acceptorPROSITE-ProRule annotation
    Metal bindingi387 – 3871Zinc; catalytic
    Metal bindingi406 – 4061Zinc; catalytic
    Sitei472 – 4721Transition state stabilizerBy similarity

    GO - Molecular functioni

    1. aminopeptidase activity Source: UniProtKB-KW
    2. metallopeptidase activity Source: UniProtKB-KW
    3. virus receptor activity Source: UniProtKB-KW
    4. zinc ion binding Source: InterPro

    GO - Biological processi

    1. angiogenesis Source: UniProtKB-KW
    2. cell differentiation Source: UniProtKB-KW
    3. viral process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Aminopeptidase, Developmental protein, Host cell receptor for virus entry, Hydrolase, Metalloprotease, Protease, Receptor

    Keywords - Biological processi

    Angiogenesis, Differentiation, Host-virus interaction

    Keywords - Ligandi

    Metal-binding, Zinc

    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:
    pAPN
    Alternative name(s):
    Alanyl aminopeptidase
    Aminopeptidase M
    Short name:
    AP-M
    Microsomal aminopeptidase
    gp130
    CD_antigen: CD13
    Gene namesi
    Name:ANPEP
    OrganismiSus scrofa (Pig)
    Taxonomic identifieri9823 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
    ProteomesiUP000008227: Unplaced

    Subcellular locationi

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 963962Aminopeptidase NPRO_0000095083Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi82 – 821N-linked (GlcNAc...)1 Publication
    Glycosylationi124 – 1241N-linked (GlcNAc...)1 Publication
    Modified residuei171 – 1711SulfotyrosineSequence Analysis
    Glycosylationi229 – 2291N-linked (GlcNAc...)1 Publication
    Glycosylationi237 – 2371N-linked (GlcNAc...)1 Publication
    Glycosylationi258 – 2581N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi286 – 2861N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi314 – 3141N-linked (GlcNAc...)1 Publication
    Glycosylationi328 – 3281N-linked (GlcNAc...)1 Publication
    Glycosylationi506 – 5061N-linked (GlcNAc...)1 Publication
    Glycosylationi556 – 5561N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi569 – 5691N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi622 – 6221N-linked (GlcNAc...)1 Publication
    Glycosylationi646 – 6461N-linked (GlcNAc...)1 Publication
    Glycosylationi736 – 7361N-linked (GlcNAc...)1 Publication
    Disulfide bondi758 ↔ 7651 Publication
    Disulfide bondi795 ↔ 8311 Publication

    Post-translational modificationi

    Sulfated.1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Sulfation

    Proteomic databases

    PaxDbiP15145.

    Miscellaneous databases

    PMAP-CutDBP15145.

    Interactioni

    Subunit structurei

    Homodimer. Interacts with TGEV and PRCoV spike glycoprotein.2 Publications

    Structurei

    Secondary structure

    1
    963
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi66 – 683
    Beta strandi69 – 713
    Beta strandi74 – 8714
    Beta strandi93 – 953
    Beta strandi98 – 11114
    Beta strandi113 – 1197
    Beta strandi122 – 1254
    Beta strandi128 – 1314
    Beta strandi133 – 1375
    Beta strandi145 – 1517
    Turni152 – 1554
    Beta strandi156 – 16510
    Beta strandi170 – 18011
    Beta strandi183 – 19513
    Beta strandi198 – 2069
    Turni208 – 2114
    Helixi212 – 2143
    Beta strandi221 – 2244
    Beta strandi226 – 23510
    Beta strandi238 – 2447
    Beta strandi246 – 2494
    Beta strandi254 – 2563
    Beta strandi259 – 2646
    Helixi272 – 2743
    Beta strandi277 – 2815
    Beta strandi283 – 2886
    Beta strandi294 – 2996
    Helixi301 – 3055
    Turni306 – 3094
    Helixi310 – 32617
    Beta strandi332 – 34110
    Beta strandi345 – 3495
    Beta strandi354 – 3585
    Helixi359 – 3624
    Turni366 – 3683
    Helixi371 – 38616
    Turni387 – 3893
    Turni391 – 3933
    Beta strandi394 – 3985
    Helixi399 – 4013
    Helixi402 – 42019
    Helixi426 – 4294
    Helixi430 – 4334
    Helixi435 – 4428
    Helixi454 – 4563
    Helixi460 – 4645
    Helixi469 – 48618
    Helixi488 – 50215
    Beta strandi505 – 5073
    Helixi509 – 52113
    Beta strandi524 – 5263
    Helixi532 – 5409
    Beta strandi546 – 5505
    Turni552 – 5543
    Beta strandi556 – 5616
    Beta strandi564 – 5674
    Turni575 – 5784
    Beta strandi582 – 5843
    Beta strandi586 – 5883
    Beta strandi596 – 5983
    Beta strandi602 – 6054
    Helixi607 – 6093
    Beta strandi617 – 6204
    Helixi621 – 6233
    Beta strandi628 – 6314
    Helixi633 – 64513
    Helixi647 – 6493
    Helixi652 – 66716
    Helixi673 – 6786
    Helixi679 – 6857
    Helixi689 – 70618
    Helixi712 – 73322
    Turni734 – 7385
    Helixi744 – 75916
    Helixi763 – 77715
    Turni787 – 7893
    Helixi790 – 80011
    Helixi803 – 81513
    Helixi819 – 82911
    Helixi835 – 84410
    Turni848 – 8503
    Helixi853 – 8553
    Helixi856 – 86510
    Helixi869 – 88012
    Turni882 – 8865
    Beta strandi887 – 8904
    Helixi895 – 9039
    Helixi909 – 91911
    Helixi920 – 9223
    Beta strandi923 – 9253
    Helixi928 – 9303
    Helixi933 – 96230

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini2 – 87Cytoplasmic
    Topological domaini33 – 963931ExtracellularAdd
    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 – 6432Cytosolic Ser/Thr-rich junctionAdd
    BLAST
    Regioni65 – 963899MetalloproteaseAdd
    BLAST
    Regioni347 – 3515Substrate bindingBy similarity
    Regioni717 – 81397Interaction with TGEV spike glycoproteinAdd
    BLAST

    Sequence similaritiesi

    Belongs to the peptidase M1 family.Curated

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0308.
    HOGENOMiHOG000106482.
    HOVERGENiHBG006616.
    KOiK11140.

    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.

    P15145-1 [UniParc]FASTAAdd to Basket

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    MAKGFYISKA LGILGILLGV AAVATIIALS VVYAQEKNKN AEHVPQAPTS    50
    PTITTTAAIT LDQSKPWNRY RLPTTLLPDS YNVTLRPYLT PNADGLYIFK 100
    GKSIVRLLCQ EPTDVIIIHS KKLNYTTQGH MVVLRGVGDS QVPEIDRTEL 150
    VELTEYLVVH LKGSLQPGHM YEMESEFQGE LADDLAGFYR SEYMEGNVKK 200
    VLATTQMQST DARKSFPCFD EPAMKATFNI TLIHPNNLTA LSNMPPKGSS 250
    TPLAEDPNWS VTEFETTPVM STYLLAYIVS EFQSVNETAQ NGVLIRIWAR 300
    PNAIAEGHGM YALNVTGPIL NFFANHYNTS YPLPKSDQIA LPDFNAGAME 350
    NWGLVTYREN ALLFDPQSSS ISNKERVVTV IAHELAHQWF GNLVTLAWWN 400
    DLWLNEGFAS YVEYLGADHA EPTWNLKDLI VPGDVYRVMA VDALASSHPL 450
    TTPAEEVNTP AQISEMFDSI SYSKGASVIR MLSNFLTEDL FKEGLASYLH 500
    AFAYQNTTYL DLWEHLQKAV DAQTSIRLPD TVRAIMDRWT LQMGFPVITV 550
    DTKTGNISQK HFLLDSESNV TRSSAFDYLW IVPISSIKNG VMQDHYWLRD 600
    VSQAQNDLFK TASDDWVLLN VNVTGYFQVN YDEDNWRMIQ HQLQTNLSVI 650
    PVINRAQVIY DSFNLATAHM VPVTLALDNT LFLNGEKEYM PWQAALSSLS 700
    YFSLMFDRSE VYGPMKKYLR KQVEPLFQHF ETLTKNWTER PENLMDQYSE 750
    INAISTACSN GLPQCENLAK TLFDQWMSDP ENNPIHPNLR STIYCNAIAQ 800
    GGQDQWDFAW GQLQQAQLVN EADKLRSALA CSNEVWLLNR YLGYTLNPDL 850
    IRKQDATSTI NSIASNVIGQ PLAWDFVQSN WKKLFQDYGG GSFSFSNLIQ 900
    GVTRRFSSEF ELQQLEQFKK NNMDVGFGSG TRALEQALEK TKANIKWVKE 950
    NKEVVLNWFI EHS 963
    Length:963
    Mass (Da):108,832
    Last modified:February 6, 2013 - v4
    Checksum:i0C55FDD2CE1F3E10
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti82 – 821N → F in CAA82641. (PubMed:7913510)Curated
    Sequence conflicti82 – 821N → F in CAA34216. (PubMed:2568950)Curated
    Sequence conflicti107 – 1082LL → FI in CAA23291. (PubMed:8672129)Curated
    Sequence conflicti111 – 1111E → G in CAA23291. (PubMed:8672129)Curated
    Sequence conflicti126 – 1261T → N in CAA23291. (PubMed:8672129)Curated
    Sequence conflicti140 – 1401S → F in CAA23291. (PubMed:8672129)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z29522 mRNA. Translation: CAA82641.1.
    X16088 Genomic DNA. Translation: CAA34216.1. Different termination.
    F14846 mRNA. Translation: CAA23291.1.
    PIRiA53984.
    RefSeqiNP_999442.1. NM_214277.1.
    UniGeneiSsc.820.

    Genome annotation databases

    GeneIDi397520.
    KEGGissc:397520.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z29522 mRNA. Translation: CAA82641.1 .
    X16088 Genomic DNA. Translation: CAA34216.1 . Different termination.
    F14846 mRNA. Translation: CAA23291.1 .
    PIRi A53984.
    RefSeqi NP_999442.1. NM_214277.1.
    UniGenei Ssc.820.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4F5C X-ray 3.20 A/B 36-963 [» ]
    4FKE X-ray 1.85 A 62-963 [» ]
    4FKH X-ray 2.05 A 62-963 [» ]
    4FKK X-ray 2.60 A 62-963 [» ]
    4HOM X-ray 1.90 A 63-963 [» ]
    4NAQ X-ray 2.10 A 64-963 [» ]
    4NZ8 X-ray 2.00 A 64-963 [» ]
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    BindingDBi P15145.
    ChEMBLi CHEMBL2590.

    Protein family/group databases

    MEROPSi M01.001.

    Proteomic databases

    PaxDbi P15145.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 397520.
    KEGGi ssc:397520.

    Organism-specific databases

    CTDi 290.

    Phylogenomic databases

    eggNOGi COG0308.
    HOGENOMi HOG000106482.
    HOVERGENi HBG006616.
    KOi K11140.

    Miscellaneous databases

    PMAP-CutDB P15145.

    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. "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.

    Entry informationi

    Entry nameiAMPN_PIG
    AccessioniPrimary (citable) accession number: P15145
    Secondary accession number(s): Q29242
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: February 6, 2013
    Last modified: October 1, 2014
    This is version 127 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3