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P15145

- AMPN_PIG

UniProt

P15145 - AMPN_PIG

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Protein

Aminopeptidase N

Gene

ANPEP

Organism
Sus scrofa (Pig)
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). 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

Zn2+1 PublicationNote: 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
Complete GO annotation...

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 87Cytoplasmic
Transmembranei9 – 3224Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini33 – 963931ExtracellularAdd
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

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.
InParanoidiP15145.
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

« Hide

        10         20         30         40         50
MAKGFYISKA LGILGILLGV AAVATIIALS VVYAQEKNKN AEHVPQAPTS
60 70 80 90 100
PTITTTAAIT LDQSKPWNRY RLPTTLLPDS YNVTLRPYLT PNADGLYIFK
110 120 130 140 150
GKSIVRLLCQ EPTDVIIIHS KKLNYTTQGH MVVLRGVGDS QVPEIDRTEL
160 170 180 190 200
VELTEYLVVH LKGSLQPGHM YEMESEFQGE LADDLAGFYR SEYMEGNVKK
210 220 230 240 250
VLATTQMQST DARKSFPCFD EPAMKATFNI TLIHPNNLTA LSNMPPKGSS
260 270 280 290 300
TPLAEDPNWS VTEFETTPVM STYLLAYIVS EFQSVNETAQ NGVLIRIWAR
310 320 330 340 350
PNAIAEGHGM YALNVTGPIL NFFANHYNTS YPLPKSDQIA LPDFNAGAME
360 370 380 390 400
NWGLVTYREN ALLFDPQSSS ISNKERVVTV IAHELAHQWF GNLVTLAWWN
410 420 430 440 450
DLWLNEGFAS YVEYLGADHA EPTWNLKDLI VPGDVYRVMA VDALASSHPL
460 470 480 490 500
TTPAEEVNTP AQISEMFDSI SYSKGASVIR MLSNFLTEDL FKEGLASYLH
510 520 530 540 550
AFAYQNTTYL DLWEHLQKAV DAQTSIRLPD TVRAIMDRWT LQMGFPVITV
560 570 580 590 600
DTKTGNISQK HFLLDSESNV TRSSAFDYLW IVPISSIKNG VMQDHYWLRD
610 620 630 640 650
VSQAQNDLFK TASDDWVLLN VNVTGYFQVN YDEDNWRMIQ HQLQTNLSVI
660 670 680 690 700
PVINRAQVIY DSFNLATAHM VPVTLALDNT LFLNGEKEYM PWQAALSSLS
710 720 730 740 750
YFSLMFDRSE VYGPMKKYLR KQVEPLFQHF ETLTKNWTER PENLMDQYSE
760 770 780 790 800
INAISTACSN GLPQCENLAK TLFDQWMSDP ENNPIHPNLR STIYCNAIAQ
810 820 830 840 850
GGQDQWDFAW GQLQQAQLVN EADKLRSALA CSNEVWLLNR YLGYTLNPDL
860 870 880 890 900
IRKQDATSTI NSIASNVIGQ PLAWDFVQSN WKKLFQDYGG GSFSFSNLIQ
910 920 930 940 950
GVTRRFSSEF ELQQLEQFKK NNMDVGFGSG TRALEQALEK TKANIKWVKE
960
NKEVVLNWFI EHS
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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.
InParanoidi P15145.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 129 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