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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

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

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 – 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.
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:
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.
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: October 29, 2014
This is version 128 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