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P79171

- AMPN_FELCA

UniProt

P79171 - AMPN_FELCA

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Protein

Aminopeptidase N

Gene

ANPEP

Organism
Felis catus (Cat) (Felis silvestris catus)
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). In case of feline coronavirus (FCoV) infection, serves as a receptor for FCoV spike glycoprotein. It is as well a receptor for other serogroup I coronaviruses, like canine coronavirus (CCoV), porcine transmissible gastroenteritis virus (TGEV), and human coronavirus 229E (HCoV-229E). Also serves as a receptor for infectious bronchitis virus (IBV, Arkansas 99 serotype) in serogroup III.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.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi387 – 3871Zinc; catalyticPROSITE-ProRule annotation
Active sitei388 – 3881Proton acceptorPROSITE-ProRule annotation
Metal bindingi391 – 3911Zinc; catalyticPROSITE-ProRule annotation
Metal bindingi410 – 4101Zinc; catalyticPROSITE-ProRule annotation
Sitei476 – 4761Transition 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:
fAPN
Alternative name(s):
Alanyl aminopeptidase
Aminopeptidase M
Short name:
AP-M
Microsomal aminopeptidase
CD_antigen: CD13
Gene namesi
Name:ANPEP
Synonyms:APN
OrganismiFelis catus (Cat) (Felis silvestris catus)
Taxonomic identifieri9685 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraFeliformiaFelidaeFelinaeFelis
ProteomesiUP000011712: 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 – 11RemovedBy similarity
Chaini2 – 967966Aminopeptidase NPRO_0000095080Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi38 – 381N-linked (GlcNAc...)Sequence Analysis
Glycosylationi84 – 841N-linked (GlcNAc...)Sequence Analysis
Glycosylationi126 – 1261N-linked (GlcNAc...)Sequence Analysis
Modified residuei175 – 1751SulfotyrosineSequence Analysis
Glycosylationi233 – 2331N-linked (GlcNAc...)Sequence Analysis
Glycosylationi338 – 3381N-linked (GlcNAc...)Sequence Analysis
Modified residuei418 – 4181SulfotyrosineSequence Analysis
Glycosylationi626 – 6261N-linked (GlcNAc...)Sequence Analysis
Glycosylationi682 – 6821N-linked (GlcNAc...)Sequence Analysis
Glycosylationi740 – 7401N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi762 ↔ 769By similarity
Disulfide bondi799 ↔ 835By similarity

Post-translational modificationi

Sulfated.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Sulfation

Interactioni

Subunit structurei

Homodimer (By similarity). Interacts with FCoV, CCoV, TGEV and HCoV-229E spike glycoprotein.By similarity1 Publication

Structurei

3D structure databases

ProteinModelPortaliP79171.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 87Cytoplasmic
Topological domaini33 – 967935ExtracellularAdd
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 – 6634Cytosolic Ser/Thr-rich junctionAdd
BLAST
Regioni67 – 967901MetalloproteaseAdd
BLAST
Regioni351 – 3555Substrate bindingBy similarity
Regioni670 – 840171Interaction with FCoV and TGEV spike glycoproteinAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase M1 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0308.
HOVERGENiHBG006616.
InParanoidiP79171.
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.

P79171-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAKGFYISKP VGILAILLGV AAVCTIIALS VVYSQEKNRS TESSTAASTA
60 70 80 90 100
APTGPTTTVA TTLDQSKPWN VYRLPKTLIP DSYNVTLRPY LTPNNKGLYV
110 120 130 140 150
FTGTNIVRFT CKESTNIVII HSKRLNYTSH QGHMVALSGV GGFHPQPVIV
160 170 180 190 200
RTELVELTEY LVVHLQEPLV AGRQYEMNSE FQGELADDLA GFYRSEYMEN
210 220 230 240 250
GVKKVLATTH MQATEARKSF PCFDEPAMKA TFNITIIHPN NLVALSNMLP
260 270 280 290 300
RGPSVPFGED PTWKVTEFET TPIMSTYLLA YIVSEFSYVE TRAPSGVLIR
310 320 330 340 350
IWARPSAINQ GHGDYALKVT GPILDFFSQH YDTPYPLNKS DQIALPDFNA
360 370 380 390 400
GAMENWGLVT YRESALLYDR QSSSSGNQER VVTVIAHELA HQWFGNLVTL
410 420 430 440 450
EWWNDLWLNE GFASYVEYLG ADFAEPTWNL KDLMVLNDVY RVMAVDALAS
460 470 480 490 500
SHPLSTPASE INTPAQISEV FDSISYSKGA SVLRMLSNFL TEDLFKMGIA
510 520 530 540 550
SYLHTYKYGN TIYLNLWEHL QQVVDKQPTI KLPDTVSAIM DRWILQMGFP
560 570 580 590 600
VITVDTQTGT ISQQHFLLDP QSVVTRPSQF NYLWIVPISS VRSGSPQAHY
610 620 630 640 650
WLPGVEKAQN DLFKTTANDW VLLNLNVTGY YLVNYDNENW KKIQTQLQTD
660 670 680 690 700
LSVIPVINRA QVIHDAFNLA SAQKVPVTLA LNNTLFLIQE TEYMPWQAAL
710 720 730 740 750
SSLSYFKLMF DRSEVYGPMK RYLKKQVTPL FNHFERVTKN WTDHPQTLMD
760 770 780 790 800
QYSEINAVST ACSYGVPECE KLAATLFAQW KKNPQNNPIH PNLRSTVYCN
810 820 830 840 850
AIAQGGEEEW NFVWEQFLKA ELVNEADKLR GALACSNQVW ILNRFLSYTL
860 870 880 890 900
DPNLIRKQDV TSTLSSISSN VVGQTLVWDF VQSNWKKLFQ DYGTGSFSFS
910 920 930 940 950
NLIQAVTRRF STEFELQQLE QFKKNNMDTG FGSATRALEQ ALEKTKANLK
960
WVKENKDVVL RWFTENS
Length:967
Mass (Da):109,424
Last modified:January 23, 2007 - v3
Checksum:i119BDAA34F5B5E89
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti105 – 1051N → S in AAD09272. (PubMed:9782265)Curated
Sequence conflicti144 – 1441H → Q in AAD09272. (PubMed:9782265)Curated
Sequence conflicti178 – 1781N → K in AAD09272. (PubMed:9782265)Curated
Sequence conflicti215 – 2151E → D in AAD09272. (PubMed:9782265)Curated
Sequence conflicti236 – 2361I → T in AAD09272. (PubMed:9782265)Curated
Sequence conflicti258 – 2581Missing in AAD09272. (PubMed:9782265)Curated
Sequence conflicti581 – 5811N → K in AAD09272. (PubMed:9782265)Curated
Sequence conflicti593 – 5931S → N in AAD09272. (PubMed:9782265)Curated
Sequence conflicti623 – 6231L → V in AAD09272. (PubMed:9782265)Curated
Sequence conflicti730 – 7301L → S in AAD09272. (PubMed:9782265)Curated
Sequence conflicti735 – 7373ERV → RKS in AAD09272. (PubMed:9782265)Curated
Sequence conflicti747 – 7471T → A in AAD09272. (PubMed:9782265)Curated
Sequence conflicti829 – 8291L → F in AAD09272. (PubMed:9782265)Curated
Sequence conflicti949 – 9491L → I in AAD09272. (PubMed:9782265)Curated
Sequence conflicti967 – 9671S → SK in AAD09272. (PubMed:9782265)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U58920 mRNA. Translation: AAC48686.1.
U96104 mRNA. Translation: AAD09272.1.
RefSeqiNP_001009252.2. NM_001009252.2.

Genome annotation databases

GeneIDi493785.
KEGGifca:493785.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U58920 mRNA. Translation: AAC48686.1 .
U96104 mRNA. Translation: AAD09272.1 .
RefSeqi NP_001009252.2. NM_001009252.2.

3D structure databases

ProteinModelPortali P79171.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi M01.001.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 493785.
KEGGi fca:493785.

Organism-specific databases

CTDi 290.

Phylogenomic databases

eggNOGi COG0308.
HOVERGENi HBG006616.
InParanoidi P79171.
KOi K11140.

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. "Feline aminopeptidase N serves as a receptor for feline, canine, porcine, and human coronaviruses in serogroup I."
    Tresnan D.B., Levis R., Holmes K.V.
    J. Virol. 70:8669-8674(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH FCOV SPIKE GLYCOPROTEIN, CHARACTERIZATION OF CORONAVIRUS RECEPTOR FUNCTION.
  2. "Molecular analysis of the coronavirus-receptor function of aminopeptidase N."
    Kolb A.F., Hegyi A., Maile J., Heister A., Hagemann M., Siddell S.G.
    Adv. Exp. Med. Biol. 440:61-67(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION OF RECEPTOR FUNCTIONAL DOMAINS FOR FIPV INFECTION.
  3. "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 FIPV; TGEV AND HCV-229E INFECTION.
  4. "The role of feline aminopeptidase N as a receptor for infectious bronchitis virus."
    Miguel B., Pharr G.T., Wang C.
    Arch. Virol. 147:2047-2056(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF IBV RECEPTOR FUNCTION.

Entry informationi

Entry nameiAMPN_FELCA
AccessioniPrimary (citable) accession number: P79171
Secondary accession number(s): O97783
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 109 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3