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Protein

Aminopeptidase N

Gene

ANPEP

Organism
Felis catus (Cat) (Felis silvestris catus)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Broad specificity aminopeptidase which plays a role in the final digestion of peptides generated from hydrolysis of proteins by gastric and pancreatic proteases. Also involved in the processing of various peptides including peptide hormones, such as angiotensin III and IV, neuropeptides, and chemokines. May also be involved the cleavage of peptides bound to major histocompatibility complex class II molecules of antigen presenting cells. May have a role in angiogenesis and promote cholesterol crystallization.By similarity
(Microbial infection) 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.3 Publications

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.By similarity

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi387Zinc; catalyticPROSITE-ProRule annotation1
Active sitei388Proton acceptorPROSITE-ProRule annotation1
Metal bindingi391Zinc; catalyticPROSITE-ProRule annotation1
Metal bindingi410Zinc; catalyticPROSITE-ProRule annotation1
Sitei476Transition state stabilizerBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionAminopeptidase, Developmental protein, Host cell receptor for virus entry, Hydrolase, Metalloprotease, Protease, Receptor
Biological processAngiogenesis, Differentiation, Host-virus interaction
LigandMetal-binding, Zinc

Protein family/group databases

MEROPSiM01.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Aminopeptidase NCurated (EC:3.4.11.2By similarity)
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
Proteomesi
  • UP000011712 Componenti: Unplaced

Subcellular locationi

  • Cell membrane 2 Publications; Single-pass type II membrane protein 2 Publications

  • Note: Also found as a soluble form.By similarity

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini2 – 8Cytoplasmic1 Publication7
Transmembranei9 – 32Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST24
Topological domaini33 – 967Extracellular2 PublicationsAdd BLAST935

GO - Cellular componenti

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000950802 – 967Aminopeptidase NAdd BLAST966

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi38N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi84N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi126N-linked (GlcNAc...) asparagineSequence analysis1
Modified residuei175SulfotyrosineSequence analysis1
Glycosylationi233N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi338N-linked (GlcNAc...) asparagineSequence analysis1
Modified residuei418SulfotyrosineSequence analysis1
Glycosylationi626N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi682N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi740N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi762 ↔ 769By similarity
Disulfide bondi799 ↔ 835By similarity

Post-translational modificationi

Sulfated.By similarity
N- and O-glycosylated.By similarity
May undergo proteolysis and give rise to a soluble form.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Sulfation

Proteomic databases

PRIDEiP79171.

Interactioni

Subunit structurei

Homodimer.By similarity
(Microbial infection) Interacts with FCoV, CCoV, TGEV and HCoV-229E spike glycoprotein.2 Publications

Protein-protein interaction databases

STRINGi9685.ENSFCAP00000008319.

Structurei

3D structure databases

ProteinModelPortaliP79171.
SMRiP79171.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni33 – 66Cytosolic Ser/Thr-rich junctionAdd BLAST34
Regioni67 – 967MetalloproteaseAdd BLAST901
Regioni351 – 355Substrate bindingBy similarity5
Regioni670 – 840Interaction with FCoV and TGEV spike glycoprotein2 PublicationsAdd BLAST171

Sequence similaritiesi

Belongs to the peptidase M1 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1046. Eukaryota.
COG0308. LUCA.
HOVERGENiHBG006616.
InParanoidiP79171.
KOiK11140.

Family and domain databases

CDDicd09601. M1_APN_2. 1 hit.
InterProiView protein in InterPro
IPR024571. ERAP1-like_C_dom.
IPR034016. M1_APN-typ.
IPR001930. Peptidase_M1.
IPR014782. Peptidase_M1_N.
PANTHERiPTHR11533. PTHR11533. 1 hit.
PfamiView protein in Pfam
PF11838. ERAP1_C. 1 hit.
PF01433. Peptidase_M1. 1 hit.
PRINTSiPR00756. ALADIPTASE.
PROSITEiView protein in PROSITE
PS00142. ZINC_PROTEASE. 1 hit.

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)DescriptionActionsGraphical viewLength
Sequence conflicti105N → S in AAD09272 (PubMed:9782265).Curated1
Sequence conflicti144H → Q in AAD09272 (PubMed:9782265).Curated1
Sequence conflicti178N → K in AAD09272 (PubMed:9782265).Curated1
Sequence conflicti215E → D in AAD09272 (PubMed:9782265).Curated1
Sequence conflicti236I → T in AAD09272 (PubMed:9782265).Curated1
Sequence conflicti258Missing in AAD09272 (PubMed:9782265).Curated1
Sequence conflicti581N → K in AAD09272 (PubMed:9782265).Curated1
Sequence conflicti593S → N in AAD09272 (PubMed:9782265).Curated1
Sequence conflicti623L → V in AAD09272 (PubMed:9782265).Curated1
Sequence conflicti730L → S in AAD09272 (PubMed:9782265).Curated1
Sequence conflicti735 – 737ERV → RKS in AAD09272 (PubMed:9782265).Curated3
Sequence conflicti747T → A in AAD09272 (PubMed:9782265).Curated1
Sequence conflicti829L → F in AAD09272 (PubMed:9782265).Curated1
Sequence conflicti949L → I in AAD09272 (PubMed:9782265).Curated1
Sequence conflicti967S → SK in AAD09272 (PubMed:9782265).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
U58920 mRNA. Translation: AAC48686.1.
U96104 mRNA. Translation: AAD09272.1.
RefSeqiNP_001009252.2. NM_001009252.2.

3D structure databases

ProteinModelPortaliP79171.
SMRiP79171.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9685.ENSFCAP00000008319.

Protein family/group databases

MEROPSiM01.001.

Proteomic databases

PRIDEiP79171.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi493785.
KEGGifca:493785.

Organism-specific databases

CTDi290.

Phylogenomic databases

eggNOGiKOG1046. Eukaryota.
COG0308. LUCA.
HOVERGENiHBG006616.
InParanoidiP79171.
KOiK11140.

Family and domain databases

CDDicd09601. M1_APN_2. 1 hit.
InterProiView protein in InterPro
IPR024571. ERAP1-like_C_dom.
IPR034016. M1_APN-typ.
IPR001930. Peptidase_M1.
IPR014782. Peptidase_M1_N.
PANTHERiPTHR11533. PTHR11533. 1 hit.
PfamiView protein in Pfam
PF11838. ERAP1_C. 1 hit.
PF01433. Peptidase_M1. 1 hit.
PRINTSiPR00756. ALADIPTASE.
PROSITEiView protein in PROSITE
PS00142. ZINC_PROTEASE. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiAMPN_FELCA
AccessioniPrimary (citable) accession number: P79171
Secondary accession number(s): O97783
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 23, 2007
Last modified: May 10, 2017
This is version 120 of the entry and version 3 of the sequence. See 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.