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Entry version 130 (11 Dec 2019)
Sequence version 3 (23 Jan 2007)
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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

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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. May have a role in amino acid transport by acting as binding partner of amino acid transporter SLC6A19 and regulating its activity (By similarity).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

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>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 EC:3.4.11.2

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi387Zinc; catalyticPROSITE-ProRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei388Proton acceptorPROSITE-ProRule annotation1
Metal bindingi391Zinc; catalyticPROSITE-ProRule annotation1
Metal bindingi410Zinc; catalyticPROSITE-ProRule annotation1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei476Transition state stabilizerBy similarity1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>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

MEROPS protease database

More...
MEROPSi
M01.001

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:ANPEP
Synonyms:APN
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiFelis catus (Cat) (Felis silvestris catus)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9685 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraFeliformiaFelidaeFelinaeFelis
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000011712 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Unplaced

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 8Cytoplasmic1 Publication8
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei9 – 32Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST24
Topological domaini33 – 967Extracellular2 PublicationsAdd BLAST935

Keywords - Cellular componenti

Cell membrane, Membrane

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000950801 – 967Aminopeptidase NAdd BLAST967

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi38N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi84N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi126N-linked (GlcNAc...) asparagineSequence analysis1
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>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
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi762 ↔ 769By similarity
Disulfide bondi799 ↔ 835By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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

PRoteomics IDEntifications database

More...
PRIDEi
P79171

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer.

Interacts with SLC6A19 (By similarity).

By similarity

(Microbial infection) Interacts with FCoV, CCoV, TGEV and HCoV-229E spike glycoprotein.

2 Publications

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
9685.ENSFCAP00000008319

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P79171

Database of comparative protein structure models

More...
ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni33 – 66Cytosolic Ser/Thr-rich junctionAdd BLAST34
Regioni67 – 967MetalloproteaseAdd BLAST901
Regioni351 – 355Substrate bindingBy similarity5
Regioni670 – 840Interaction with FCoV and TGEV spike glycoprotein2 PublicationsAdd BLAST171

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the peptidase M1 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG1046 Eukaryota
COG0308 LUCA

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P79171

KEGG Orthology (KO)

More...
KOi
K11140

Database of Orthologous Groups

More...
OrthoDBi
110058at2759

Family and domain databases

Conserved Domains Database

More...
CDDi
cd09601 M1_APN-Q_like, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.60.40.1730, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR042097 Aminopeptidase_N-like_N
IPR024571 ERAP1-like_C_dom
IPR034016 M1_APN-typ
IPR001930 Peptidase_M1
IPR014782 Peptidase_M1_dom

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF11838 ERAP1_C, 1 hit
PF01433 Peptidase_M1, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00756 ALADIPTASE

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF63737 SSF63737, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00142 ZINC_PROTEASE, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i119BDAA34F5B5E89
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>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:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
U58920 mRNA Translation: AAC48686.1
U96104 mRNA Translation: AAD09272.1

NCBI Reference Sequences

More...
RefSeqi
NP_001009252.2, NM_001009252.2

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
493785

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
fca:493785

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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

SMRiP79171
ModBaseiSearch...

Protein-protein interaction databases

STRINGi9685.ENSFCAP00000008319

Protein family/group databases

MEROPSiM01.001

Proteomic databases

PRIDEiP79171

Genome annotation databases

GeneIDi493785
KEGGifca:493785

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
290

Phylogenomic databases

eggNOGiKOG1046 Eukaryota
COG0308 LUCA
InParanoidiP79171
KOiK11140
OrthoDBi110058at2759

Family and domain databases

CDDicd09601 M1_APN-Q_like, 1 hit
Gene3Di2.60.40.1730, 1 hit
InterProiView protein in InterPro
IPR042097 Aminopeptidase_N-like_N
IPR024571 ERAP1-like_C_dom
IPR034016 M1_APN-typ
IPR001930 Peptidase_M1
IPR014782 Peptidase_M1_dom
PfamiView protein in Pfam
PF11838 ERAP1_C, 1 hit
PF01433 Peptidase_M1, 1 hit
PRINTSiPR00756 ALADIPTASE
SUPFAMiSSF63737 SSF63737, 1 hit
PROSITEiView protein in PROSITE
PS00142 ZINC_PROTEASE, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiAMPN_FELCA
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P79171
Secondary accession number(s): O97783
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 23, 2007
Last modified: December 11, 2019
This is version 130 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Reference proteome

Documents

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