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Entry version 121 (02 Jun 2021)
Sequence version 1 (01 Feb 1997)
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Protein

Glutamyl aminopeptidase

Gene

ENPEP

Organism
Sus scrofa (Pig)
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

Regulates central hypertension through its calcium-modulated preference to cleave N-terminal acidic residues from peptides such as angiotensin II.

By similarity

<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 N-terminal glutamate (and to a lesser extent aspartate) from a peptide.By similarity EC:3.4.11.7

<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

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Substrate specificity is modulated by calcium which enhances the enzymatic activity for cleavage of acidic residues while reducing its activity with basic residues. Inhibited by aminopeptidase inhibitors amastatin and bestatin.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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>Sitei211Binds calcium which modulates its enzyme activityBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei213SubstrateBy similarity1
<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 bindingi383Zinc; via tele nitrogen; 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 sitei384Proton acceptorPROSITE-ProRule annotation1
Metal bindingi387Zinc; via tele nitrogen; catalyticPROSITE-ProRule annotation1
Metal bindingi406Zinc; catalyticPROSITE-ProRule annotation1
Sitei469Transition state stabilizerBy similarity1
Binding sitei877SubstrateBy 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, Hydrolase, Metalloprotease, Protease
LigandCalcium, Metal-binding, Zinc

Enzyme and pathway databases

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
Q95334

Protein family/group databases

MEROPS protease database

More...
MEROPSi
M01.003

<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:
Glutamyl aminopeptidase (EC:3.4.11.7)
Short name:
EAP
Alternative name(s):
Aminopeptidase A
Short name:
AP-A
CD_antigen: CD249
<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:ENPEP
<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>OrganismiSus scrofa (Pig)
<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 identifieri9823 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaArtiodactylaSuinaSuidaeSus
<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
  • UP000314985 <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
  • UP000008227 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

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 – 14CytoplasmicSequence analysisAdd BLAST14
<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>Transmembranei15 – 35Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST21
Topological domaini36 – 942ExtracellularSequence analysisAdd BLAST907

Keywords - Cellular componenti

Cell membrane, Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL4868

<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_00000950971 – 942Glutamyl aminopeptidaseAdd BLAST942

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>Glycosylationi110N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi114N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi187N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi314N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi367N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi557N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi579N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi587N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi597N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi632N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi668N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi753N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi786N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi791N-linked (GlcNAc...) asparagineSequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PeptideAtlas

More...
PeptideAtlasi
Q95334

PRoteomics IDEntifications database

More...
PRIDEi
Q95334

<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; disulfide-linked.

1 Publication

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
9823.ENSSSCP00000009739

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
Q95334

<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
Q95334

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>Regioni40 – 74DisorderedSequence analysisAdd BLAST35
Regioni347 – 351Substrate bindingBy similarity5

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi40 – 54Polar residuesSequence analysisAdd BLAST15

<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

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q95334

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
IPR033508, Aminopeptidase_A
IPR042097, Aminopeptidase_N-like_N
IPR024571, ERAP1-like_C_dom
IPR034016, M1_APN-typ
IPR001930, Peptidase_M1
IPR014782, Peptidase_M1_dom

The PANTHER Classification System

More...
PANTHERi
PTHR11533:SF242, PTHR11533:SF242, 1 hit

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.

Q95334-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSTDSKRYCI KTKHVAIICA AVVAVGLIVG LSVGLTRSCD SKDGGQGTTQ
60 70 80 90 100
SPSHLPPTSS PPQDQGVCPA SEDESGNWRD FRLPDFINPV HYDLQVKPLL
110 120 130 140 150
EQDTYTGTVN ISINVTSPTQ HLWLHLRETR ITQLPVLWRP SGEQVQVRRC
160 170 180 190 200
FEYKKQEYVV VEAEEELAPN SGEGLYHLTM EFAGWLNGSL VGFYRTTYVE
210 220 230 240 250
KGQIKSIAAT DHEPTDARKS FPCFDEPNKK ATYTISIIHP KEYKALSNMP
260 270 280 290 300
VEKEESVDDI WTQTTFQKSV PMSTYLVCFA VHQFDSVTRT SRSGKPLTIY
310 320 330 340 350
VQPEQKHTAE YAANITKSVF DYFEDYFAME YSLPKLDKIA IPDFGTGAME
360 370 380 390 400
NWGLITYRET NLLYDPNESA SSNQQRVAAV VAHELVHQWF GNIVTMEWWE
410 420 430 440 450
DLWLNEGFAS FFEFLGVDHA EKEWQMRDQI LLEDVLPVQE DDSLISSHPI
460 470 480 490 500
VVTVSTPAEI TSVFDGISYS KGASILRMLE DWITPEKFQK GCQEYLKKFE
510 520 530 540 550
FKNAKTSDFW EALEEASNLP VKEVMDTWTN QMGYPVLNVE DMRIISQKRF
560 570 580 590 600
LLDPNANSSE PHSVFGYTWN IPVRWTNDNE STITIYNRSE TGGITLNSSN
610 620 630 640 650
PNGNAFLKIN PDHIGFYRVN YEVSTWEWIA TNLSLNHKDF STADRASLID
660 670 680 690 700
DAFALARAQL LNYKEALNLT KYLKMEDEYL PWQRVISAVT YIISMFEDDK
710 720 730 740 750
ELYPMIEKYF RDQVKPIADS LGWNDNGDHL TKLLRASVLG FACKMGDSNA
760 770 780 790 800
LNNASHLFEQ WLTGTVSLPV NLRLLVYRYG MQNSGNETSW NYTLKQYQET
810 820 830 840 850
SLAQEKEKLL YGLASVKNVA LLSRYLDLLK DPNVIKSQDV FTVIRYISYN
860 870 880 890 900
SYGKTMAWNW IQLNWEYLVN RYTLNDRNLG RIVTIAEPFN TELQLWQMES
910 920 930 940
FFKRYPEAGA GEKPREQVLE TVKNNIEWLK QNRDTIRDWF FN
Length:942
Mass (Da):108,284
Last modified:February 1, 1997 - v1
<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:iC531E639A588EF2E
GO

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
U66371 mRNA Translation: AAB07141.1

NCBI Reference Sequences

More...
RefSeqi
NP_999182.1, NM_214017.1

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSSSCT00055031803; ENSSSCP00055025312; ENSSSCG00055016116
ENSSSCT00065093299; ENSSSCP00065040826; ENSSSCG00065067948

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
397080

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ssc:397080

<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
U66371 mRNA Translation: AAB07141.1
RefSeqiNP_999182.1, NM_214017.1

3D structure databases

SMRiQ95334
ModBaseiSearch...

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000009739

Chemistry databases

BindingDBiQ95334
ChEMBLiCHEMBL4868

Protein family/group databases

MEROPSiM01.003

Proteomic databases

PeptideAtlasiQ95334
PRIDEiQ95334

Genome annotation databases

EnsembliENSSSCT00055031803; ENSSSCP00055025312; ENSSSCG00055016116
ENSSSCT00065093299; ENSSSCP00065040826; ENSSSCG00065067948
GeneIDi397080
KEGGissc:397080

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
2028

Phylogenomic databases

eggNOGiKOG1046, Eukaryota
InParanoidiQ95334
OrthoDBi110058at2759

Enzyme and pathway databases

SABIO-RKiQ95334

Family and domain databases

CDDicd09601, M1_APN-Q_like, 1 hit
Gene3Di2.60.40.1730, 1 hit
InterProiView protein in InterPro
IPR033508, Aminopeptidase_A
IPR042097, Aminopeptidase_N-like_N
IPR024571, ERAP1-like_C_dom
IPR034016, M1_APN-typ
IPR001930, Peptidase_M1
IPR014782, Peptidase_M1_dom
PANTHERiPTHR11533:SF242, PTHR11533:SF242, 1 hit
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

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 nameiAMPE_PIG
<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: Q95334
<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: August 31, 2004
Last sequence update: February 1, 1997
Last modified: June 2, 2021
This is version 121 of the entry and version 1 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. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families
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