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Entry version 119 (29 Sep 2021)
Sequence version 2 (26 Nov 2014)
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Protein

Aminopeptidase S

Gene

SGR_5809

Organism
Streptomyces griseus subsp. griseus (strain JCM 4626 / NBRC 13350)
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

An exopeptidase specific for larger hydrophobic amino acids (especially leucine), no cleavage occurs if the next residue is proline (PubMed:8444149).

3 Publications

Miscellaneous

Most experiments use protein purified from a commercial source rather than protein that has been overexpressed.Curated

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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

<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

Protein has several cofactor binding sites:

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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

Calcium activates the enzyme, inhibited by 1,10-phenanthroline, EDTA and EGTA (PubMed:2503378). End-product inhibited by L-amino acids (PubMed:15388919). Non-competitively inhibited by NaF and NaH2PO4 (PubMed:17608735).4 Publications

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

kcat is 390 s(-1) with Leu-pNA.1 Publication
  1. KM=0.59 mM for Leu-NH-Np (with zinc as cofactor)1 Publication
  2. KM=0.13 mM for Leu-NH-Np (with manganese as cofactor)1 Publication
  3. KM=0.046 mM for Leu-NH-Np (with cobalt as cofactor)1 Publication
  4. KM=4.1 mM for Ala-NH-Np (with zinc as cofactor)1 Publication
  5. KM=1.74 mM for Ala-NH-Np (with cobalt as cofactor)1 Publication
  6. KM=0.57 mM for Leu-pNA (with zinc as cofactor)1 Publication

Temperature dependencei

Stable after heating at 69 degrees Celsius for 5 hours.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 bindingi48Calcium2 Publications1
Metal bindingi49Calcium; via carbonyl oxygen2 Publications1
Metal bindingi130Zinc 1; catalytic2 Publications1
Metal bindingi142Zinc 1; catalytic2 Publications1
Metal bindingi142Zinc 2; catalytic2 Publications1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei176Proton acceptor2 Publications1
Metal bindingi177Zinc 2; catalytic2 Publications1
Metal bindingi205Zinc 1; catalytic2 Publications1
<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>Sitei291Transition state stabilizer2 Publications1
Metal bindingi292Zinc 2; catalytic2 Publications1
Metal bindingi307Calcium2 Publications1
Metal bindingi311Calcium2 Publications1

<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

<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, Protease
LigandCalcium, Metal-binding, Zinc

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
SGRI455632:G1G2X-5896-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.4.11.24, 6035

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P80561

Protein family/group databases

MEROPS protease database

More...
MEROPSi
M28.003

<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_and_taxonomy_section">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 S (EC:3.4.11.24)
Alternative name(s):
API1 Publication
SGAP1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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
Ordered Locus Names:SGR_5809
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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>OrganismiStreptomyces griseus subsp. griseus (strain JCM 4626 / NBRC 13350)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 identifieri455632 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomyces
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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
  • UP000001685 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">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: Chromosome

<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

Keywords - Cellular componenti

Secreted

<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

<p>This subsection of the 'Pathology and Biotech' section describes the use of a specific protein in the biotechnological industry.<p><a href='/help/biotechnological_use' target='_top'>More...</a></p>Biotechnological usei

Sold by several companies as an extracellular extract called Pronase.3 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi176E → A: KM halves (0.33 mM), kcat reduces by 5 orders of magnitude. 1 Publication1
Mutagenesisi176E → D or Q: KM decreases (to 0.4 mM), kcat reduces by 4 orders of magnitude. 1 Publication1
Mutagenesisi291Y → A, F or S: Activity decreases about 100-fold. 1 Publication1

Chemistry databases

Drug and drug target database

More...
DrugBanki
DB04713, 4-Iodo-D-phenylalanine
DB03660, 4-Iodo-L-phenylalanine
DB02467, L-methionine (S)-S-oxide

<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 denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 452 PublicationsAdd BLAST45
<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_000017414346 – 329Aminopeptidase SAdd BLAST284
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_0000431389330 – 445Removed in mature form1 PublicationAdd BLAST116

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 bondi290 ↔ 2952 Publications

Keywords - PTMi

Disulfide bond, Zymogen

<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_section">'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_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Monomer.

2 Publications

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
455632.SGR_5809

<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

Secondary structure

1445
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...
SMRi
P80561

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P80561

<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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini325 – 445P/Homo BPROSITE-ProRule annotationAdd BLAST121

<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 M28 family. M28A subfamily.Curated

Keywords - Domaini

Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
COG2234, Bacteria
COG4935, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_024336_2_0_11

Identification of Orthologs from Complete Genome Data

More...
OMAi
DHASFKN

Database of Orthologous Groups

More...
OrthoDBi
1465483at2

Family and domain databases

Conserved Domains Database

More...
CDDi
cd03876, M28_SGAP_like, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR008979, Galactose-bd-like_sf
IPR041756, M28_SGAP-like
IPR002884, P_dom
IPR007484, Peptidase_M28

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01483, P_proprotein, 1 hit
PF04389, Peptidase_M28, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF49785, SSF49785, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51829, P_HOMO_B, 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_length">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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P80561-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MRPNRFSLRR SPTAVAAVAL AAVLAAGAPA AQAAGAAAPT AAAAAAPDIP
60 70 80 90 100
LANVKAHLTQ LSTIAANNGG NRAHGRPGYK ASVDYVKAKL DAAGYTTTLQ
110 120 130 140 150
QFTSGGATGY NLIADWPGGD PNKVLMAGAH LDSVSSGAGI NDNGSGSAAV
160 170 180 190 200
LETALAVSRA GYQPDKHLRF AWWGAEELGL IGSKYYVNNL PSADRSKLAG
210 220 230 240 250
YLNFDMIGSP NPGYFVYDDD PVIEKTFKDY FAGLNVPTEI ETEGDGRSDH
260 270 280 290 300
APFKNVGVPV GGLFTGAGYT KSAAQAQKWG GTAGQAFDRC YHSSCDSLSN
310 320 330 340 350
INDTALDRNS DAAAHAIWTL SSGTGEPPTG EGVFSNTTDV AIPDAGAAVT
360 370 380 390 400
SSVAVTGRTG NAPAALQVGV DIKHTYRGDL VVDLLAPDGT AYRLKNSSSG
410 420 430 440
DSADNVIATY TVNASSEVAN GSWKLRVQDI ARQDTGYIDS WKLTF
Length:445
Mass (Da):45,940
Last modified:November 26, 2014 - v2
<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:i6B42B63191F700C9
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 conflicti185Y → F AA sequence (PubMed:8665903).1
Sequence conflicti285Q → R no nucleotide entry (PubMed:15280041).1

<p>This subsection of the 'Sequence' section reports information derived from mass spectrometry experiments done on the entire protein or on biologically active derived peptide(s).<p><a href='/help/mass_spectrometry' target='_top'>More...</a></p>Mass spectrometryi

Molecular mass is 29728±1.0 Da. Determined by ESI. 1 Publication

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
AP009493 Genomic DNA Translation: BAG22638.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S66427

NCBI Reference Sequences

More...
RefSeqi
WP_012381549.1, NC_010572.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
BAG22638; BAG22638; SGR_5809

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
6210128

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sgr:SGR_5809

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|455632.4.peg.5952

<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
AP009493 Genomic DNA Translation: BAG22638.1
PIRiS66427
RefSeqiWP_012381549.1, NC_010572.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CP7X-ray1.58A46-329[»]
1F2OX-ray1.70A46-329[»]
1F2PX-ray1.80A46-329[»]
1QQ9X-ray1.53A46-329[»]
1TF8X-ray1.30A46-329[»]
1TF9X-ray1.30A46-329[»]
1TKFX-ray1.20A46-329[»]
1TKHX-ray1.25A46-329[»]
1TKJX-ray1.15A46-329[»]
1XBUX-ray1.20A46-322[»]
1XJOX-ray1.75A46-329[»]
SMRiP80561
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

STRINGi455632.SGR_5809

Chemistry databases

DrugBankiDB04713, 4-Iodo-D-phenylalanine
DB03660, 4-Iodo-L-phenylalanine
DB02467, L-methionine (S)-S-oxide

Protein family/group databases

MEROPSiM28.003

Genome annotation databases

EnsemblBacteriaiBAG22638; BAG22638; SGR_5809
GeneIDi6210128
KEGGisgr:SGR_5809
PATRICifig|455632.4.peg.5952

Phylogenomic databases

eggNOGiCOG2234, Bacteria
COG4935, Bacteria
HOGENOMiCLU_024336_2_0_11
OMAiDHASFKN
OrthoDBi1465483at2

Enzyme and pathway databases

BioCyciSGRI455632:G1G2X-5896-MONOMER
BRENDAi3.4.11.24, 6035
SABIO-RKiP80561

Miscellaneous databases

EvolutionaryTraceiP80561

Family and domain databases

CDDicd03876, M28_SGAP_like, 1 hit
InterProiView protein in InterPro
IPR008979, Galactose-bd-like_sf
IPR041756, M28_SGAP-like
IPR002884, P_dom
IPR007484, Peptidase_M28
PfamiView protein in Pfam
PF01483, P_proprotein, 1 hit
PF04389, Peptidase_M28, 1 hit
SUPFAMiSSF49785, SSF49785, 1 hit
PROSITEiView protein in PROSITE
PS51829, P_HOMO_B, 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 nameiAPX_STRGG
<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: P80561
Secondary accession number(s): B1W291
<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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: November 26, 2014
Last modified: September 29, 2021
This is version 119 of the entry and version 2 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 programProkaryotic 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

3D-structure, Direct protein sequencing

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
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