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Entry version 66 (26 Feb 2020)
Sequence version 2 (16 Oct 2019)
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Protein

Alpha-amylase

Gene
N/A
Organism
Dermatophagoides pteronyssinus (European house dust mite)
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

Aids in the digestion of starch and glycogen derived from food, such as skin scales, fungi and bacteria.

<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

<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%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

Inhibited by alpha-amylase inhibitors from wheat and rye. The most effective inhibitors are the wheat tetrameric alpha-amylase inhibitor (WTAI) and the rye dimeric alpha-amylase inhibitor (RDAI-1). Not inhibited by alpha-amylase inhibitor from barley.1 Publication

<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>pH dependencei

Optimum pH is 6.4.1 Publication

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 bindingi99CalciumBy similarity1
Metal bindingi155Calcium; via carbonyl oxygenBy similarity1
Metal bindingi164CalciumBy 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 sitei192ChlorideBy similarity1
<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 sitei194NucleophileBy similarity1
Metal bindingi198Calcium; via carbonyl oxygenBy similarity1
Active sitei230Proton donorBy similarity1
<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>Sitei295Transition state stabilizerBy similarity1
Binding sitei332ChlorideBy 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 functionGlycosidase, Hydrolase
Biological processCarbohydrate metabolism
LigandCalcium, Chloride, Metal-binding

Protein family/group databases

Carbohydrate-Active enZymes

More...
CAZyi
GH13 Glycoside Hydrolase Family 13

<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:
Alpha-amylase2 PublicationsUniRule annotation (EC:3.2.1.12 Publications)
Alternative name(s):
1,4-alpha-D-glucan glucanohydrolaseCurated
Allergen Der p IV1 Publication
Mite group 4 allergen Der p 41 Publication
Allergen: Der p 4.0101Curated
<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>OrganismiDermatophagoides pteronyssinus (European house dust mite)
<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 identifieri6956 [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 lineageiEukaryotaMetazoaEcdysozoaArthropodaChelicerataArachnidaAcariAcariformesSarcoptiformesAstigmataPsoroptidiaAnalgoideaPyroglyphidaeDermatophagoidinaeDermatophagoides

<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

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 <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section is used for proteins that cause an allergic reaction in mammals. We usually specify in which species the protein is allergenic.<p><a href='/help/allergenic_properties' target='_top'>More...</a></p>Allergenic propertiesi

Causes an allergic reaction in human (PubMed:10545763, PubMed:1710630, PubMed:17845417). Binds to IgE in 30% of the 10 patients tested allergic to D.pteronyssinus, the European house dust mite (HDM) (PubMed:10545763). Binds to IgE in 46% of the 27 adults and in 25% of the 20 children tested allergic to mites (PubMed:1710630). The IgE of the mite-atopic tropical Australian Aboriginal patients binds unusually mainly to this protein, whereas this protein is a minor allergen in mite-atopic urban patients from Perth, including three patients of Aboriginal origin. IgE-binding to this protein is not the result of cross-reactivity to another amylase in these patients since IgE-binding to the extract from Culicoides, the biting midges common in the north west of Western Australia, is negative, as is the IgE-binding to the major allergen of B.tropicalis, a prevalent mite in the tropics. It is also unlikely that the IgE is induced by parasites, because parasitic infections also induce IgG4 antibody, which is mostly absent in the atopic Aboriginal population, although antibody to the Der p 4 allergen is occasionally detected. The amylases in mollusks could potentially be sensitizing, but mollusks are rarely consumed in the Aboriginal community (PubMed:17845417). The allergenicity of this protein is dependent on the presence of the disulfide bonds (PubMed:1710630). Common symptoms of mite allergy are bronchial asthma, allergic rhinitis and conjunctivitis (Probable).Curated3 Publications

Keywords - Diseasei

Allergen

Protein family/group databases

Allergome; a platform for allergen knowledge

More...
Allergomei
318 Der p 4
3264 Der p 4.0101

<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_0000054284‹1 – 496Alpha-amylaseAdd BLAST›496

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 bondi29 ↔ 85By similarity
Disulfide bondi374 ↔ 380By similarity
Disulfide bondi448 ↔ 460By 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

Disulfide bonds are present.1 Publication

Keywords - PTMi

Disulfide bond

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
P49274

<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

Monomer.

By similarity

<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

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SMRi
P49274

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

<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 glycosyl hydrolase 13 family.UniRule annotationCurated

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.60.40.1180, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR006048 A-amylase/branching_C
IPR031319 A-amylase_C
IPR006046 Alpha_amylase
IPR006047 Glyco_hydro_13_cat_dom
IPR013780 Glyco_hydro_b
IPR017853 Glycoside_hydrolase_SF

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00128 Alpha-amylase, 1 hit
PF02806 Alpha-amylase_C, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00110 ALPHAAMYLASE

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00642 Aamy, 1 hit
SM00632 Aamy_C, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF51445 SSF51445, 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: Fragment.

P49274-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
KYHNPHFIGN RSVITHLMEW KYDDIGDECE RFLGPYGYGG VQVSPVNEHA
60 70 80 90 100
ILDRRPWYER YQPVSYDIRT RSGDEQQFRR MVKRCNKAGV RIYVDIVLNH
110 120 130 140 150
MTGAQSGKGT NGHHYDGNTL QYPGVPFGPN DFHGHESCPT QDLEIHDYTN
160 170 180 190 200
PKEARNCRLS GLRDLKQQSE YVRQKQVDFL NHLIDIGVAG FRSDASTHQW
210 220 230 240 250
PDDLRSIYSR LHNLNKEFFP ENSQPFIYHE TIYYGGNGIN SNEYTSLGRI
260 270 280 290 300
IEFRFYKEIT NVFRGNNPLH WLKNFGTEWG LVPSGDALVM IDSHDLRVGH
310 320 330 340 350
TGKLGFNINC FEGRLLKAAT AFMLAWNYGV PRVMSSYFWN QIIKDGKDVN
360 370 380 390 400
DWVGPPSDKN GNILSVHPNP DMTCNHEWIC EHRWREIYNM VKFRMIAGQE
410 420 430 440 450
PVHNWWDNGD YQIAFSRGNR AFIAINLQKN QQNLQQKLHT GLPAGTYCDI
460 470 480 490
ISGNLIDNKC TGKSIHVDKN GQADVYVGHD EFDAFVAYHI GARIVS
Length:496
Mass (Da):57,150
Last modified:October 16, 2019 - 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:i11F0883F682E3A45
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section is used for sequence fragments to indicate that the residue at the extremity of the sequence is not the actual terminal residue in the complete protein sequence.<p><a href='/help/non_ter' target='_top'>More...</a></p>Non-terminal residuei1Imported1

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
AF144060 mRNA Translation: AAD38942.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A39729

<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
AF144060 mRNA Translation: AAD38942.1
PIRiA39729

3D structure databases

SMRiP49274
ModBaseiSearch...

Protein family/group databases

Allergomei318 Der p 4
3264 Der p 4.0101
CAZyiGH13 Glycoside Hydrolase Family 13

Proteomic databases

PRIDEiP49274

Family and domain databases

Gene3Di2.60.40.1180, 1 hit
InterProiView protein in InterPro
IPR006048 A-amylase/branching_C
IPR031319 A-amylase_C
IPR006046 Alpha_amylase
IPR006047 Glyco_hydro_13_cat_dom
IPR013780 Glyco_hydro_b
IPR017853 Glycoside_hydrolase_SF
PfamiView protein in Pfam
PF00128 Alpha-amylase, 1 hit
PF02806 Alpha-amylase_C, 1 hit
PRINTSiPR00110 ALPHAAMYLASE
SMARTiView protein in SMART
SM00642 Aamy, 1 hit
SM00632 Aamy_C, 1 hit
SUPFAMiSSF51445 SSF51445, 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 nameiAMY_DERPT
<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: P49274
Secondary accession number(s): Q9Y197
<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: February 1, 1996
Last sequence update: October 16, 2019
Last modified: February 26, 2020
This is version 66 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)

<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

Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Allergens
    Nomenclature of allergens and list of entries
  3. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
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