AMY_DERPT
ID AMY_DERPT Reviewed; 496 AA.
AC P49274; Q9Y197;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 16-OCT-2019, sequence version 2.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Alpha-amylase {ECO:0000255|RuleBase:RU361134, ECO:0000303|PubMed:10545763, ECO:0000303|PubMed:8781672};
DE EC=3.2.1.1 {ECO:0000269|PubMed:1710630, ECO:0000269|PubMed:8781672};
DE AltName: Full=1,4-alpha-D-glucan glucanohydrolase {ECO:0000305};
DE AltName: Full=Allergen Der p IV {ECO:0000303|PubMed:1718897};
DE AltName: Full=Mite group 4 allergen Der p 4 {ECO:0000303|PubMed:10545763};
DE AltName: Allergen=Der p 4.0101 {ECO:0000305};
DE Flags: Fragment;
OS Dermatophagoides pteronyssinus (European house dust mite).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Acariformes; Sarcoptiformes; Astigmata; Psoroptidia; Analgoidea;
OC Pyroglyphidae; Dermatophagoidinae; Dermatophagoides.
OX NCBI_TaxID=6956;
RN [1] {ECO:0000312|EMBL:AAD38942.1}
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND ALLERGEN.
RX PubMed=10545763; DOI=10.1159/000024227;
RA Mills K.L., Hart B.J., Lynch N.R., Thomas W.R., Smith W.;
RT "Molecular characterization of the group 4 house dust mite allergen from
RT Dermatophagoides pteronyssinus and its amylase homologue from Euroglyphus
RT maynei.";
RL Int. Arch. Allergy Immunol. 120:100-107(1999).
RN [2]
RP PROTEIN SEQUENCE OF 1-19, AND SUBCELLULAR LOCATION.
RX PubMed=1718897; DOI=10.1159/000235402;
RA Lake F.R., Ward L.D., Simpson R.J., Thompson P.J., Stewart G.A.;
RT "Allergenicity and physicochemical characterization of house dust mite
RT derived amylase.";
RL Int. Arch. Allergy Appl. Immunol. 94:357-358(1991).
RN [3]
RP PROTEIN SEQUENCE OF 1-19, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBCELLULAR LOCATION, ALLERGEN, AND PRESENCE OF DISULFIDE
RP BONDS.
RX PubMed=1710630; DOI=10.1016/0091-6749(91)92147-s;
RA Lake F.R., Ward L.D., Simpson R.J., Thompson P.J., Stewart G.A.;
RT "House dust mite-derived amylase: allergenicity and physicochemical
RT characterization.";
RL J. Allergy Clin. Immunol. 87:1035-1042(1991).
RN [4]
RP CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND SUBCELLULAR LOCATION.
RX PubMed=8781672; DOI=10.1111/j.1398-9995.1996.tb04583.x;
RA Sanchez-Monge R., Garcia-Casado G., Barber D., Salcedo G.;
RT "Interaction of allergens from house-dust mite and from cereal flours:
RT Dermatophagoides pteronyssinus alpha-amylase (Der p 4) and wheat and rye
RT alpha-amylase inhibitors.";
RL Allergy 51:176-180(1996).
RN [5]
RP ALLERGEN.
RX PubMed=17845417; DOI=10.1111/j.1365-2222.2007.02786.x;
RA Hales B.J., Laing I.A., Pearce L.J., Hazell L.A., Mills K.L., Chua K.Y.,
RA Thornton R.B., Richmond P., Musk A.W., James A.L., Lesouef P.N.,
RA Thomas W.R.;
RT "Distinctive immunoglobulin E anti-house dust allergen-binding
RT specificities in a tropical Australian Aboriginal community.";
RL Clin. Exp. Allergy 37:1357-1363(2007).
CC -!- FUNCTION: Aids in the digestion of starch and glycogen derived from
CC food, such as skin scales, fungi and bacteria.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in
CC polysaccharides containing three or more (1->4)-alpha-linked D-
CC glucose units.; EC=3.2.1.1; Evidence={ECO:0000269|PubMed:1710630,
CC ECO:0000269|PubMed:8781672};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:P56634};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:P56634};
CC -!- COFACTOR:
CC Name=chloride; Xref=ChEBI:CHEBI:17996;
CC Evidence={ECO:0000250|UniProtKB:P56634};
CC Note=Binds 1 Cl(-) ion per subunit. {ECO:0000250|UniProtKB:P56634};
CC -!- ACTIVITY REGULATION: Inhibited by alpha-amylase inhibitors from wheat
CC and rye. The most effective inhibitors are the wheat tetrameric alpha-
CC amylase inhibitor (WTAI) and the rye dimeric alpha-amylase inhibitor
CC (RDAI-1). Not inhibited by alpha-amylase inhibitor from barley.
CC {ECO:0000269|PubMed:8781672}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6.4. {ECO:0000269|PubMed:1710630};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P56634}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10545763,
CC ECO:0000269|PubMed:1710630, ECO:0000269|PubMed:1718897,
CC ECO:0000269|PubMed:8781672}.
CC -!- PTM: Disulfide bonds are present. {ECO:0000269|PubMed:1710630}.
CC -!- ALLERGEN: Causes an allergic reaction in human (PubMed:10545763,
CC PubMed:1710630, PubMed:17845417). Binds to IgE in 30% of the 10
CC patients tested allergic to D.pteronyssinus, the European house dust
CC mite (HDM) (PubMed:10545763). Binds to IgE in 46% of the 27 adults and
CC in 25% of the 20 children tested allergic to mites (PubMed:1710630).
CC The IgE of the mite-atopic tropical Australian Aboriginal patients
CC binds unusually mainly to this protein, whereas this protein is a minor
CC allergen in mite-atopic urban patients from Perth, including three
CC patients of Aboriginal origin. IgE-binding to this protein is not the
CC result of cross-reactivity to another amylase in these patients since
CC IgE-binding to the extract from Culicoides, the biting midges common in
CC the north west of Western Australia, is negative, as is the IgE-binding
CC to the major allergen of B.tropicalis, a prevalent mite in the tropics.
CC It is also unlikely that the IgE is induced by parasites, because
CC parasitic infections also induce IgG4 antibody, which is mostly absent
CC in the atopic Aboriginal population, although antibody to the Der p 4
CC allergen is occasionally detected. The amylases in mollusks could
CC potentially be sensitizing, but mollusks are rarely consumed in the
CC Aboriginal community (PubMed:17845417). The allergenicity of this
CC protein is dependent on the presence of the disulfide bonds
CC (PubMed:1710630). Common symptoms of mite allergy are bronchial asthma,
CC allergic rhinitis and conjunctivitis (Probable).
CC {ECO:0000269|PubMed:10545763, ECO:0000269|PubMed:1710630,
CC ECO:0000269|PubMed:17845417, ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC {ECO:0000255|RuleBase:RU003615, ECO:0000305}.
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DR EMBL; AF144060; AAD38942.1; -; mRNA.
DR PIR; A39729; A39729.
DR AlphaFoldDB; P49274; -.
DR SMR; P49274; -.
DR Allergome; 318; Der p 4.
DR Allergome; 3264; Der p 4.0101.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR Proteomes; UP000515146; Unplaced.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0004556; F:alpha-amylase activity; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0031404; F:chloride ion binding; ISS:UniProtKB.
DR GO; GO:0009313; P:oligosaccharide catabolic process; IDA:UniProtKB.
DR Gene3D; 2.60.40.1180; -; 1.
DR InterPro; IPR006048; A-amylase/branching_C.
DR InterPro; IPR031319; A-amylase_C.
DR InterPro; IPR006046; Alpha_amylase.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF00128; Alpha-amylase; 1.
DR Pfam; PF02806; Alpha-amylase_C; 1.
DR PRINTS; PR00110; ALPHAAMYLASE.
DR SMART; SM00642; Aamy; 1.
DR SMART; SM00632; Aamy_C; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 1: Evidence at protein level;
KW Allergen; Calcium; Carbohydrate metabolism; Chloride;
KW Direct protein sequencing; Disulfide bond; Glycosidase; Hydrolase;
KW Metal-binding; Reference proteome; Secreted.
FT CHAIN <1..496
FT /note="Alpha-amylase"
FT /id="PRO_0000054284"
FT ACT_SITE 194
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT ACT_SITE 230
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT BINDING 99
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT BINDING 155
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT BINDING 164
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT BINDING 192
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT BINDING 198
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT BINDING 332
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT SITE 295
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT DISULFID 29..85
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT DISULFID 374..380
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT DISULFID 448..460
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT NON_TER 1
FT /evidence="ECO:0000312|EMBL:AAD38942.1"
SQ SEQUENCE 496 AA; 57150 MW; 11F0883F682E3A45 CRC64;
KYHNPHFIGN RSVITHLMEW KYDDIGDECE RFLGPYGYGG VQVSPVNEHA ILDRRPWYER
YQPVSYDIRT RSGDEQQFRR MVKRCNKAGV RIYVDIVLNH MTGAQSGKGT NGHHYDGNTL
QYPGVPFGPN DFHGHESCPT QDLEIHDYTN PKEARNCRLS GLRDLKQQSE YVRQKQVDFL
NHLIDIGVAG FRSDASTHQW PDDLRSIYSR LHNLNKEFFP ENSQPFIYHE TIYYGGNGIN
SNEYTSLGRI IEFRFYKEIT NVFRGNNPLH WLKNFGTEWG LVPSGDALVM IDSHDLRVGH
TGKLGFNINC FEGRLLKAAT AFMLAWNYGV PRVMSSYFWN QIIKDGKDVN DWVGPPSDKN
GNILSVHPNP DMTCNHEWIC EHRWREIYNM VKFRMIAGQE PVHNWWDNGD YQIAFSRGNR
AFIAINLQKN QQNLQQKLHT GLPAGTYCDI ISGNLIDNKC TGKSIHVDKN GQADVYVGHD
EFDAFVAYHI GARIVS
