MAL11_MALDO
ID MAL11_MALDO Reviewed; 159 AA.
AC P43211;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 25-MAY-2022, entry version 89.
DE RecName: Full=Major allergen Mal d 1 {ECO:0000303|PubMed:7677763};
DE AltName: Full=Allergen Mal d I {ECO:0000303|PubMed:7677763};
DE AltName: Allergen=Mal d 1 {ECO:0000303|PubMed:7677763};
GN Name=MALD1 {ECO:0000303|PubMed:7677763};
OS Malus domestica (Apple) (Pyrus malus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Maleae; Malus.
OX NCBI_TaxID=3750;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Granny Smith;
RA Schoening B., Ziegler W.H., Vieths S., Baltes W.;
RL Submitted (DEC-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Golden Delicious; TISSUE=Mesocarp;
RX PubMed=7677763; DOI=10.1006/bbrc.1995.2320;
RA Vanek-Krebitz M., Hoffmann-Sommergruber K., Laimer da Camara Machado M.,
RA Susani M., Ebner C., Kraft D., Scheiner O., Breiteneder H.;
RT "Cloning and sequencing of Mal d 1, the major allergen from apple (Malus
RT domestica), and its immunological relationship to Bet v 1, the major birch
RT pollen allergen.";
RL Biochem. Biophys. Res. Commun. 214:538-551(1995).
RN [3]
RP PROTEIN SEQUENCE OF 2-26.
RC STRAIN=cv. Golden Delicious;
RX PubMed=7518715; DOI=10.1159/000236698;
RA Vieths S., Schoening B., Petersen A.;
RT "Characterization of the 18-kDa apple allergen by two-dimensional
RT immunoblotting and microsequencing.";
RL Int. Arch. Allergy Immunol. 104:399-404(1994).
RN [4]
RP PROTEIN SEQUENCE OF 2-6, MUTAGENESIS OF THR-11; ILE-31; THR-58; THR-113 AND
RP ILE-114, AND ALLERGEN.
RX PubMed=16293967; DOI=10.1159/000089756;
RA Ma Y., Gadermaier G., Bohle B., Bolhaar S., Knulst A., Markovic-Housley Z.,
RA Breiteneder H., Briza P., Hoffmann-Sommergruber K., Ferreira F.;
RT "Mutational analysis of amino acid positions crucial for IgE-binding
RT epitopes of the major apple (Malus domestica) allergen, Mal d 1.";
RL Int. Arch. Allergy Immunol. 139:53-62(2006).
RN [5]
RP STRUCTURE BY NMR OF 2-159.
RC STRAIN=cv. Granny Smith;
RX PubMed=27165578; DOI=10.1007/s12104-016-9685-8;
RA Ahammer L., Grutsch S., Tollinger M.;
RT "NMR resonance assignments of the major apple allergen Mal d 1.";
RL Biomol. NMR. Assign. 10:287-290(2016).
RN [6]
RP STRUCTURE BY NMR OF 2-159.
RC STRAIN=cv. Granny Smith; TISSUE=Fruit;
RX PubMed=28161953; DOI=10.1021/acs.jafc.6b05752;
RA Ahammer L., Grutsch S., Kamenik A.S., Liedl K.R., Tollinger M.;
RT "Structure of the major apple allergen Mald1.";
RL J. Agric. Food Chem. 65:1606-1612(2017).
CC -!- ALLERGEN: Causes an allergic reaction in human; allergic reactions
CC against this protein result from initial sensitization to the major
CC allergen from birch pollen, Bet v 1. {ECO:0000269|PubMed:16293967,
CC ECO:0000305|PubMed:27165578, ECO:0000305|PubMed:28161953}.
CC -!- SIMILARITY: Belongs to the BetVI family. {ECO:0000305}.
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DR EMBL; X83672; CAA58646.1; -; mRNA.
DR EMBL; Z48969; CAA88833.1; -; mRNA.
DR PIR; JC4276; JC4276.
DR PDB; 5MMU; NMR; -; A=2-159.
DR PDBsum; 5MMU; -.
DR AlphaFoldDB; P43211; -.
DR BMRB; P43211; -.
DR SMR; P43211; -.
DR STRING; 3750.XP_008390602.1; -.
DR Allergome; 1447; Mal d 1.0101.
DR Allergome; 1448; Mal d 1.0102.
DR Allergome; 464; Mal d 1.
DR GO; GO:0010427; F:abscisic acid binding; IEA:InterPro.
DR GO; GO:0004864; F:protein phosphatase inhibitor activity; IEA:InterPro.
DR GO; GO:0038023; F:signaling receptor activity; IEA:InterPro.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IEA:InterPro.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0009607; P:response to biotic stimulus; IEA:UniProtKB-KW.
DR Gene3D; 3.30.530.20; -; 1.
DR InterPro; IPR000916; Bet_v_I/MLP.
DR InterPro; IPR024949; Bet_v_I_allergen.
DR InterPro; IPR023393; START-like_dom_sf.
DR Pfam; PF00407; Bet_v_1; 1.
DR PRINTS; PR00634; BETALLERGEN.
DR PROSITE; PS00451; PATHOGENESIS_BETVI; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Allergen; Direct protein sequencing;
KW Pathogenesis-related protein; Plant defense.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:16293967,
FT ECO:0000269|PubMed:7518715"
FT CHAIN 2..159
FT /note="Major allergen Mal d 1"
FT /id="PRO_0000154190"
FT SITE 11
FT /note="Crucial for IgE recognition during allergic reaction
FT in human"
FT /evidence="ECO:0000269|PubMed:16293967"
FT SITE 31
FT /note="Crucial for IgE recognition during allergic reaction
FT in human"
FT /evidence="ECO:0000269|PubMed:16293967"
FT SITE 58
FT /note="Crucial for IgE recognition during allergic reaction
FT in human"
FT /evidence="ECO:0000269|PubMed:16293967"
FT SITE 113
FT /note="Crucial for IgE recognition during allergic reaction
FT in human"
FT /evidence="ECO:0000269|PubMed:16293967"
FT SITE 114
FT /note="Crucial for IgE recognition during allergic reaction
FT in human"
FT /evidence="ECO:0000269|PubMed:16293967"
FT VARIANT 10
FT /note="F -> Y"
FT MUTAGEN 11
FT /note="T->P: Reduced capacity to bind specific IgE leading
FT to attenuated allergic reactions in human; when associated
FT with P-11, N-58, C-113 and V-114."
FT /evidence="ECO:0000269|PubMed:16293967"
FT MUTAGEN 31
FT /note="I->V: Reduced capacity to bind specific IgE leading
FT to attenuated allergic reactions in human; when associated
FT with P-11, N-58, C-113 and V-114."
FT /evidence="ECO:0000269|PubMed:16293967"
FT MUTAGEN 58
FT /note="T->N: Reduced capacity to bind specific IgE leading
FT to attenuated allergic reactions in human; when associated
FT with P-11, V-31, C-113 and V-114."
FT /evidence="ECO:0000269|PubMed:16293967"
FT MUTAGEN 113
FT /note="T->C: Reduced capacity to bind specific IgE leading
FT to attenuated allergic reactions in human; when associated
FT with P-11, V-31, N-58 and V-114."
FT /evidence="ECO:0000269|PubMed:16293967"
FT MUTAGEN 114
FT /note="I->V: Reduced capacity to bind specific IgE leading
FT to attenuated allergic reactions in human; when associated
FT with P-11, V-31, N-58 and C-113."
FT /evidence="ECO:0000269|PubMed:16293967"
FT CONFLICT 17
FT /note="S -> P (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 112
FT /note="S -> A (in Ref. 2; CAA88833)"
FT /evidence="ECO:0000305"
FT CONFLICT 122
FT /note="T -> P (in Ref. 2; CAA88833)"
FT /evidence="ECO:0000305"
FT CONFLICT 140
FT /note="A -> G (in Ref. 2; CAA88833)"
FT /evidence="ECO:0000305"
FT CONFLICT 153
FT /note="D -> G (in Ref. 2; CAA88833)"
FT /evidence="ECO:0000305"
FT STRAND 3..14
FT /evidence="ECO:0007829|PDB:5MMU"
FT HELIX 16..24
FT /evidence="ECO:0007829|PDB:5MMU"
FT HELIX 27..34
FT /evidence="ECO:0007829|PDB:5MMU"
FT TURN 36..38
FT /evidence="ECO:0007829|PDB:5MMU"
FT STRAND 41..50
FT /evidence="ECO:0007829|PDB:5MMU"
FT STRAND 54..58
FT /evidence="ECO:0007829|PDB:5MMU"
FT STRAND 67..75
FT /evidence="ECO:0007829|PDB:5MMU"
FT TURN 77..79
FT /evidence="ECO:0007829|PDB:5MMU"
FT STRAND 81..89
FT /evidence="ECO:0007829|PDB:5MMU"
FT TURN 93..95
FT /evidence="ECO:0007829|PDB:5MMU"
FT STRAND 96..108
FT /evidence="ECO:0007829|PDB:5MMU"
FT STRAND 111..122
FT /evidence="ECO:0007829|PDB:5MMU"
FT HELIX 130..153
FT /evidence="ECO:0007829|PDB:5MMU"
FT TURN 155..158
FT /evidence="ECO:0007829|PDB:5MMU"
SQ SEQUENCE 159 AA; 17651 MW; 2E5447E3343098BE CRC64;
MGVYTFENEF TSEIPPSRLF KAFVLDADNL IPKIAPQAIK QAEILEGNGG PGTIKKITFG
EGSQYGYVKH RIDSIDEASY SYSYTLIEGD ALTDTIEKIS YETKLVACGS GSTIKSISHY
HTKGNIEIKE EHVKVGKEKA HGLFKLIESY LKDHPDAYN
