ALL1_APIGR
ID ALL1_APIGR Reviewed; 154 AA.
AC P49372;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 25-MAY-2022, entry version 82.
DE RecName: Full=Major allergen Api g 1, isoallergen 1;
DE AltName: Full=Allergen Api g 1.0101;
DE AltName: Full=Allergen Api g I;
DE AltName: Allergen=Api g 1;
OS Apium graveolens (Celery).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Apiales; Apiaceae; Apioideae; apioid superclade;
OC Apieae; Apium.
OX NCBI_TaxID=4045;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Bulb, and Leaf;
RX PubMed=7588792; DOI=10.1111/j.1432-1033.1995.484_2.x;
RA Breiteneder H., Hoffmann-Sommergruber K., O'Riordain G., Susani M.,
RA Ahorn H., Ebner C., Kraft D., Scheiner O.;
RT "Molecular characterization of Api g 1, the major allergen of celery (Apium
RT graveolens), and its immunological and structural relationships to a group
RT of 17-kDa tree pollen allergens.";
RL Eur. J. Biochem. 233:484-489(1995).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
RX PubMed=16051263; DOI=10.1016/j.jmb.2005.06.054;
RA Schirmer T., Hoffimann-Sommergrube K., Susani M., Breiteneder H.,
RA Markovic-Housley Z.;
RT "Crystal structure of the major celery allergen Api g 1: molecular analysis
RT of cross-reactivity.";
RL J. Mol. Biol. 351:1101-1109(2005).
CC -!- ALLERGEN: Causes an allergic reaction in human.
CC -!- SIMILARITY: Belongs to the BetVI family. {ECO:0000305}.
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DR EMBL; Z48967; CAA88831.1; -; mRNA.
DR PIR; S63984; S63984.
DR PDB; 2BK0; X-ray; 2.90 A; A/B=1-154.
DR PDBsum; 2BK0; -.
DR AlphaFoldDB; P49372; -.
DR SMR; P49372; -.
DR Allergome; 40; Api g 1.
DR Allergome; 41; Api g 1.0101.
DR EvolutionaryTrace; P49372; -.
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 SMART; SM01037; Bet_v_1; 1.
DR PROSITE; PS00451; PATHOGENESIS_BETVI; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Allergen; Pathogenesis-related protein; Plant defense.
FT CHAIN 1..154
FT /note="Major allergen Api g 1, isoallergen 1"
FT /id="PRO_0000154172"
FT STRAND 3..14
FT /evidence="ECO:0007829|PDB:2BK0"
FT HELIX 16..23
FT /evidence="ECO:0007829|PDB:2BK0"
FT HELIX 27..34
FT /evidence="ECO:0007829|PDB:2BK0"
FT HELIX 36..38
FT /evidence="ECO:0007829|PDB:2BK0"
FT STRAND 40..49
FT /evidence="ECO:0007829|PDB:2BK0"
FT STRAND 53..57
FT /evidence="ECO:0007829|PDB:2BK0"
FT STRAND 66..75
FT /evidence="ECO:0007829|PDB:2BK0"
FT TURN 76..79
FT /evidence="ECO:0007829|PDB:2BK0"
FT STRAND 80..88
FT /evidence="ECO:0007829|PDB:2BK0"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:2BK0"
FT TURN 92..94
FT /evidence="ECO:0007829|PDB:2BK0"
FT STRAND 95..106
FT /evidence="ECO:0007829|PDB:2BK0"
FT STRAND 112..123
FT /evidence="ECO:0007829|PDB:2BK0"
FT HELIX 130..153
FT /evidence="ECO:0007829|PDB:2BK0"
SQ SEQUENCE 154 AA; 16321 MW; 86C47DDB0A9B7ABB CRC64;
MGVQTHVLEL TSSVSAEKIF QGFVIDVDTV LPKAAPGAYK SVEIKGDGGP GTLKIITLPD
GGPITTMTLR IDGVNKEALT FDYSVIDGDI LLGFIESIEN HVVLVPTADG GSICKTTAIF
HTKGDAVVPE ENIKYANEQN TALFKALEAY LIAN
