KIRO_ACTDE
ID KIRO_ACTDE Reviewed; 150 AA.
AC P85524;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 1.
DT 25-MAY-2022, entry version 29.
DE RecName: Full=Kirola {ECO:0000303|PubMed:21309790};
DE AltName: Allergen=Act d 11 {ECO:0000303|PubMed:21309790};
OS Actinidia deliciosa (Kiwi).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; Ericales; Actinidiaceae; Actinidia.
OX NCBI_TaxID=3627;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT THR-54.
RC TISSUE=Fruit {ECO:0000305};
RX PubMed=18655731; DOI=10.1186/1471-2164-9-351;
RA Crowhurst R.N., Gleave A.P., MacRae E.A., Ampomah-Dwamena C.,
RA Atkinson R.G., Beuning L.L., Bulley S.M., Chagne D., Marsh K.B.,
RA Matich A.J., Montefiori M., Newcomb R.D., Schaffer R.J., Usadel B.,
RA Allan A.C., Boldingh H.L., Bowen J.H., Davy M.W., Eckloff R.,
RA Ferguson A.R., Fraser L.G., Gera E., Hellens R.P., Janssen B.J., Klages K.,
RA Lo K.R., MacDiarmid R.M., Nain B., McNeilage M.A., Rassam M.,
RA Richardson A.C., Rikkerink E.H., Ross G.S., Schroder R., Snowden K.C.,
RA Souleyre E.J., Templeton M.D., Walton E.F., Wang D., Wang M.Y., Wang Y.Y.,
RA Wood M., Wu R., Yauk Y.K., Laing W.A.;
RT "Analysis of expressed sequence tags from Actinidia: applications of a
RT cross species EST database for gene discovery in the areas of flavor,
RT health, color and ripening.";
RL BMC Genomics 9:351-351(2008).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 2-118 AND 129-150, MASS SPECTROMETRY, ACETYLATION AT
RP MET-1, AND ALLERGENICITY.
RC TISSUE=Fruit {ECO:0000269|PubMed:21309790};
RX PubMed=21309790; DOI=10.1111/j.1398-9995.2011.02555.x;
RA D'Avino R., Bernardi M.L., Wallner M., Palazzo P., Camardella L., Tuppo L.,
RA Alessandri C., Breiteneder H., Ferreira F., Ciardiello M.A., Mari A.;
RT "Kiwifruit Act d 11 is the first member of the ripening-related protein
RT family identified as an allergen.";
RL Allergy 66:870-877(2011).
RN [3] {ECO:0000305}
RP MASS SPECTROMETRY.
RC TISSUE=Fruit {ECO:0000269|Ref.3};
RA D'Avino R., Camardella L., Ciardiello M.A., Tamburrini M., Carratore V.;
RT "Kirola, a new allergenic protein in kiwi fruit.";
RL Submitted (APR-2008) to UniProtKB.
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 1-150, SUBUNIT, AND MASS
RP SPECTROMETRY.
RC TISSUE=Fruit {ECO:0000303|PubMed:23969108};
RX PubMed=23969108; DOI=10.1016/j.molimm.2013.07.004;
RA Chruszcz M., Ciardiello M.A., Osinski T., Majorek K.A., Giangrieco I.,
RA Font J., Breiteneder H., Thalassinos K., Minor W.;
RT "Structural and bioinformatic analysis of the kiwifruit allergen Act d 11,
RT a member of the family of ripening-related proteins.";
RL Mol. Immunol. 56:794-803(2013).
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:23969108}.
CC -!- PTM: The N-terminus is blocked. {ECO:0000269|PubMed:21309790}.
CC -!- MASS SPECTROMETRY: Mass=17441; Method=MALDI;
CC Evidence={ECO:0000269|Ref.3};
CC -!- MASS SPECTROMETRY: Mass=17460; Method=MALDI; Note=Variant Thr-54.;
CC Evidence={ECO:0000269|PubMed:21309790};
CC -!- MASS SPECTROMETRY: Mass=17446.043; Mass_error=0.028;
CC Method=Electrospray; Evidence={ECO:0000269|PubMed:23969108};
CC -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE.
CC {ECO:0000269|PubMed:21309790}.
CC -!- SIMILARITY: Belongs to the MLP family. {ECO:0000255}.
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DR EMBL; FG437290; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; FG440357; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; FG445803; -; NOT_ANNOTATED_CDS; mRNA.
DR PDB; 4IGV; X-ray; 1.50 A; A=1-150.
DR PDB; 4IGW; X-ray; 2.55 A; A/B=1-150.
DR PDB; 4IGX; X-ray; 2.35 A; A/B/C/D=1-150.
DR PDB; 4IGY; X-ray; 2.92 A; A/B/C/D=1-150.
DR PDB; 4IH0; X-ray; 1.75 A; A=1-150.
DR PDB; 4IH2; X-ray; 2.00 A; A=1-150.
DR PDB; 4IHR; X-ray; 1.60 A; A=1-150.
DR PDBsum; 4IGV; -.
DR PDBsum; 4IGW; -.
DR PDBsum; 4IGX; -.
DR PDBsum; 4IGY; -.
DR PDBsum; 4IH0; -.
DR PDBsum; 4IH2; -.
DR PDBsum; 4IHR; -.
DR AlphaFoldDB; P85524; -.
DR SMR; P85524; -.
DR Allergome; 5903; Act d 11.
DR Allergome; 6135; Act d 11.0101.
DR iPTMnet; P85524; -.
DR GO; GO:0002253; P:activation of immune response; IDA:UniProtKB.
DR GO; GO:0006952; P:defense response; IEA:InterPro.
DR Gene3D; 3.30.530.20; -; 1.
DR InterPro; IPR000916; Bet_v_I/MLP.
DR InterPro; IPR023393; START-like_dom_sf.
DR Pfam; PF00407; Bet_v_1; 1.
DR SMART; SM01037; Bet_v_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Allergen; Direct protein sequencing.
FT CHAIN 1..150
FT /note="Kirola"
FT /id="PRO_0000407853"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|PubMed:21309790"
FT VARIANT 54
FT /note="S -> T"
FT /evidence="ECO:0000269|PubMed:18655731,
FT ECO:0000269|PubMed:21309790"
FT STRAND 4..12
FT /evidence="ECO:0007829|PDB:4IGV"
FT HELIX 17..25
FT /evidence="ECO:0007829|PDB:4IGV"
FT HELIX 30..34
FT /evidence="ECO:0007829|PDB:4IGV"
FT TURN 36..38
FT /evidence="ECO:0007829|PDB:4IGV"
FT STRAND 39..47
FT /evidence="ECO:0007829|PDB:4IGV"
FT STRAND 55..62
FT /evidence="ECO:0007829|PDB:4IGV"
FT STRAND 65..77
FT /evidence="ECO:0007829|PDB:4IGV"
FT TURN 78..81
FT /evidence="ECO:0007829|PDB:4IGV"
FT STRAND 82..90
FT /evidence="ECO:0007829|PDB:4IGV"
FT HELIX 91..94
FT /evidence="ECO:0007829|PDB:4IGV"
FT STRAND 96..107
FT /evidence="ECO:0007829|PDB:4IGV"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:4IGX"
FT STRAND 112..124
FT /evidence="ECO:0007829|PDB:4IGV"
FT HELIX 131..145
FT /evidence="ECO:0007829|PDB:4IGV"
FT TURN 146..148
FT /evidence="ECO:0007829|PDB:4IGV"
SQ SEQUENCE 150 AA; 17404 MW; E5D429C4B5605898 CRC64;
MDLSGKMVKQ VEILSDGIVF YEIFRYRLYL ISEMSPVNIQ GVDLLEGNWG TVGSVIFFKY
TIDGKEKTAK DIVEAIDEET KSVTFKIVEG DLMELYKTFI IIVQVDTKGE HNSVTWTFHY
EKLKEDVEEP NTLMNFCIEI TKDIETYHLK