KIWEL_ACTDE
ID KIWEL_ACTDE Reviewed; 213 AA.
AC P84527; L7TRW4; P83975; P83976;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-DEC-2018, sequence version 2.
DT 25-MAY-2022, entry version 49.
DE RecName: Full=Kiwellin {ECO:0000303|PubMed:16328735};
DE AltName: Allergen=Act d 5;
DE Contains:
DE RecName: Full=Kissper {ECO:0000303|PubMed:18186145};
DE Contains:
DE RecName: Full=KiTH-3 {ECO:0000303|PubMed:18442249};
DE Contains:
DE RecName: Full=KiTH-1 {ECO:0000303|PubMed:18442249};
DE Contains:
DE RecName: Full=KiTH-2 {ECO:0000303|PubMed:18442249};
DE Flags: Precursor;
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]
RP NUCLEOTIDE SEQUENCE [MRNA], AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=23289429; DOI=10.1021/jf304289f;
RA Maddumage R., Nieuwenhuizen N.J., Bulley S.M., Cooney J.M., Green S.A.,
RA Atkinson R.G.;
RT "Diversity and relative levels of actinidin, kiwellin, and thaumatin-like
RT allergens in 15 varieties of kiwifruit (Actinidia).";
RL J. Agric. Food Chem. 61:728-739(2013).
RN [2]
RP PROTEIN SEQUENCE OF 25-213, ALLERGEN, AND VARIANT HIS-85.
RC TISSUE=Fruit {ECO:0000269|PubMed:16328735};
RX PubMed=16328735; DOI=10.1007/s10930-005-7638-7;
RA Tamburrini M., Cerasuolo I., Carratore V., Stanziola A.A., Zofra S.,
RA Romano L., Camardella L., Ciardiello M.A.;
RT "Kiwellin, a novel protein from kiwi fruit. Purification, biochemical
RT characterization and identification as an allergen.";
RL Protein J. 24:423-429(2005).
RN [3]
RP PROTEIN SEQUENCE OF 25-63, AND FUNCTION.
RC TISSUE=Fruit {ECO:0000269|PubMed:18186145};
RX PubMed=18186145; DOI=10.1002/psc.992;
RA Ciardiello M.A., Meleleo D., Saviano G., Crescenzo R., Carratore V.,
RA Camardella L., Gallucci E., Micelli S., Tancredi T., Picone D.,
RA Tamburrini M.;
RT "Kissper, a kiwi fruit peptide with channel-like activity: structural and
RT functional features.";
RL J. Pept. Sci. 14:742-754(2008).
RN [4]
RP PROTEIN SEQUENCE OF 64-213, ALLERGEN, AND PROTEOLYTIC CLEAVAGE BY
RP ACTINIDIN.
RC STRAIN=cv. Hayward {ECO:0000269|PubMed:18442249};
RC TISSUE=Fruit {ECO:0000269|PubMed:18442249};
RX PubMed=18442249; DOI=10.1021/jf703620m;
RA Tuppo L., Giangrieco I., Palazzo P., Bernardi M.L., Scala E., Carratore V.,
RA Tamburrini M., Mari A., Ciardiello M.A.;
RT "Kiwellin, a modular protein from green and gold kiwi fruits: evidence of
RT in vivo and in vitro processing and IgE binding.";
RL J. Agric. Food Chem. 56:3812-3817(2008).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 25-213, DISULFIDE BONDS, AND
RP HYDROXYLATION AT PRO-65 AND PRO-67.
RX PubMed=26146952; DOI=10.1021/acs.jafc.5b02159;
RA Offermann L.R., Giangrieco I., Perdue M.L., Zuzzi S., Santoro M.,
RA Tamburrini M., Cosgrove D.J., Mari A., Ciardiello M.A., Chruszcz M.;
RT "Elusive structural, functional, and immunological features of Act d 5, the
RT green kiwifruit kiwellin.";
RL J. Agric. Food Chem. 63:6567-6576(2015).
CC -!- FUNCTION: [Kissper]: pH-dependent, voltage-gated and anion-selective
CC pore-forming peptide. {ECO:0000305|PubMed:18186145}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- PTM: Undergoes proteolytic cleavage by actinidin to produce kissper and
CC KiTH (PubMed:18442249). Three forms of KiTH are produced by cleavage at
CC different sites, the main form produced in vivo is KiTH-1
CC (PubMed:18442249). {ECO:0000269|PubMed:18442249}.
CC -!- ALLERGEN: Causes an allergic reaction in human (PubMed:16328735,
CC PubMed:18442249). Binds to IgE from the serum of kiwi-allergic
CC patients. {ECO:0000269|PubMed:16328735, ECO:0000269|PubMed:18442249}.
CC -!- SIMILARITY: Belongs to the kiwellin family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JX905292; AGC39166.1; -; mRNA.
DR PDB; 4X9U; X-ray; 2.10 A; A/B=25-213.
DR PDBsum; 4X9U; -.
DR AlphaFoldDB; P84527; -.
DR SMR; P84527; -.
DR Allergome; 2821; Act d 5.
DR Allergome; 3588; Act d 5.0101.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR Gene3D; 2.40.40.10; -; 1.
DR InterPro; IPR039271; Kiwellin-like.
DR InterPro; IPR036908; RlpA-like_sf.
DR PANTHER; PTHR33191; PTHR33191; 1.
DR SUPFAM; SSF50685; SSF50685; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Allergen; Direct protein sequencing; Disulfide bond;
KW Hydroxylation; Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000269|PubMed:16328735"
FT CHAIN 25..213
FT /note="Kiwellin"
FT /id="PRO_0000083396"
FT PEPTIDE 25..63
FT /note="Kissper"
FT /evidence="ECO:0000269|PubMed:18186145,
FT ECO:0000269|PubMed:18442249"
FT /id="PRO_0000318767"
FT CHAIN 62..213
FT /note="KiTH-3"
FT /evidence="ECO:0000269|PubMed:18442249"
FT /id="PRO_0000341246"
FT CHAIN 64..213
FT /note="KiTH-1"
FT /evidence="ECO:0000269|PubMed:18442249"
FT /id="PRO_0000341247"
FT CHAIN 66..213
FT /note="KiTH-2"
FT /evidence="ECO:0000269|PubMed:18442249"
FT /id="PRO_0000341248"
FT REGION 91..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 65
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:26146952"
FT MOD_RES 67
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:26146952"
FT DISULFID 28..60
FT /evidence="ECO:0000269|PubMed:26146952,
FT ECO:0007744|PDB:4X9U"
FT DISULFID 32..44
FT /evidence="ECO:0000269|PubMed:26146952,
FT ECO:0007744|PDB:4X9U"
FT DISULFID 38..49
FT /evidence="ECO:0000269|PubMed:26146952,
FT ECO:0007744|PDB:4X9U"
FT DISULFID 72..90
FT /evidence="ECO:0000269|PubMed:26146952,
FT ECO:0007744|PDB:4X9U"
FT DISULFID 80..172
FT /evidence="ECO:0000269|PubMed:26146952,
FT ECO:0007744|PDB:4X9U"
FT DISULFID 119..144
FT /evidence="ECO:0000269|PubMed:26146952,
FT ECO:0007744|PDB:4X9U"
FT DISULFID 166..172
FT /evidence="ECO:0000269|PubMed:26146952,
FT ECO:0007744|PDB:4X9U"
FT VARIANT 85
FT /note="Y -> H"
FT /evidence="ECO:0000269|PubMed:16328735"
FT CONFLICT 65..67
FT /note="PSP -> HSH (in Ref. 2; AA sequence)"
FT CONFLICT 113
FT /note="D -> G (in Ref. 1; AGC39166)"
FT /evidence="ECO:0000305"
FT CONFLICT 125
FT /note="N -> S (in Ref. 1; AGC39166)"
FT /evidence="ECO:0000305"
FT TURN 53..56
FT /evidence="ECO:0007829|PDB:4X9U"
FT TURN 59..62
FT /evidence="ECO:0007829|PDB:4X9U"
FT STRAND 76..79
FT /evidence="ECO:0007829|PDB:4X9U"
FT STRAND 84..87
FT /evidence="ECO:0007829|PDB:4X9U"
FT STRAND 98..104
FT /evidence="ECO:0007829|PDB:4X9U"
FT STRAND 111..117
FT /evidence="ECO:0007829|PDB:4X9U"
FT TURN 118..121
FT /evidence="ECO:0007829|PDB:4X9U"
FT STRAND 130..134
FT /evidence="ECO:0007829|PDB:4X9U"
FT HELIX 135..138
FT /evidence="ECO:0007829|PDB:4X9U"
FT HELIX 139..141
FT /evidence="ECO:0007829|PDB:4X9U"
FT TURN 142..145
FT /evidence="ECO:0007829|PDB:4X9U"
FT STRAND 147..151
FT /evidence="ECO:0007829|PDB:4X9U"
FT STRAND 157..166
FT /evidence="ECO:0007829|PDB:4X9U"
FT HELIX 174..176
FT /evidence="ECO:0007829|PDB:4X9U"
FT STRAND 184..189
FT /evidence="ECO:0007829|PDB:4X9U"
FT HELIX 191..196
FT /evidence="ECO:0007829|PDB:4X9U"
FT HELIX 201..203
FT /evidence="ECO:0007829|PDB:4X9U"
FT STRAND 205..212
FT /evidence="ECO:0007829|PDB:4X9U"
SQ SEQUENCE 213 AA; 22324 MW; 4778801902DB6E55 CRC64;
MAQLALLLLS LFLTLISLAP PGASISSCNG PCRDLNDCDG QLICIKGKCN DDPQVGTHIC
RGTTPSPQPG GCKPSGTLTC RGKSYPTYDC SPPVTSSTPA KLTNNDFSEG GDDGGPSECD
ESYHNNNERI VALSTGWYNG GSRCGKMIRI TASNGKSVSA KVVDECDSRH GCDKEHAGQP
PCRNNIVDGS NAVWSALGLD KNVGVVDITW SMA
