ID   KIWEL_ACTCC             Reviewed;         213 AA.
AC   P85261; A0A2R6P7K4; L7TT83;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2019, sequence version 2.
DT   02-SEP-2026, entry version 34.
DE   RecName: Full=Kiwellin;
DE   AltName: Allergen=Act c 5;
DE   Contains:
DE     RecName: Full=Kissper;
DE   Contains:
DE     RecName: Full=KiTH-3;
DE   Contains:
DE     RecName: Full=KiTH-1;
DE   Contains:
DE     RecName: Full=KiTH-2;
DE   Flags: Precursor;
GN   Name=KWL1 {ECO:0000303|PubMed:23289429};
GN   ORFNames=CEY00_Acc32202 {ECO:0000312|EMBL:PSR86579.1};
OS   Actinidia chinensis var. chinensis (Chinese soft-hair kiwi).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; Ericales; Actinidiaceae; Actinidia.
OX   NCBI_TaxID=1590841;
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   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Red5;
RX   PubMed=29661190; DOI=10.1186/s12864-018-4656-3;
RA   Pilkington S.M., Crowhurst R., Hilario E., Nardozza S., Fraser L., Peng Y.,
RA   Gunaseelan K., Simpson R., Tahir J., Deroles S.C., Templeton K., Luo Z.,
RA   Davy M., Cheng C., McNeilage M., Scaglione D., Liu Y., Zhang Q., Datson P.,
RA   De Silva N., Gardiner S.E., Bassett H., Chagne D., McCallum J.,
RA   Dzierzon H., Deng C., Wang Y.Y., Barron L., Manako K., Bowen J.,
RA   Foster T.M., Erridge Z.A., Tiffin H., Waite C.N., Davies K.M.,
RA   Grierson E.P., Laing W.A., Kirk R., Chen X., Wood M., Montefiori M.,
RA   Brummell D.A., Schwinn K.E., Catanach A., Fullerton C., Li D.,
RA   Meiyalaghan S., Nieuwenhuizen N., Read N., Prakash R., Hunter D., Zhang H.,
RA   McKenzie M., Knabel M., Harris A., Allan A.C., Gleave A., Chen A.,
RA   Janssen B.J., Plunkett B., Ampomah-Dwamena C., Voogd C., Leif D.,
RA   Lafferty D., Souleyre E.J.F., Varkonyi-Gasic E., Gambi F., Hanley J.,
RA   Yao J.L., Cheung J., David K.M., Warren B., Marsh K., Snowden K.C.,
RA   Lin-Wang K., Brian L., Martinez-Sanchez M., Wang M., Ileperuma N.,
RA   Macnee N., Campin R., McAtee P., Drummond R.S.M., Espley R.V.,
RA   Ireland H.S., Wu R., Atkinson R.G., Karunairetnam S., Bulley S.,
RA   Chunkath S., Hanley Z., Storey R., Thrimawithana A.H., Thomson S.,
RA   David C., Testolin R., Huang H., Hellens R.P., Schaffer R.J.;
RT   "A manually annotated Actinidia chinensis var. chinensis (kiwifruit) genome
RT   highlights the challenges associated with draft genomes and gene prediction
RT   in plants.";
RL   BMC Genomics 19:257-257(2018).
RN   [3] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 25-44 AND 62-75, ALLERGEN, AND PROTEOLYTIC CLEAVAGE BY
RP   ACTINIDIN.
RC   STRAIN=cv. Hort 16A {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   [4]
RP   X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 25-213, AND DISULFIDE BONDS.
RX   PubMed=25093947; DOI=10.1016/j.jsb.2014.07.005;
RA   Hamiaux C., Maddumage R., Middleditch M.J., Prakash R., Brummell D.A.,
RA   Baker E.N., Atkinson R.G.;
RT   "Crystal structure of kiwellin, a major cell-wall protein from kiwifruit.";
RL   J. Struct. Biol. 187:276-281(2014).
CC   -!- FUNCTION: Kissper is an anion-selective pore-forming peptide.
CC       {ECO:0000250|UniProtKB:P84527}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P84527}.
CC   -!- PTM: Undergoes proteolytic cleavage by actinidin to produce kissper and
CC       KiTH. Three forms of KiTH are produced by cleavage at different sites.
CC       {ECO:0000269|PubMed:18442249}.
CC   -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE from the
CC       serum of kiwi-allergic patients. {ECO:0000269|PubMed:18442249}.
CC   -!- SIMILARITY: Belongs to the kiwellin family. {ECO:0000255}.
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DR   EMBL; JX905294; AGC39168.1; -; mRNA.
DR   EMBL; NKQK01000028; PSR86579.1; -; Genomic_DNA.
DR   PDB; 4PMK; X-ray; 2.05 A; A/B=25-213.
DR   AlphaFoldDB; P85261; -.
DR   SMR; P85261; -.
DR   STRING; 1590841.P85261; -.
DR   Allergome; 11668; Act c 5.0102.
DR   Allergome; 4062; Act c 5.
DR   Allergome; 5734; Act c 5.0101.
DR   EnsemblPlants; PSR86579; PSR86579; CEY00_Acc32202.
DR   Gramene; PSR86579; PSR86579; CEY00_Acc32202.
DR   InParanoid; P85261; -.
DR   OMA; SVNGCDR; -.
DR   OrthoDB; 406505at2759; -.
DR   EvolutionaryTrace; P85261; -.
DR   Proteomes; UP000241394; Chromosome LG28.
DR   GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR   CDD; cd22270; DPBB_kiwellin-like; 1.
DR   Gene3D; 2.40.40.10; RlpA-like domain; 1.
DR   InterPro; IPR039271; Kiwellin-like.
DR   InterPro; IPR036908; RlpA-like_sf.
DR   PANTHER; PTHR33191; RIPENING-RELATED PROTEIN 2-RELATED; 1.
DR   PANTHER; PTHR33191:SF9; RIPENING-RELATED PROTEIN 2-RELATED; 1.
DR   Pfam; PF24300; KWL1; 1.
DR   SUPFAM; SSF50685; Barwin-like endoglucanases; 1.
DR   PDBsum; 4PMK; -.
PE   1: Evidence at protein level;
KW   3D-structure; Allergen; Direct protein sequencing; Disulfide bond;
KW   Hydroxylation; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000269|PubMed:18442249"
FT   CHAIN           25..213
FT                   /note="Kiwellin"
FT                   /id="PRO_0000343453"
FT   PEPTIDE         25..63
FT                   /note="Kissper"
FT                   /evidence="ECO:0000269|PubMed:18442249"
FT                   /id="PRO_0000343454"
FT   CHAIN           62..213
FT                   /note="KiTH-3"
FT                   /evidence="ECO:0000269|PubMed:18442249"
FT                   /id="PRO_0000343455"
FT   CHAIN           64..213
FT                   /note="KiTH-1"
FT                   /evidence="ECO:0000269|PubMed:18442249"
FT                   /id="PRO_0000343456"
FT   CHAIN           66..213
FT                   /note="KiTH-2"
FT                   /evidence="ECO:0000269|PubMed:18442249"
FT                   /id="PRO_0000343457"
FT   REGION          91..121
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        93..107
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         65
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000250|UniProtKB:P84527"
FT   MOD_RES         67
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000250|UniProtKB:P84527"
FT   DISULFID        28..60
FT                   /evidence="ECO:0000250|UniProtKB:P84527"
FT   DISULFID        32..44
FT                   /evidence="ECO:0000250|UniProtKB:P84527"
FT   DISULFID        38..49
FT                   /evidence="ECO:0000250|UniProtKB:P84527"
FT   DISULFID        72..90
FT                   /evidence="ECO:0000269|PubMed:25093947,
FT                   ECO:0007744|PDB:4PMK"
FT   DISULFID        80..172
FT                   /evidence="ECO:0000269|PubMed:25093947,
FT                   ECO:0007744|PDB:4PMK"
FT   DISULFID        119..144
FT                   /evidence="ECO:0000269|PubMed:25093947,
FT                   ECO:0007744|PDB:4PMK"
FT   DISULFID        166..182
FT                   /evidence="ECO:0000269|PubMed:25093947,
FT                   ECO:0007744|PDB:4PMK"
FT   CONFLICT        8
FT                   /note="V -> L (in Ref. 1; AGC39168)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        46
FT                   /note="E -> K (in Ref. 1; AGC39168)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        81
FT                   /note="R -> Q (in Ref. 1; AGC39168)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        165
FT                   /note="K -> E (in Ref. 1; AGC39168)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        200
FT                   /note="D -> N (in Ref. 1; AGC39168)"
FT                   /evidence="ECO:0000305"
FT   TURN            53..56
FT                   /evidence="ECO:0007829|PDB:4PMK"
FT   TURN            59..62
FT                   /evidence="ECO:0007829|PDB:4PMK"
FT   STRAND          76..79
FT                   /evidence="ECO:0007829|PDB:4PMK"
FT   STRAND          84..87
FT                   /evidence="ECO:0007829|PDB:4PMK"
FT   HELIX           92..94
FT                   /evidence="ECO:0007829|PDB:4PMK"
FT   STRAND          98..104
FT                   /evidence="ECO:0007829|PDB:4PMK"
FT   STRAND          108..113
FT                   /evidence="ECO:0007829|PDB:4PMK"
FT   TURN            118..121
FT                   /evidence="ECO:0007829|PDB:4PMK"
FT   STRAND          130..134
FT                   /evidence="ECO:0007829|PDB:4PMK"
FT   HELIX           135..138
FT                   /evidence="ECO:0007829|PDB:4PMK"
FT   HELIX           139..141
FT                   /evidence="ECO:0007829|PDB:4PMK"
FT   TURN            142..145
FT                   /evidence="ECO:0007829|PDB:4PMK"
FT   STRAND          147..152
FT                   /evidence="ECO:0007829|PDB:4PMK"
FT   STRAND          157..166
FT                   /evidence="ECO:0007829|PDB:4PMK"
FT   TURN            174..178
FT                   /evidence="ECO:0007829|PDB:4PMK"
FT   HELIX           179..182
FT                   /evidence="ECO:0007829|PDB:4PMK"
FT   STRAND          184..189
FT                   /evidence="ECO:0007829|PDB:4PMK"
FT   HELIX           191..196
FT                   /evidence="ECO:0007829|PDB:4PMK"
FT   HELIX           201..203
FT                   /evidence="ECO:0007829|PDB:4PMK"
FT   STRAND          206..212
FT                   /evidence="ECO:0007829|PDB:4PMK"
SQ   SEQUENCE   213 AA;  22242 MW;  67660BF64A4386BC CRC64;
     MAQLSLLVLS LFLTLISLPP PGASISSCNG PCRDLNDCDG QLICIEGKCN DDPEVGTHIC
     RGTTPSPQPG GCKPSGTLTC RGKSHPTYDC SPPVTSSTPA KLTNNDFSEG GDGGGPSECD
     ESYHSNNERI VALSTGWYNG GSRCGKMIRI TASNGKSVSA KVVDKCDSRH GCDKEHAGQP
     PCRNNIVDGS NAVWSALGLD KNVGVVDITW SMA
//