KIWEL_ACTCC
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 25-MAY-2022, entry version 23.
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 PDBsum; 4PMK; -.
DR AlphaFoldDB; P85261; -.
DR SMR; 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 OMA; RDLNDCD; -.
DR Proteomes; UP000241394; Chromosome lg28.
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; 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..122
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: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..55
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 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 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
