ID   ACTN_ACTDE              Reviewed;         380 AA.
AC   A5HII1; Q43367; Q96227;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   RecName: Full=Actinidain {ECO:0000250|UniProtKB:P00785, ECO:0000312|EMBL:ABQ10189.1};
DE            Short=Actinidin {ECO:0000250|UniProtKB:P00785, ECO:0000312|EMBL:ABQ10189.1};
DE            EC=3.4.22.14 {ECO:0000250|UniProtKB:P00785};
DE   AltName: Full=Allergen Act d 1;
DE   AltName: Allergen=Act d 1;
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] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2813065; DOI=10.1093/nar/17.20.8363;
RA   Podivinsky E., Forster R.L.S., Gardner R.C.;
RT   "Nucleotide sequence of actinidin, a kiwi fruit protease.";
RL   Nucleic Acids Res. 17:8363-8363(1989).
RN   [2] {ECO:0000312|EMBL:AAA32629.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Hayward {ECO:0000312|EMBL:AAA32629.1};
RX   PubMed=2251128; DOI=10.1093/nar/18.22.6684;
RA   Snowden K.C., Gardner R.C.;
RT   "Nucleotide sequence of an actinidin genomic clone.";
RL   Nucleic Acids Res. 18:6684-6684(1990).
RN   [3] {ECO:0000305, ECO:0000312|EMBL:ABQ10189.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC   STRAIN=cv. Hayward {ECO:0000269|Ref.3};
RA   Nieuwenhuizen N.J., Beuning L.L., Sutherland P.W., Sharma N.N.,
RA   Cooney J.M., Bieleski L.R.F., Schroeder R., MacRae E.A., Atkinson R.G.;
RT   "Identification and characterisation of acidic and novel basic forms of
RT   actinidin, the highly abundant cysteine protease from kiwifruit.";
RL   Funct. Plant Biol. 34:946-961(2007).
RN   [4] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-13.
RX   PubMed=2102886; DOI=10.1007/bf00016129;
RA   Keeling J., Maxwell P., Gardner R.C.;
RT   "Nucleotide sequence of the promoter region from kiwifruit actinidin
RT   genes.";
RL   Plant Mol. Biol. 15:787-788(1990).
RN   [5] {ECO:0000305, ECO:0000312|EMBL:AAA32630.1}
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 70-380.
RC   STRAIN=cv. Exbury;
RA   Praekelt U.M., McKee R.A., Smith H.;
RL   Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases.
RN   [6] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 127-136, AND FUNCTION.
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   [7] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 127-131, AND ALLERGEN.
RC   STRAIN=cv. Hayward {ECO:0000269|PubMed:15536427};
RC   TISSUE=Fruit {ECO:0000269|PubMed:15536427};
RX   PubMed=15536427; DOI=10.1016/j.jaci.2004.07.016;
RA   Bublin M., Mari A., Ebner C., Knulst A., Scheiner O.,
RA   Hoffmann-Sommergruber K., Breiteneder H., Radauer C.;
RT   "IgE sensitization profiles toward green and gold kiwifruits differ among
RT   patients allergic to kiwifruit from 3 European countries.";
RL   J. Allergy Clin. Immunol. 114:1169-1175(2004).
RN   [8] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 127-131, AND ALLERGEN.
RC   STRAIN=cv. Hayward {ECO:0000269|PubMed:18205857};
RC   TISSUE=Fruit {ECO:0000269|PubMed:18205857};
RX   PubMed=18205857; DOI=10.1111/j.1365-2222.2007.02927.x;
RA   Palacin A., Rodriguez J., Blanco C., Lopez-Torrejon G., Sanchez-Monge R.,
RA   Varela J., Jimenez M.A., Cumplido J., Carrillo T., Crespo J.F., Salcedo G.;
RT   "Immunoglobulin E recognition patterns to purified Kiwifruit (Actinidinia
RT   deliciosa) allergens in patients sensitized to Kiwi with different clinical
RT   symptoms.";
RL   Clin. Exp. Allergy 38:1220-1228(2008).
CC   -!- FUNCTION: Cysteine protease responsible for the cleavage of kiwellin
CC       into kissper and KiTH. {ECO:0000269|PubMed:18442249}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Specificity close to that of papain.; EC=3.4.22.14;
CC         Evidence={ECO:0000250|UniProtKB:P00785};
CC   -!- TISSUE SPECIFICITY: Fruit, present in small cells of the outer pericarp
CC       of mature fruit, but not large cells. {ECO:0000269|Ref.3}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in ripening fruit, levels are highest at
CC       the harvest of fruit and decrease as the fruit ripens.
CC       {ECO:0000269|Ref.3}.
CC   -!- ALLERGEN: Causes an allergic reaction in human. Binds IgE.
CC       {ECO:0000269|PubMed:15536427, ECO:0000269|PubMed:18205857}.
CC   -!- SIMILARITY: Belongs to the peptidase C1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU10088, ECO:0000255|PROSITE-ProRule:PRU10089,
CC       ECO:0000255|PROSITE-ProRule:PRU10090}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA32630.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; X16466; CAA34486.1; -; mRNA.
DR   EMBL; M38422; AAA32629.1; -; Genomic_DNA.
DR   EMBL; EF530131; ABQ10189.1; -; mRNA.
DR   EMBL; X57551; CAA40778.1; -; Genomic_DNA.
DR   EMBL; M21335; AAA32630.1; ALT_FRAME; mRNA.
DR   AlphaFoldDB; A5HII1; -.
DR   SMR; A5HII1; -.
DR   Allergome; 1; Act d 1.
DR   MEROPS; C01.007; -.
DR   MEROPS; I29.003; -.
DR   BRENDA; 3.4.22.14; 121.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd02248; Peptidase_C1A; 1.
DR   Gene3D; 1.10.287.2250; -; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR025661; Pept_asp_AS.
DR   InterPro; IPR000169; Pept_cys_AS.
DR   InterPro; IPR025660; Pept_his_AS.
DR   InterPro; IPR013128; Peptidase_C1A.
DR   InterPro; IPR000668; Peptidase_C1A_C.
DR   InterPro; IPR039417; Peptidase_C1A_papain-like.
DR   InterPro; IPR013201; Prot_inhib_I29.
DR   PANTHER; PTHR12411; CYSTEINE PROTEASE FAMILY C1-RELATED; 1.
DR   PANTHER; PTHR12411:SF937; CYSTEINE PROTEINASE RD21A; 1.
DR   Pfam; PF08246; Inhibitor_I29; 1.
DR   Pfam; PF00112; Peptidase_C1; 1.
DR   PRINTS; PR00705; PAPAIN.
DR   SMART; SM00848; Inhibitor_I29; 1.
DR   SMART; SM00645; Pept_C1; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN; 1.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
PE   1: Evidence at protein level;
KW   Allergen; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW   Hydrolase; Protease; Signal; Thiol protease; Zymogen.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   PROPEP          25..126
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000269|PubMed:15536427,
FT                   ECO:0000269|PubMed:18205857, ECO:0000269|PubMed:18442249"
FT                   /id="PRO_0000343461"
FT   CHAIN           127..380
FT                   /note="Actinidain"
FT                   /evidence="ECO:0000269|PubMed:18442249"
FT                   /id="PRO_0000343462"
FT   ACT_SITE        151
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10088"
FT   ACT_SITE        288
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10089"
FT   ACT_SITE        308
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10090"
FT   CARBOHYD        29
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        81
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        111
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        148..191
FT                   /evidence="ECO:0000250|UniProtKB:P00785"
FT   DISULFID        182..224
FT                   /evidence="ECO:0000250|UniProtKB:P00785"
FT   DISULFID        282..332
FT                   /evidence="ECO:0000250|UniProtKB:P00785"
FT   CONFLICT        96
FT                   /note="D -> G (in Ref. 5; AAA32630)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        108
FT                   /note="S -> G (in Ref. 5; AAA32630)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        123
FT                   /note="V -> F (in Ref. 5; AAA32630)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        124
FT                   /note="G -> S (in Ref. 5; AAA32630)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        181
FT                   /note="D -> G (in Ref. 5; AAA32630)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        184
FT                   /note="R -> G (in Ref. 5; AAA32630)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        212
FT                   /note="E -> G (in Ref. 5; AAA32630)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        226..227
FT                   /note="LD -> VE (in Ref. 2; AAA32629)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        240
FT                   /note="E -> G (in Ref. 5; AAA32630)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        272
FT                   /note="H -> Q (in Ref. 2; AAA32629)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        307
FT                   /note="K -> E (in Ref. 5; AAA32630)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        349
FT                   /note="H -> Y (in Ref. 2; AAA32629 and 5; AAA32630)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        351
FT                   /note="K -> E (in Ref. 2; AAA32629)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        360
FT                   /note="P -> S (in Ref. 5; AAA32630)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        373
FT                   /note="D -> E (in Ref. 2; AAA32629 and 5; AAA32630)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   380 AA;  42110 MW;  70FDAD2235388224 CRC64;
     MGLPKSFVSM SLLFFSTLLI LSLAFNAKNL TQRTNDEVKA MYESWLIKYG KSYNSLGEWE
     RRFEIFKETL RFIDEHNADT NRSYKVGLNQ FADLTDEEFR STYLGFTSGS NKTKVSNRYE
     PRVGQVLPSY VDWRSAGAVV DIKSQGECGG CWAFSAIATV EGINKIVTGV LISLSEQELI
     DCGRTQNTRG CNGGYITDGF QFIINNGGIN TEENYPYTAQ DGECNLDLQN EKYVTIDTYE
     NVPYNNEWAL QTAVTYQPVS VALDAAGDAF KHYSSGIFTG PCGTAIDHAV TIVGYGTEGG
     IDYWIVKNSW DTTWGEEGYM RILRNVGGAG TCGIATMPSY PVKYNNQNHP KPYSSLINPP
     AFSMSKDGPV GVDDGQRYSA
//