ACTN_ACTDE
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 03-AUG-2022, entry version 46.
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;
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};
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; 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 PRIDE; A5HII1; -.
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 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; IPR000668; Peptidase_C1A_C.
DR InterPro; IPR039417; Peptidase_C1A_papain-like.
DR InterPro; IPR013201; Prot_inhib_I29.
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; SSF54001; 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; Hydrolase; Protease;
KW 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:0000250|UniProtKB:P00785"
FT ACT_SITE 288
FT /evidence="ECO:0000250|UniProtKB:P00785"
FT ACT_SITE 308
FT /evidence="ECO:0000250|UniProtKB:P00785"
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
