ID ACTN_ACTCC Reviewed; 380 AA. AC P00785; A0A2R6QY08; A0A3G9DHM4; E5D7U1; E5D7U2; Q9AXD2; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 13-NOV-2019, sequence version 5. DT 02-SEP-2026, entry version 139. DE RecName: Full=Actinidain; DE Short=Actinidin; DE EC=3.4.22.14 {ECO:0000269|PubMed:18442249}; DE AltName: Allergen=Act c 1; DE Flags: Precursor; GN Name=ACT1A {ECO:0000303|PubMed:22039217}; GN ORFNames=CEY00_Acc12058 {ECO:0000312|EMBL:PSS17271.1}; 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 [GENOMIC DNA / MRNA]. RX PubMed=22039217; DOI=10.1104/pp.111.187989; RA Nieuwenhuizen N.J., Maddumage R., Tsang G.K., Fraser L.G., Cooney J.M., RA De Silva H.N., Green S., Richardson K.A., Atkinson R.G.; RT "Mapping, complementation, and targets of the cysteine protease actinidin RT in kiwifruit."; RL Plant Physiol. 158:376-388(2012). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX DOI=10.2503/hortj.OKD-133; RA Kamiyoshihara Y., Nakamura T., Itagaki Y., Asada S., Aoki T., Mizuno S., RA Watanabe K., Inoue H., Tateishi A.; RT "Differential constitution in promoter region leads to a phenotype with a RT lower allergic actinidin level in yellow-fleshed kiwifruit (Actinidia RT chinensis)."; RL Hort. J. 87:288-296(2018). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Lee N.K., Hahm Y.T.; RT "Isolation and expression in E. coli of actinidin gene from Chinese wild RT kiwifruit."; RL Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases. RN [4] 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 [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 70-380, TISSUE SPECIFICITY, AND DEVELOPMENTAL RP STAGE. RX AGRICOLA=IND92000625; DOI=10.1007/BF00027396; RA Praekelt U.M., McKee R.A., Smith H.; RT "Molecular analysis of actinidin, the cysteine proteinase of Actinidia RT chinesis."; RL Plant Mol. Biol. 10:193-202(1988). RN [6] RP PROTEIN SEQUENCE OF 127-346. RX PubMed=687380; DOI=10.1042/bj1730073; RA Carne A., Moore C.H.; RT "The amino acid sequence of the tryptic peptides from actinidin, a RT proteolytic enzyme from the fruit of Actinidia chinensis."; RL Biochem. J. 173:73-83(1978). RN [7] RP PROTEIN SEQUENCE OF 127-136, FUNCTION, AND CATALYTIC ACTIVITY. RC STRAIN=cv. Hort 16A; TISSUE=Fruit; 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 [8] RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 127-346, DISULFIDE BONDS, AND RP SEQUENCE REVISION. RX PubMed=7003158; DOI=10.1016/0022-2836(80)90255-7; RA Baker E.N.; RT "Structure of actinidin, after refinement at 1.7-A resolution."; RL J. Mol. Biol. 141:441-484(1980). RN [9] RP X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS) OF 127-344 IN COMPLEX WITH E64, RP DISULFIDE BONDS, AND ACTIVITY REGULATION. RX PubMed=1606141; DOI=10.1021/bi00137a012; RA Varughese K.I., Su Y., Cromwell D., Hasnain S., Xuong N.H.; RT "Crystal structure of an actinidin-E-64 complex."; RL Biochemistry 31:5172-5176(1992). 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:0000269|PubMed:18442249}; CC -!- ACTIVITY REGULATION: Repressed by the active-site-directed cysteine CC protease inhibitor E64 (L-trans-epoxysuccinyl-leucylamide-(4-guanido)- CC butane) produced by Aspergillus japonicus. CC {ECO:0000269|PubMed:1606141}. CC -!- TISSUE SPECIFICITY: Fruit. {ECO:0000269|Ref.5}. CC -!- DEVELOPMENTAL STAGE: Levels of mRNA accumulate during early fruit CC development. {ECO:0000269|Ref.5}. CC -!- ALLERGEN: Causes an allergic reaction in human. 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=CAA31435.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=CAA31529.1; 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; GU201520; ADQ85985.1; -; Genomic_DNA. DR EMBL; GU201528; ADQ85986.1; -; mRNA. DR EMBL; LC330913; BBA83994.1; -; Genomic_DNA. DR EMBL; AF343446; AAK06862.1; -; mRNA. DR EMBL; NKQK01000011; PSS17271.1; -; Genomic_DNA. DR EMBL; X13013; CAA31435.1; ALT_FRAME; mRNA. DR EMBL; X13139; CAA31529.1; ALT_FRAME; mRNA. DR PDB; 1AEC; X-ray; 1.86 A; A=127-344. DR PDB; 2ACT; X-ray; 1.70 A; A=127-346. DR AlphaFoldDB; P00785; -. DR SMR; P00785; -. DR STRING; 1590841.P00785; -. DR Allergome; 1; Act d 1. DR Allergome; 3052; Act d 1.0101. DR MEROPS; C01.007; -. DR MEROPS; I29.003; -. DR EnsemblPlants; PSS17271; PSS17271; CEY00_Acc12058. DR Gramene; PSS17271; PSS17271; CEY00_Acc12058. DR InParanoid; P00785; -. DR OMA; FEKWIAM; -. DR OrthoDB; 10253408at2759; -. DR BRENDA; 3.4.22.14; 120. DR EvolutionaryTrace; P00785; -. DR Proteomes; UP000241394; Chromosome LG11. DR GO; GO:0004197; F:cysteine-type endopeptidase activity; EXP:UniProtKB. DR GO; GO:0006508; P:proteolysis; IEA:InterPro. DR CDD; cd02248; Peptidase_C1A; 1. DR FunFam; 3.90.70.10:FF:000068; Cysteine protease 1; 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 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. DR PDBsum; 1AEC; -. DR PDBsum; 2ACT; -. PE 1: Evidence at protein level; KW 3D-structure; Allergen; Direct protein sequencing; Disulfide bond; KW Hydrolase; Protease; Reference proteome; 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:18442249, FT ECO:0000269|PubMed:687380" FT /id="PRO_0000026398" FT CHAIN 127..380 FT /note="Actinidain" FT /id="PRO_0000026399" FT ACT_SITE 151 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10088, FT ECO:0000305|PubMed:1606141, ECO:0007744|PDB:1AEC" FT ACT_SITE 288 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10089" FT ACT_SITE 308 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10090" FT BINDING 151 FT /ligand="E64" FT /ligand_id="ChEBI:CHEBI:192370" FT /ligand_note="inhibitor; produced by Aspergillus japonicus" FT /note="covalent" FT /evidence="ECO:0000269|PubMed:1606141, FT ECO:0007744|PDB:1AEC" FT DISULFID 148..191 FT /evidence="ECO:0000269|PubMed:1606141, FT ECO:0000269|PubMed:7003158, ECO:0007744|PDB:1AEC, FT ECO:0007744|PDB:2ACT" FT DISULFID 182..224 FT /evidence="ECO:0000269|PubMed:1606141, FT ECO:0000269|PubMed:7003158, ECO:0007744|PDB:1AEC, FT ECO:0007744|PDB:2ACT" FT DISULFID 282..332 FT /evidence="ECO:0000269|PubMed:1606141, FT ECO:0000269|PubMed:7003158, ECO:0007744|PDB:1AEC, FT ECO:0007744|PDB:2ACT" FT CONFLICT 27 FT /note="A -> T (in Ref. 1; ADQ85985)" FT /evidence="ECO:0000305" FT CONFLICT 96 FT /note="D -> G (in Ref. 5; CAA31435)" FT /evidence="ECO:0000305" FT CONFLICT 108 FT /note="S -> G (in Ref. 5; CAA31435)" FT /evidence="ECO:0000305" FT CONFLICT 118 FT /note="Q -> R (in Ref. 1; ADQ85985/ADQ85986)" FT /evidence="ECO:0000305" FT CONFLICT 124 FT /note="G -> S (in Ref. 5; CAA31435)" FT /evidence="ECO:0000305" FT CONFLICT 167..170 FT /note="VTGV -> TSGS (in Ref. 6; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 181 FT /note="D -> G (in Ref. 5; CAA31435)" FT /evidence="ECO:0000305" FT CONFLICT 184 FT /note="R -> G (in Ref. 5; CAA31435)" FT /evidence="ECO:0000305" FT CONFLICT 192 FT /note="N -> D (in Ref. 6; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 193..194 FT /note="VG -> GS (in Ref. 1; ADQ85986)" FT /evidence="ECO:0000305" FT CONFLICT 193 FT /note="V -> G (in Ref. 1; ADQ85985)" FT /evidence="ECO:0000305" FT CONFLICT 201 FT /note="Q -> P (in Ref. 1; ADQ85986)" FT /evidence="ECO:0000305" FT CONFLICT 206 FT /note="N -> D (in Ref. 6; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 212 FT /note="E -> G (in Ref. 5; CAA31435)" FT /evidence="ECO:0000305" FT CONFLICT 223 FT /note="E -> D (in Ref. 6; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 225 FT /note="N -> D (in Ref. 6; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 226 FT /note="V -> L (in Ref. 5; CAA31435)" FT /evidence="ECO:0000305" FT CONFLICT 227 FT /note="D -> A (in Ref. 6; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 230..231 FT /note="NE -> DQ (in Ref. 6; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 240 FT /note="E -> G (in Ref. 5; CAA31435)" FT /evidence="ECO:0000305" FT CONFLICT 272 FT /note="H -> Q (in Ref. 1; ADQ85985/ADQ85986)" FT /evidence="ECO:0000305" FT CONFLICT 274 FT /note="S -> A (in Ref. 6; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 279 FT /note="I -> T (in Ref. 1; ADQ85985/ADQ85986)" FT /evidence="ECO:0000305" FT CONFLICT 290..291 FT /note="VT -> IV (in Ref. 6; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 301 FT /note="I -> V (in Ref. 6; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 307 FT /note="K -> E (in Ref. 5; CAA31435)" FT /evidence="ECO:0000305" FT CONFLICT 349 FT /note="H -> Y (in Ref. 5; CAA31435/CAA31529)" FT /evidence="ECO:0000305" FT CONFLICT 360 FT /note="P -> S (in Ref. 5; CAA31435/CAA31529)" FT /evidence="ECO:0000305" FT CONFLICT 366 FT /note="N -> K (in Ref. 1; ADQ85985)" FT /evidence="ECO:0000305" FT CONFLICT 373 FT /note="D -> E (in Ref. 5; CAA31435/CAA31529)" FT /evidence="ECO:0000305" FT CONFLICT 374 FT /note="D -> H (in Ref. 5; CAA31529)" FT /evidence="ECO:0000305" FT HELIX 133..136 FT /evidence="ECO:0007829|PDB:2ACT" FT HELIX 140..142 FT /evidence="ECO:0007829|PDB:2ACT" FT HELIX 151..168 FT /evidence="ECO:0007829|PDB:2ACT" FT HELIX 176..182 FT /evidence="ECO:0007829|PDB:2ACT" FT HELIX 190..192 FT /evidence="ECO:0007829|PDB:2ACT" FT HELIX 196..206 FT /evidence="ECO:0007829|PDB:2ACT" FT TURN 212..214 FT /evidence="ECO:0007829|PDB:2ACT" FT HELIX 226..230 FT /evidence="ECO:0007829|PDB:2ACT" FT STRAND 238..241 FT /evidence="ECO:0007829|PDB:2ACT" FT HELIX 247..256 FT /evidence="ECO:0007829|PDB:2ACT" FT STRAND 259..263 FT /evidence="ECO:0007829|PDB:2ACT" FT HELIX 268..272 FT /evidence="ECO:0007829|PDB:2ACT" FT STRAND 275..278 FT /evidence="ECO:0007829|PDB:2ACT" FT STRAND 288..298 FT /evidence="ECO:0007829|PDB:2ACT" FT STRAND 301..307 FT /evidence="ECO:0007829|PDB:2ACT" FT STRAND 319..323 FT /evidence="ECO:0007829|PDB:2ACT" FT HELIX 331..333 FT /evidence="ECO:0007829|PDB:2ACT" FT STRAND 339..342 FT /evidence="ECO:0007829|PDB:2ACT" SQ SEQUENCE 380 AA; 42098 MW; C2DA505454525B93 CRC64; MGLPKSFVSM SLLFFSTLLI LSLAFNAKNL TQRTNDEVKA MYESWLIKYG KSYNSLGEWE RRFEIFKETL RFIDEHNADT NRSYKVGLNQ FADLTDEEFR STYLGFTSGS NKTKVSNQYE PRVGQVLPSY VDWRSAGAVV DIKSQGECGG CWAFSAIATV EGINKIVTGV LISLSEQELI DCGRTQNTRG CNVGYITDGF QFIINNGGIN TEENYPYTAQ DGECNVDLQN EKYVTIDTYE NVPYNNEWAL QTAVTYQPVS VALDAAGDAF KHYSSGIFIG PCGTAIDHAV TIVGYGTEGG IDYWIVKNSW DTTWGEEGYM RILRNVGGAG TCGIATMPSY PVKYNNQNHP KSYSSLINPP AFSMSNDGPV GVDDGQRYSA //