A5HII1 · ACTN_ACTDE
- ProteinActinidain
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids380 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Cysteine protease responsible for the cleavage of kiwellin into kissper and KiTH.
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 151 | |||||
Sequence: C | ||||||
Active site | 288 | |||||
Sequence: H | ||||||
Active site | 308 | |||||
Sequence: N |
GO annotations
all annotations | all molecular function | nucleotide binding | molecular_function | nucleic acid binding | dna binding | chromatin binding | dna-binding transcription factor activity | rna binding | cytoskeletal motor activity | catalytic activity | nuclease activity | signaling receptor binding | structural molecule activity | transporter activity | binding | protein binding | translation factor activity, rna binding | lipid binding | kinase activity | transferase activity | hydrolase activity | oxygen binding | enzyme regulator activity | carbohydrate binding | signaling receptor activity | translation regulator activity | transcription regulator activity | other molecular function | all biological process | carbohydrate metabolic process | generation of precursor metabolites and energy | nucleobase-containing compound metabolic process | dna metabolic process | translation | lipid metabolic process | transport | response to stress | cell cycle | cell communication | signal transduction | cell-cell signaling | multicellular organism development | circadian rhythm | biological_process | metabolic process | catabolic process | biosynthetic process | response to light stimulus | response to external stimulus | tropism | response to biotic stimulus | response to abiotic stimulus | response to endogenous stimulus | embryo development | post-embryonic development | fruit ripening | abscission | pollination | flower development | cellular process | programmed cell death | photosynthesis | cellular component organization | cell growth | protein metabolic process | cellular homeostasis | secondary metabolic process | reproductive process | cell differentiation | protein modification process | growth | epigenetic regulation of gene expression | response to chemical | anatomical structure development | regulation of molecular function | other biological process | all cellular component | cellular_component | extracellular region | cell wall | intracellular anatomical structure | nucleus | nuclear envelope | nucleoplasm | nucleolus | cytoplasm | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | cytosol | ribosome | cytoskeleton | plasma membrane | chloroplast | plastid | thylakoid | membrane | external encapsulating structure | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | extracellular space | |
Cellular Component | lysosome | |
Molecular Function | cysteine-type endopeptidase activity | |
Biological Process | proteolysis involved in protein catabolic process |
Keywords
- Molecular function
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameActinidain
- EC number
- Short namesActinidin
- Alternative names
- Allergen nameAct d 1
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > asterids > Ericales > Actinidiaceae > Actinidia
Accessions
- Primary accessionA5HII1
- Secondary accessions
Subcellular Location
UniProt Annotation
GO Annotation
Phenotypes & Variants
Allergenic properties
Causes an allergic reaction in human. Binds IgE.
Keywords
- Disease
Protein family/group databases
PTM/Processing
Features
Showing features for signal, propeptide, glycosylation, chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-24 | |||||
Sequence: MGLPKSFVSMSLLFFSTLLILSLA | ||||||
Propeptide | PRO_0000343461 | 25-126 | Activation peptide | |||
Sequence: FNAKNLTQRTNDEVKAMYESWLIKYGKSYNSLGEWERRFEIFKETLRFIDEHNADTNRSYKVGLNQFADLTDEEFRSTYLGFTSGSNKTKVSNRYEPRVGQV | ||||||
Glycosylation | 29 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 81 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 111 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Chain | PRO_0000343462 | 127-380 | Actinidain | |||
Sequence: LPSYVDWRSAGAVVDIKSQGECGGCWAFSAIATVEGINKIVTGVLISLSEQELIDCGRTQNTRGCNGGYITDGFQFIINNGGINTEENYPYTAQDGECNLDLQNEKYVTIDTYENVPYNNEWALQTAVTYQPVSVALDAAGDAFKHYSSGIFTGPCGTAIDHAVTIVGYGTEGGIDYWIVKNSWDTTWGEEGYMRILRNVGGAGTCGIATMPSYPVKYNNQNHPKPYSSLINPPAFSMSKDGPVGVDDGQRYSA | ||||||
Disulfide bond | 148↔191 | |||||
Sequence: CGGCWAFSAIATVEGINKIVTGVLISLSEQELIDCGRTQNTRGC | ||||||
Disulfide bond | 182↔224 | |||||
Sequence: CGRTQNTRGCNGGYITDGFQFIINNGGINTEENYPYTAQDGEC | ||||||
Disulfide bond | 282↔332 | |||||
Sequence: CGTAIDHAVTIVGYGTEGGIDYWIVKNSWDTTWGEEGYMRILRNVGGAGTC |
Keywords
- PTM
Expression
Tissue specificity
Fruit, present in small cells of the outer pericarp of mature fruit, but not large cells.
Developmental stage
Expressed in ripening fruit, levels are highest at the harvest of fruit and decrease as the fruit ripens.
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length380
- Mass (Da)42,110
- Last updated2007-06-12 v1
- Checksum70FDAD2235388224
Sequence caution
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 96 | in Ref. 5; AAA32630 | ||||
Sequence: D → G | ||||||
Sequence conflict | 108 | in Ref. 5; AAA32630 | ||||
Sequence: S → G | ||||||
Sequence conflict | 123 | in Ref. 5; AAA32630 | ||||
Sequence: V → F | ||||||
Sequence conflict | 124 | in Ref. 5; AAA32630 | ||||
Sequence: G → S | ||||||
Sequence conflict | 181 | in Ref. 5; AAA32630 | ||||
Sequence: D → G | ||||||
Sequence conflict | 184 | in Ref. 5; AAA32630 | ||||
Sequence: R → G | ||||||
Sequence conflict | 212 | in Ref. 5; AAA32630 | ||||
Sequence: E → G | ||||||
Sequence conflict | 226-227 | in Ref. 2; AAA32629 | ||||
Sequence: LD → VE | ||||||
Sequence conflict | 240 | in Ref. 5; AAA32630 | ||||
Sequence: E → G | ||||||
Sequence conflict | 272 | in Ref. 2; AAA32629 | ||||
Sequence: H → Q | ||||||
Sequence conflict | 307 | in Ref. 5; AAA32630 | ||||
Sequence: K → E | ||||||
Sequence conflict | 349 | in Ref. 2; AAA32629 and 5; AAA32630 | ||||
Sequence: H → Y | ||||||
Sequence conflict | 351 | in Ref. 2; AAA32629 | ||||
Sequence: K → E | ||||||
Sequence conflict | 360 | in Ref. 5; AAA32630 | ||||
Sequence: P → S | ||||||
Sequence conflict | 373 | in Ref. 2; AAA32629 and 5; AAA32630 | ||||
Sequence: D → E |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X16466 EMBL· GenBank· DDBJ | CAA34486.1 EMBL· GenBank· DDBJ | mRNA | ||
M38422 EMBL· GenBank· DDBJ | AAA32629.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
EF530131 EMBL· GenBank· DDBJ | ABQ10189.1 EMBL· GenBank· DDBJ | mRNA | ||
X57551 EMBL· GenBank· DDBJ | CAA40778.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M21335 EMBL· GenBank· DDBJ | AAA32630.1 EMBL· GenBank· DDBJ | mRNA | Frameshift |