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A5HII1 (ACTN_ACTDE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 26. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Actinidain

Short name=Actinidin
EC=3.4.22.14
Alternative name(s):
Allergen Act d 1
Allergen=Act d 1
OrganismActinidia deliciosa (Kiwi)
Taxonomic identifier3627 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridsEricalesActinidiaceaeActinidia

Protein attributes

Sequence length380 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Cysteine protease responsible for the cleavage of kiwellin into kissper and KiTH. Ref.6

Catalytic activity

Specificity close to that of papain. UniProtKB P00785

Tissue specificity

Fruit, present in small cells of the outer pericarp of mature fruit, but not large cells. Ref.3

Developmental stage

Expressed in ripening fruit, levels are highest at the harvest of fruit and decrease as the fruit ripens. Ref.3

Allergenic properties

Causes an allergic reaction in human. Binds IgE. Ref.7 Ref.8

Sequence similarities

Belongs to the peptidase C1 family.

Sequence caution

The sequence AAA32630.1 differs from that shown. Reason: Frameshift at position 371.

Ontologies

Keywords
   DiseaseAllergen
   DomainSignal
   Molecular functionHydrolase
Protease
Thiol protease
   PTMDisulfide bond
Zymogen
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Molecular_functioncysteine-type peptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Potential
Propeptide25 – 126102Activation peptide Ref.6
PRO_0000343461
Chain127 – 380254Actinidain Ref.6
PRO_0000343462

Sites

Active site1511 By similarity UniProtKB P00785
Active site2881 By similarity UniProtKB P00785
Active site3081 By similarity UniProtKB P00785

Amino acid modifications

Disulfide bond148 ↔ 191 By similarity UniProtKB P00785
Disulfide bond182 ↔ 224 By similarity UniProtKB P00785
Disulfide bond282 ↔ 332 By similarity UniProtKB P00785

Experimental info

Sequence conflict961D → G in AAA32630. Ref.5
Sequence conflict1081S → G in AAA32630. Ref.5
Sequence conflict1231V → F in AAA32630. Ref.5
Sequence conflict1241G → S in AAA32630. Ref.5
Sequence conflict1811D → G in AAA32630. Ref.5
Sequence conflict1841R → G in AAA32630. Ref.5
Sequence conflict2121E → G in AAA32630. Ref.5
Sequence conflict226 – 2272LD → VE in AAA32629. Ref.2
Sequence conflict2401E → G in AAA32630. Ref.5
Sequence conflict2721H → Q in AAA32629. Ref.2
Sequence conflict3071K → E in AAA32630. Ref.5
Sequence conflict3491H → Y in AAA32629. Ref.2
Sequence conflict3491H → Y in AAA32630. Ref.5
Sequence conflict3511K → E in AAA32629. Ref.2
Sequence conflict3601P → S in AAA32630. Ref.5
Sequence conflict3731D → E in AAA32629. Ref.2
Sequence conflict3731D → E in AAA32630. Ref.5

Sequences

Sequence LengthMass (Da)Tools
A5HII1 [UniParc].

Last modified June 12, 2007. Version 1.
Checksum: 70FDAD2235388224

FASTA38042,110
        10         20         30         40         50         60 
MGLPKSFVSM SLLFFSTLLI LSLAFNAKNL TQRTNDEVKA MYESWLIKYG KSYNSLGEWE 

        70         80         90        100        110        120 
RRFEIFKETL RFIDEHNADT NRSYKVGLNQ FADLTDEEFR STYLGFTSGS NKTKVSNRYE 

       130        140        150        160        170        180 
PRVGQVLPSY VDWRSAGAVV DIKSQGECGG CWAFSAIATV EGINKIVTGV LISLSEQELI 

       190        200        210        220        230        240 
DCGRTQNTRG CNGGYITDGF QFIINNGGIN TEENYPYTAQ DGECNLDLQN EKYVTIDTYE 

       250        260        270        280        290        300 
NVPYNNEWAL QTAVTYQPVS VALDAAGDAF KHYSSGIFTG PCGTAIDHAV TIVGYGTEGG 

       310        320        330        340        350        360 
IDYWIVKNSW DTTWGEEGYM RILRNVGGAG TCGIATMPSY PVKYNNQNHP KPYSSLINPP 

       370        380 
AFSMSKDGPV GVDDGQRYSA 

« Hide

References

[1]"Nucleotide sequence of actinidin, a kiwi fruit protease."
Podivinsky E., Forster R.L.S., Gardner R.C.
Nucleic Acids Res. 17:8363-8363(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Nucleotide sequence of an actinidin genomic clone."
Snowden K.C., Gardner R.C.
Nucleic Acids Res. 18:6684-6684(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: cv. Hayward.
[3]"Identification and characterisation of acidic and novel basic forms of actinidin, the highly abundant cysteine protease from kiwifruit."
Nieuwenhuizen N.J., Beuning L.L., Sutherland P.W., Sharma N.N., Cooney J.M., Bieleski L.R.F., Schroeder R., MacRae E.A., Atkinson R.G.
Funct. Plant Biol. 34:946-961(2007)
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
Strain: cv. Hayward.
[4]"Nucleotide sequence of the promoter region from kiwifruit actinidin genes."
Keeling J., Maxwell P., Gardner R.C.
Plant Mol. Biol. 15:787-788(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-13.
[5]Praekelt U.M., McKee R.A., Smith H.
Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 70-380.
Strain: cv. Exbury.
[6]"Kiwellin, a modular protein from green and gold kiwi fruits: evidence of in vivo and in vitro processing and IgE binding."
Tuppo L., Giangrieco I., Palazzo P., Bernardi M.L., Scala E., Carratore V., Tamburrini M., Mari A., Ciardiello M.A.
J. Agric. Food Chem. 56:3812-3817(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 127-136, FUNCTION.
Strain: cv. Hayward.
Tissue: Fruit.
[7]"IgE sensitization profiles toward green and gold kiwifruits differ among patients allergic to kiwifruit from 3 European countries."
Bublin M., Mari A., Ebner C., Knulst A., Scheiner O., Hoffmann-Sommergruber K., Breiteneder H., Radauer C.
J. Allergy Clin. Immunol. 114:1169-1175(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 127-131, ALLERGEN.
Strain: cv. Hayward.
Tissue: Fruit.
[8]"Immunoglobulin E recognition patterns to purified Kiwifruit (Actinidinia deliciosa) allergens in patients sensitized to Kiwi with different clinical symptoms."
Palacin A., Rodriguez J., Blanco C., Lopez-Torrejon G., Sanchez-Monge R., Varela J., Jimenez M.A., Cumplido J., Carrillo T., Crespo J.F., Salcedo G.
Clin. Exp. Allergy 38:1220-1228(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 127-131, ALLERGEN.
Strain: cv. Hayward.
Tissue: Fruit.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X16466 mRNA. Translation: CAA34486.1.
M38422 Genomic DNA. Translation: AAA32629.1.
EF530131 mRNA. Translation: ABQ10189.1.
X57551 Genomic DNA. Translation: CAA40778.1.
M21335 mRNA. Translation: AAA32630.1. Frameshift.

3D structure databases

ProteinModelPortalA5HII1.
SMRA5HII1. Positions 127-343.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

Allergome1. Act d 1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR025661. Pept_asp_AS.
IPR000169. Pept_cys_AS.
IPR025660. Pept_his_AS.
IPR013128. Peptidase_C1A.
IPR000668. Peptidase_C1A_C.
IPR013201. Prot_inhib_I29.
[Graphical view]
PANTHERPTHR12411. PTHR12411. 1 hit.
PfamPF08246. Inhibitor_I29. 1 hit.
PF00112. Peptidase_C1. 1 hit.
[Graphical view]
PRINTSPR00705. PAPAIN.
SMARTSM00848. Inhibitor_I29. 1 hit.
SM00645. Pept_C1. 1 hit.
[Graphical view]
PROSITEPS00640. THIOL_PROTEASE_ASN. 1 hit.
PS00139. THIOL_PROTEASE_CYS. 1 hit.
PS00639. THIOL_PROTEASE_HIS. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameACTN_ACTDE
AccessionPrimary (citable) accession number: A5HII1
Secondary accession number(s): Q43367, Q96227
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 2008
Last sequence update: June 12, 2007
Last modified: May 14, 2014
This is version 26 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries