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P00785 (ACTN_ACTCH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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 c 1
OrganismActinidia chinensis (Kiwi) (Yangtao)
Taxonomic identifier3625 [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.4

Catalytic activity

Specificity close to that of papain.

Tissue specificity

Fruit. Ref.2

Developmental stage

Levels of mRNA accumulate during early fruit development. Ref.2

Allergenic properties

Causes an allergic reaction in human.

Sequence similarities

Belongs to the peptidase C1 family.

Sequence caution

The sequence CAA31435.1 differs from that shown. Reason: Frameshift at position 371.

The sequence CAA31529.1 differs from that shown. Reason: Frameshift at position 371.

Ontologies

Keywords
   DiseaseAllergen
   DomainSignal
   Molecular functionHydrolase
Protease
Thiol protease
   PTMDisulfide bond
Zymogen
   Technical term3D-structure
Direct 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
PRO_0000026398
Chain127 – 380254Actinidain
PRO_0000026399

Sites

Active site1511
Active site2881
Active site3081

Amino acid modifications

Disulfide bond148 ↔ 191
Disulfide bond182 ↔ 224
Disulfide bond282 ↔ 332

Experimental info

Sequence conflict961D → G in CAA31435. Ref.2
Sequence conflict1051R → G in CAA31435. Ref.2
Sequence conflict1081S → G in CAA31435. Ref.2
Sequence conflict1241G → S in CAA31435. Ref.2
Sequence conflict167 – 1704VTGV → TSGS AA sequence Ref.3
Sequence conflict1811D → G in CAA31435. Ref.2
Sequence conflict1841R → G in CAA31435. Ref.2
Sequence conflict1921N → D AA sequence Ref.3
Sequence conflict2061N → D AA sequence Ref.3
Sequence conflict2121E → G in CAA31435. Ref.2
Sequence conflict2231E → D AA sequence Ref.3
Sequence conflict2251N → D AA sequence Ref.3
Sequence conflict2261V → L in CAA31435. Ref.2
Sequence conflict2271D → A AA sequence Ref.3
Sequence conflict230 – 2312NE → DQ AA sequence Ref.3
Sequence conflict2401E → G in CAA31435. Ref.2
Sequence conflict2721Q → H in CAA31435. Ref.2
Sequence conflict2721Q → H in CAA31529. Ref.2
Sequence conflict2741S → A AA sequence Ref.3
Sequence conflict2861V → I in CAA31435. Ref.2
Sequence conflict2861V → I in CAA31529. Ref.2
Sequence conflict290 – 2912VT → IV AA sequence Ref.3
Sequence conflict3011I → V AA sequence Ref.3
Sequence conflict3071K → E in CAA31435. Ref.2
Sequence conflict3491H → Y in CAA31435. Ref.2
Sequence conflict3491H → Y in CAA31529. Ref.2
Sequence conflict3601P → S in CAA31435. Ref.2
Sequence conflict3601P → S in CAA31529. Ref.2
Sequence conflict3731D → E in CAA31435. Ref.2
Sequence conflict3731D → E in CAA31529. Ref.2
Sequence conflict3741D → H in CAA31529. Ref.2

Secondary structure

................................... 380
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00785 [UniParc].

Last modified June 10, 2008. Version 4.
Checksum: 26BFDC612D53A50B

FASTA38042,172
        10         20         30         40         50         60 
MGLPKSFVSM SLLFFSTLLI LSLAFNAKNL TQRTNDEVKA MYESWLIKYG KSYNSLGEWE 

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

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

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

       250        260        270        280        290        300 
NVPYNNEWAL QTAVTYQPVS VALDAAGDAF KQYSSGIFTG PCGTAVDHAV TIVGYGTEGG 

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

       370        380 
AFSMSKDGPV GVDDGQRYSA 

« Hide

References

[1]"Isolation and expression in E. coli of actinidin gene from Chinese wild kiwifruit."
Lee N.K., Hahm Y.T.
Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Molecular analysis of actinidin, the cysteine proteinase of Actinidia chinesis."
Praekelt U.M., McKee R.A., Smith H.
Plant Mol. Biol. 10:193-202(1988) [AGRICOLA] [Europe PMC]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 70-380, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[3]"The amino acid sequence of the tryptic peptides from actinidin, a proteolytic enzyme from the fruit of Actinidia chinensis."
Carne A., Moore C.H.
Biochem. J. 173:73-83(1978) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 127-346.
[4]"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. Hort 16A.
Tissue: Fruit.
[5]"Structure of actinidin, after refinement at 1.7-A resolution."
Baker E.N.
J. Mol. Biol. 141:441-484(1980) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS), SEQUENCE REVISION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF343446 mRNA. Translation: AAK06862.1.
X13013 mRNA. Translation: CAA31435.1. Frameshift.
X13139 mRNA. Translation: CAA31529.1. Frameshift.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AECX-ray1.86A127-344[»]
1F3Qmodel-A127-344[»]
1FOGmodel-A127-344[»]
1FTVmodel-A127-344[»]
2ACTX-ray1.70A127-346[»]
ProteinModelPortalP00785.
SMRP00785. Positions 127-343.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

Allergome1. Act d 1.
3052. Act d 1.0101.
MEROPSC01.007.

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...

Other

EvolutionaryTraceP00785.

Entry information

Entry nameACTN_ACTCH
AccessionPrimary (citable) accession number: P00785
Secondary accession number(s): Q9AXD2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: June 10, 2008
Last modified: May 14, 2014
This is version 102 of the entry and version 4 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Allergens

Nomenclature of allergens and list of entries