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Protein

Actinidain

Gene
N/A
Organism
Actinidia chinensis (Kiwi) (Yangtao)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Cysteine protease responsible for the cleavage of kiwellin into kissper and KiTH.1 Publication

Catalytic activityi

Specificity close to that of papain.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei151 – 1511
Active sitei288 – 2881
Active sitei308 – 3081

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Enzyme and pathway databases

BRENDAi3.4.22.14. 120.

Protein family/group databases

MEROPSiC01.007.

Names & Taxonomyi

Protein namesi
Recommended name:
Actinidain (EC:3.4.22.14)
Short name:
Actinidin
Alternative name(s):
Allergen: Act c 1
OrganismiActinidia chinensis (Kiwi) (Yangtao)
Taxonomic identifieri3625 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridsEricalesActinidiaceaeActinidia

Pathology & Biotechi

Allergenic propertiesi

Causes an allergic reaction in human.

Keywords - Diseasei

Allergen

Protein family/group databases

Allergomei1. Act d 1.
3052. Act d 1.0101.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424Sequence AnalysisAdd
BLAST
Propeptidei25 – 126102Activation peptide2 PublicationsPRO_0000026398Add
BLAST
Chaini127 – 380254ActinidainPRO_0000026399Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi148 ↔ 191
Disulfide bondi182 ↔ 224
Disulfide bondi282 ↔ 332

Keywords - PTMi

Disulfide bond, Zymogen

Expressioni

Tissue specificityi

Fruit.1 Publication

Developmental stagei

Levels of mRNA accumulate during early fruit development.1 Publication

Structurei

Secondary structure

1
380
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi133 – 1364Combined sources
Helixi151 – 16818Combined sources
Helixi176 – 1827Combined sources
Helixi190 – 1923Combined sources
Helixi196 – 20611Combined sources
Turni212 – 2143Combined sources
Helixi226 – 2305Combined sources
Beta strandi238 – 2414Combined sources
Helixi247 – 25610Combined sources
Beta strandi259 – 2635Combined sources
Helixi268 – 2725Combined sources
Beta strandi275 – 2784Combined sources
Beta strandi288 – 29811Combined sources
Beta strandi301 – 3077Combined sources
Beta strandi319 – 3235Combined sources
Helixi331 – 3333Combined sources
Beta strandi339 – 3424Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AECX-ray1.86A127-344[»]
1F3Qmodel-A127-344[»]
1FOGmodel-A127-344[»]
1FTVmodel-A127-344[»]
2ACTX-ray1.70A127-346[»]
ProteinModelPortaliP00785.
SMRiP00785. Positions 127-343.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00785.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase C1 family.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Family and domain databases

InterProiIPR025661. Pept_asp_AS.
IPR000169. Pept_cys_AS.
IPR025660. Pept_his_AS.
IPR013128. Peptidase_C1A.
IPR000668. Peptidase_C1A_C.
IPR013201. Prot_inhib_I29.
[Graphical view]
PANTHERiPTHR12411. PTHR12411. 1 hit.
PfamiPF08246. Inhibitor_I29. 1 hit.
PF00112. Peptidase_C1. 1 hit.
[Graphical view]
PRINTSiPR00705. PAPAIN.
SMARTiSM00848. Inhibitor_I29. 1 hit.
SM00645. Pept_C1. 1 hit.
[Graphical view]
PROSITEiPS00640. THIOL_PROTEASE_ASN. 1 hit.
PS00139. THIOL_PROTEASE_CYS. 1 hit.
PS00639. THIOL_PROTEASE_HIS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P00785-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGLPKSFVSM SLLFFSTLLI LSLAFNAKNL TQRTNDEVKA MYESWLIKYG
60 70 80 90 100
KSYNSLGEWE RRFEIFKETL RFIDEHNADT NRSYKVGLNQ FADLTDEEFR
110 120 130 140 150
STYLRFTSGS NKTKVSNRYE PRVGQVLPSY VDWRSAGAVV DIKSQGECGG
160 170 180 190 200
CWAFSAIATV EGINKIVTGV LISLSEQELI DCGRTQNTRG CNGGYITDGF
210 220 230 240 250
QFIINNGGIN TEENYPYTAQ DGECNVDLQN EKYVTIDTYE NVPYNNEWAL
260 270 280 290 300
QTAVTYQPVS VALDAAGDAF KQYSSGIFTG PCGTAVDHAV TIVGYGTEGG
310 320 330 340 350
IDYWIVKNSW DTTWGEEGYM RILRNVGGAG TCGIATMPSY PVKYNNQNHP
360 370 380
KPYSSLINPP AFSMSKDGPV GVDDGQRYSA
Length:380
Mass (Da):42,172
Last modified:June 10, 2008 - v4
Checksum:i26BFDC612D53A50B
GO

Sequence cautioni

The sequence CAA31435.1 differs from that shown. Reason: Frameshift at position 371. Curated
The sequence CAA31529.1 differs from that shown. Reason: Frameshift at position 371. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti96 – 961D → G in CAA31435 (Ref. 2) Curated
Sequence conflicti105 – 1051R → G in CAA31435 (Ref. 2) Curated
Sequence conflicti108 – 1081S → G in CAA31435 (Ref. 2) Curated
Sequence conflicti124 – 1241G → S in CAA31435 (Ref. 2) Curated
Sequence conflicti167 – 1704VTGV → TSGS AA sequence (PubMed:687380).Curated
Sequence conflicti181 – 1811D → G in CAA31435 (Ref. 2) Curated
Sequence conflicti184 – 1841R → G in CAA31435 (Ref. 2) Curated
Sequence conflicti192 – 1921N → D AA sequence (PubMed:687380).Curated
Sequence conflicti206 – 2061N → D AA sequence (PubMed:687380).Curated
Sequence conflicti212 – 2121E → G in CAA31435 (Ref. 2) Curated
Sequence conflicti223 – 2231E → D AA sequence (PubMed:687380).Curated
Sequence conflicti225 – 2251N → D AA sequence (PubMed:687380).Curated
Sequence conflicti226 – 2261V → L in CAA31435 (Ref. 2) Curated
Sequence conflicti227 – 2271D → A AA sequence (PubMed:687380).Curated
Sequence conflicti230 – 2312NE → DQ AA sequence (PubMed:687380).Curated
Sequence conflicti240 – 2401E → G in CAA31435 (Ref. 2) Curated
Sequence conflicti272 – 2721Q → H in CAA31435 (Ref. 2) Curated
Sequence conflicti272 – 2721Q → H in CAA31529 (Ref. 2) Curated
Sequence conflicti274 – 2741S → A AA sequence (PubMed:687380).Curated
Sequence conflicti286 – 2861V → I in CAA31435 (Ref. 2) Curated
Sequence conflicti286 – 2861V → I in CAA31529 (Ref. 2) Curated
Sequence conflicti290 – 2912VT → IV AA sequence (PubMed:687380).Curated
Sequence conflicti301 – 3011I → V AA sequence (PubMed:687380).Curated
Sequence conflicti307 – 3071K → E in CAA31435 (Ref. 2) Curated
Sequence conflicti349 – 3491H → Y in CAA31435 (Ref. 2) Curated
Sequence conflicti349 – 3491H → Y in CAA31529 (Ref. 2) Curated
Sequence conflicti360 – 3601P → S in CAA31435 (Ref. 2) Curated
Sequence conflicti360 – 3601P → S in CAA31529 (Ref. 2) Curated
Sequence conflicti373 – 3731D → E in CAA31435 (Ref. 2) Curated
Sequence conflicti373 – 3731D → E in CAA31529 (Ref. 2) Curated
Sequence conflicti374 – 3741D → H in CAA31529 (Ref. 2) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF343446 mRNA. Translation: AAK06862.1.
X13013 mRNA. Translation: CAA31435.1. Frameshift.
X13139 mRNA. Translation: CAA31529.1. Frameshift.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF343446 mRNA. Translation: AAK06862.1.
X13013 mRNA. Translation: CAA31435.1. Frameshift.
X13139 mRNA. Translation: CAA31529.1. Frameshift.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AECX-ray1.86A127-344[»]
1F3Qmodel-A127-344[»]
1FOGmodel-A127-344[»]
1FTVmodel-A127-344[»]
2ACTX-ray1.70A127-346[»]
ProteinModelPortaliP00785.
SMRiP00785. Positions 127-343.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

Allergomei1. Act d 1.
3052. Act d 1.0101.
MEROPSiC01.007.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.4.22.14. 120.

Miscellaneous databases

EvolutionaryTraceiP00785.

Family and domain databases

InterProiIPR025661. Pept_asp_AS.
IPR000169. Pept_cys_AS.
IPR025660. Pept_his_AS.
IPR013128. Peptidase_C1A.
IPR000668. Peptidase_C1A_C.
IPR013201. Prot_inhib_I29.
[Graphical view]
PANTHERiPTHR12411. PTHR12411. 1 hit.
PfamiPF08246. Inhibitor_I29. 1 hit.
PF00112. Peptidase_C1. 1 hit.
[Graphical view]
PRINTSiPR00705. PAPAIN.
SMARTiSM00848. Inhibitor_I29. 1 hit.
SM00645. Pept_C1. 1 hit.
[Graphical view]
PROSITEiPS00640. THIOL_PROTEASE_ASN. 1 hit.
PS00139. THIOL_PROTEASE_CYS. 1 hit.
PS00639. THIOL_PROTEASE_HIS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.

Entry informationi

Entry nameiACTN_ACTCH
AccessioniPrimary (citable) accession number: P00785
Secondary accession number(s): Q9AXD2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: June 10, 2008
Last modified: April 1, 2015
This is version 105 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. Allergens
    Nomenclature of allergens and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Peptidase families
    Classification of peptidase families and list of entries
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.