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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)DescriptionActionsGraphical viewLength
Active sitei1511
Active sitei2881
Active sitei3081

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

MEROPSiI29.003.

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)DescriptionActionsGraphical viewLength
Signal peptidei1 – 24Sequence analysisAdd BLAST24
PropeptideiPRO_000002639825 – 126Activation peptide2 PublicationsAdd BLAST102
ChainiPRO_0000026399127 – 380ActinidainAdd BLAST254

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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

1380
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi133 – 136Combined sources4
Helixi151 – 168Combined sources18
Helixi176 – 182Combined sources7
Helixi190 – 192Combined sources3
Helixi196 – 206Combined sources11
Turni212 – 214Combined sources3
Helixi226 – 230Combined sources5
Beta strandi238 – 241Combined sources4
Helixi247 – 256Combined sources10
Beta strandi259 – 263Combined sources5
Helixi268 – 272Combined sources5
Beta strandi275 – 278Combined sources4
Beta strandi288 – 298Combined sources11
Beta strandi301 – 307Combined sources7
Beta strandi319 – 323Combined sources5
Helixi331 – 333Combined sources3
Beta strandi339 – 342Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AECX-ray1.86A127-344[»]
1F3Qmodel-A127-344[»]
1FOGmodel-A127-344[»]
1FTVmodel-A127-344[»]
2ACTX-ray1.70A127-346[»]
ProteinModelPortaliP00785.
SMRiP00785.
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 differs from that shown. Reason: Frameshift at position 371.Curated
The sequence CAA31529 differs from that shown. Reason: Frameshift at position 371.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti96D → G in CAA31435 (Ref. 2) Curated1
Sequence conflicti105R → G in CAA31435 (Ref. 2) Curated1
Sequence conflicti108S → G in CAA31435 (Ref. 2) Curated1
Sequence conflicti124G → S in CAA31435 (Ref. 2) Curated1
Sequence conflicti167 – 170VTGV → TSGS AA sequence (PubMed:687380).Curated4
Sequence conflicti181D → G in CAA31435 (Ref. 2) Curated1
Sequence conflicti184R → G in CAA31435 (Ref. 2) Curated1
Sequence conflicti192N → D AA sequence (PubMed:687380).Curated1
Sequence conflicti206N → D AA sequence (PubMed:687380).Curated1
Sequence conflicti212E → G in CAA31435 (Ref. 2) Curated1
Sequence conflicti223E → D AA sequence (PubMed:687380).Curated1
Sequence conflicti225N → D AA sequence (PubMed:687380).Curated1
Sequence conflicti226V → L in CAA31435 (Ref. 2) Curated1
Sequence conflicti227D → A AA sequence (PubMed:687380).Curated1
Sequence conflicti230 – 231NE → DQ AA sequence (PubMed:687380).Curated2
Sequence conflicti240E → G in CAA31435 (Ref. 2) Curated1
Sequence conflicti272Q → H in CAA31435 (Ref. 2) Curated1
Sequence conflicti272Q → H in CAA31529 (Ref. 2) Curated1
Sequence conflicti274S → A AA sequence (PubMed:687380).Curated1
Sequence conflicti286V → I in CAA31435 (Ref. 2) Curated1
Sequence conflicti286V → I in CAA31529 (Ref. 2) Curated1
Sequence conflicti290 – 291VT → IV AA sequence (PubMed:687380).Curated2
Sequence conflicti301I → V AA sequence (PubMed:687380).Curated1
Sequence conflicti307K → E in CAA31435 (Ref. 2) Curated1
Sequence conflicti349H → Y in CAA31435 (Ref. 2) Curated1
Sequence conflicti349H → Y in CAA31529 (Ref. 2) Curated1
Sequence conflicti360P → S in CAA31435 (Ref. 2) Curated1
Sequence conflicti360P → S in CAA31529 (Ref. 2) Curated1
Sequence conflicti373D → E in CAA31435 (Ref. 2) Curated1
Sequence conflicti373D → E in CAA31529 (Ref. 2) Curated1
Sequence conflicti374D → H in CAA31529 (Ref. 2) Curated1

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AECX-ray1.86A127-344[»]
1F3Qmodel-A127-344[»]
1FOGmodel-A127-344[»]
1FTVmodel-A127-344[»]
2ACTX-ray1.70A127-346[»]
ProteinModelPortaliP00785.
SMRiP00785.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

Allergomei1. Act d 1.
3052. Act d 1.0101.
MEROPSiI29.003.

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...

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: November 2, 2016
This is version 110 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

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 one 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.