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Protein

Actinidain

Gene
N/A
Organism
Actinidia deliciosa (Kiwi)
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.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei151By similarity1
Active sitei288By similarity1
Active sitei308By similarity1

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Enzyme and pathway databases

BRENDAi3.4.22.14. 121.

Names & Taxonomyi

Protein namesi
Recommended name:
ActinidainBy similarityImported (EC:3.4.22.14)
Short name:
ActinidinBy similarityImported
Alternative name(s):
Allergen Act d 1
Allergen: Act d 1
OrganismiActinidia deliciosa (Kiwi)
Taxonomic identifieri3627 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridsEricalesActinidiaceaeActinidia

Pathology & Biotechi

Allergenic propertiesi

Causes an allergic reaction in human. Binds IgE.2 Publications

Keywords - Diseasei

Allergen

Protein family/group databases

Allergomei1. Act d 1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 24Sequence analysisAdd BLAST24
PropeptideiPRO_000034346125 – 126Activation peptide3 PublicationsAdd BLAST102
ChainiPRO_0000343462127 – 380Actinidain1 PublicationAdd BLAST254

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi148 ↔ 191By similarity
Disulfide bondi182 ↔ 224By similarity
Disulfide bondi282 ↔ 332By similarity

Keywords - PTMi

Disulfide bond, Zymogen

Expressioni

Tissue specificityi

Fruit, present in small cells of the outer pericarp of mature fruit, but not large cells.1 Publication

Developmental stagei

Expressed in ripening fruit, levels are highest at the harvest of fruit and decrease as the fruit ripens.1 Publication

Structurei

3D structure databases

ProteinModelPortaliA5HII1.
ModBaseiSearch...
MobiDBiSearch...

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.

A5HII1-1 [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
STYLGFTSGS NKTKVSNRYE PRVGQVLPSY VDWRSAGAVV DIKSQGECGG
160 170 180 190 200
CWAFSAIATV EGINKIVTGV LISLSEQELI DCGRTQNTRG CNGGYITDGF
210 220 230 240 250
QFIINNGGIN TEENYPYTAQ DGECNLDLQN EKYVTIDTYE NVPYNNEWAL
260 270 280 290 300
QTAVTYQPVS VALDAAGDAF KHYSSGIFTG PCGTAIDHAV TIVGYGTEGG
310 320 330 340 350
IDYWIVKNSW DTTWGEEGYM RILRNVGGAG TCGIATMPSY PVKYNNQNHP
360 370 380
KPYSSLINPP AFSMSKDGPV GVDDGQRYSA
Length:380
Mass (Da):42,110
Last modified:June 12, 2007 - v1
Checksum:i70FDAD2235388224
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti96D → G in AAA32630 (Ref. 5) Curated1
Sequence conflicti108S → G in AAA32630 (Ref. 5) Curated1
Sequence conflicti123V → F in AAA32630 (Ref. 5) Curated1
Sequence conflicti124G → S in AAA32630 (Ref. 5) Curated1
Sequence conflicti181D → G in AAA32630 (Ref. 5) Curated1
Sequence conflicti184R → G in AAA32630 (Ref. 5) Curated1
Sequence conflicti212E → G in AAA32630 (Ref. 5) Curated1
Sequence conflicti226 – 227LD → VE in AAA32629 (PubMed:2251128).Curated2
Sequence conflicti240E → G in AAA32630 (Ref. 5) Curated1
Sequence conflicti272H → Q in AAA32629 (PubMed:2251128).Curated1
Sequence conflicti307K → E in AAA32630 (Ref. 5) Curated1
Sequence conflicti349H → Y in AAA32629 (PubMed:2251128).Curated1
Sequence conflicti349H → Y in AAA32630 (Ref. 5) Curated1
Sequence conflicti351K → E in AAA32629 (PubMed:2251128).Curated1
Sequence conflicti360P → S in AAA32630 (Ref. 5) Curated1
Sequence conflicti373D → E in AAA32629 (PubMed:2251128).Curated1
Sequence conflicti373D → E in AAA32630 (Ref. 5) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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

ProteinModelPortaliA5HII1.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

Allergomei1. Act d 1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.4.22.14. 121.

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_ACTDE
AccessioniPrimary (citable) accession number: A5HII1
Secondary accession number(s): Q43367, Q96227
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 2008
Last sequence update: June 12, 2007
Last modified: October 5, 2016
This is version 32 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. 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.