P00785 (ACTN_ACTCH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Actinidain Short name=Actinidin EC=3.4.22.14 Alternative name(s): Allergen=Act c 1
Organism	Actinidia chinensis (Kiwi) (Yangtao)
Taxonomic identifier	3625 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › Ericales › Actinidiaceae › Actinidia

Protein attributes

Sequence length	380 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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
Disease	Allergen
Domain	Signal
Molecular function	Hydrolase Protease Thiol protease
PTM	Disulfide bond Zymogen
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological_process	proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	cysteine-type peptidase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 24

24

Potential

Propeptide

25 – 126

102

Activation peptide

PRO_0000026398

Chain

127 – 380

254

Actinidain

PRO_0000026399

Sites

Active site

151

1

Active site

288

1

Active site

308

1

Amino acid modifications

Disulfide bond

148 ↔ 191

Disulfide bond

182 ↔ 224

Disulfide bond

282 ↔ 332

Experimental info

Sequence conflict

96

1

D → G in CAA31435. Ref.2

Sequence conflict

105

1

R → G in CAA31435. Ref.2

Sequence conflict

108

1

S → G in CAA31435. Ref.2

Sequence conflict

124

1

G → S in CAA31435. Ref.2

Sequence conflict

167 – 170

4

VTGV → TSGS AA sequence Ref.3

Sequence conflict

181

1

D → G in CAA31435. Ref.2

Sequence conflict

184

1

R → G in CAA31435. Ref.2

Sequence conflict

192

1

N → D AA sequence Ref.3

Sequence conflict

206

1

N → D AA sequence Ref.3

Sequence conflict

212

1

E → G in CAA31435. Ref.2

Sequence conflict

223

1

E → D AA sequence Ref.3

Sequence conflict

225

1

N → D AA sequence Ref.3

Sequence conflict

226

1

V → L in CAA31435. Ref.2

Sequence conflict

227

1

D → A AA sequence Ref.3

Sequence conflict

230 – 231

2

NE → DQ AA sequence Ref.3

Sequence conflict

240

1

E → G in CAA31435. Ref.2

Sequence conflict

272

1

Q → H in CAA31435. Ref.2

Sequence conflict

272

1

Q → H in CAA31529. Ref.2

Sequence conflict

274

1

S → A AA sequence Ref.3

Sequence conflict

286

1

V → I in CAA31435. Ref.2

Sequence conflict

286

1

V → I in CAA31529. Ref.2

Sequence conflict

290 – 291

2

VT → IV AA sequence Ref.3

Sequence conflict

301

1

I → V AA sequence Ref.3

Sequence conflict

307

1

K → E in CAA31435. Ref.2

Sequence conflict

349

1

H → Y in CAA31435. Ref.2

Sequence conflict

349

1

H → Y in CAA31529. Ref.2

Sequence conflict

360

1

P → S in CAA31435. Ref.2

Sequence conflict

360

1

P → S in CAA31529. Ref.2

Sequence conflict

373

1

D → E in CAA31435. Ref.2

Sequence conflict

373

1

D → E in CAA31529. Ref.2

Sequence conflict

374

1

D → H in CAA31529. Ref.2

Secondary structure

1

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380

Helix Strand Turn

Details...

Helix

133 – 136

4

Helix

151 – 168

18

Helix

176 – 182

7

Helix

190 – 192

3

Helix

196 – 206

11

Turn

212 – 214

3

Helix

226 – 230

5

Beta strand

238 – 241

4

Helix

247 – 256

10

Beta strand

259 – 263

5

Helix

268 – 272

5

Beta strand

275 – 278

4

Beta strand

288 – 298

11

Beta strand

301 – 307

7

Beta strand

319 – 323

5

Helix

331 – 333

3

Beta strand

339 – 342

4

Sequences

	Sequence		Length	Mass (Da)
	P00785 [UniParc]. Last modified June 10, 2008. Version 4. Checksum: 26BFDC612D53A50B	FASTA	380	42,172
	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

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

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AEC	X-ray	1.86	A	127-344	[»]
1F3Q	model	-	A	127-344	[»]
1FOG	model	-	A	127-344	[»]
1FTV	model	-	A	127-344	[»]
2ACT	X-ray	1.70	A	127-346	[»]

ProteinModelPortal

P00785.

SMR

P00785. Positions 127-343.

ModBase

Search...

Protein family/group databases

Allergome

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

MEROPS

I29.003.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

InterPro

IPR025661. Pept_asp_AS.
IPR000169. Pept_cys_AS.
IPR025660. Pept_his_AS.
IPR013128. Peptidase_C1A.
IPR000668. Peptidase_C1A_C.
IPR013201. Prot_inhib_I29.
[Graphical view]

PANTHER

PTHR12411. PTHR12411. 1 hit.

Pfam

PF08246. Inhibitor_I29. 1 hit.
PF00112. Peptidase_C1. 1 hit.
[Graphical view]

PRINTS

PR00705. PAPAIN.

SMART

SM00848. Inhibitor_I29. 1 hit.
SM00645. Pept_C1. 1 hit.
[Graphical view]

PROSITE

PS00640. THIOL_PROTEASE_ASN. 1 hit.
PS00139. THIOL_PROTEASE_CYS. 1 hit.
PS00639. THIOL_PROTEASE_HIS. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P00785.

Entry information

Entry name

ACTN_ACTCH

Accession

Primary (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:	April 3, 2013
This is version 99 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program