[1]	NUCLEOTIDE SEQUENCE [MRNA]. Lee N.K., Hahm Y.T.; "Isolation and expression in E. coli of actinidin gene from Chinese wild kiwifruit."; Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
[2]	NUCLEOTIDE SEQUENCE [MRNA] OF 70-380, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE. DOI=10.1007/BF00027396; AGRICOLA=IND92000625 Praekelt U.M., McKee R.A., Smith H.; "Molecular analysis of actinidin, the cysteine proteinase of Actinidia chinesis."; Plant Mol. Biol. 10:193-202(1988).
[3]	PROTEIN SEQUENCE OF 127-346. PubMed=687380 [NCBI, ExPASy, EBI, Israel, Japan] Carne A., Moore C.H.; "The amino acid sequence of the tryptic peptides from actinidin, a proteolytic enzyme from the fruit of Actinidia chinensis."; Biochem. J. 173:73-83(1978).
[4]	PROTEIN SEQUENCE OF 127-136, AND FUNCTION. STRAIN=cv. Hort 16A; TISSUE=Fruit; DOI=10.1021/jf703620m; PubMed=18442249 [NCBI, ExPASy, EBI, Israel, Japan] Tuppo L., Giangrieco I., Palazzo P., Bernardi M.L., Scala E., Carratore V., Tamburrini M., Mari A., Ciardiello M.A.; "Kiwellin, a modular protein from green and gold kiwi fruits: evidence of in vivo and in vitro processing and IgE binding."; J. Agric. Food Chem. 56:3812-3817(2008).
[5]	X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS), AND SEQUENCE REVISION. DOI=10.1016/0022-2836(80)90255-7; PubMed=7003158 [NCBI, ExPASy, EBI, Israel, Japan] Baker E.N.; "Structure of actinidin, after refinement at 1.7-A resolution."; J. Mol. Biol. 141:441-484(1980).

Comments

FUNCTION: Cysteine protease responsible for the cleavage of kiwellin into kissper and KiTH.
CATALYTIC ACTIVITY: Specificity close to that of papain.
TISSUE SPECIFICITY: Fruit.
DEVELOPMENTAL STAGE: Levels of mRNA accumulate during early fruit development.
ALLERGEN: Causes an allergic reaction in human.
SIMILARITY: Belongs to the peptidase C1 family [view classification].
SEQUENCE CAUTION:
- Sequence=CAA31435.1; Type=Frameshift; Positions=371;
- Sequence=CAA31529.1; Type=Frameshift; Positions=371;

Copyright

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Cross-references

Sequence databases

EMBL

AF343446; AAK06862.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X13013; CAA31435.1; ALT_FRAME; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X13139; CAA31529.1; ALT_FRAME; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

PDB

1AEC; X-ray; 1.86 A; A=127-344.	[ExPASy / RCSB / EBI]
1F3Q; Model; -; A=127-344.	[ExPASy / RCSB / EBI]
1FOG; Model; -; A=127-344.	[ExPASy / RCSB / EBI]
1FTV; Model; -; A=127-344.	[ExPASy / RCSB / EBI]
2ACT; X-ray; 1.70 A; A=127-346.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1AEC; -.
1F3Q; -.
1FOG; -.
1FTV; -.
2ACT; -.

SMR

P00785; 127-343.

ModBase

P00785.

Protein family/group databases

MEROPS

C01.007; -.

Family and domain databases

InterPro

IPR000169; Pept_cys_AS.
IPR013128; Peptidase_C1A.
IPR000668; Peptidase_C1A_C.
IPR013201; Prot_inhib_I29.
Graphical view of domain structure.

PANTHER

PTHR12411; Peptidase_C1A; 1.

Pfam

PF08246; Inhibitor_I29; 1.
PF00112; Peptidase_C1; 1.
Pfam graphical view of domain structure.

PRINTS

PR00705; PAPAIN.

ProDom

PD000158; Peptidase_C1; 1.
[Domain structure / List of seq. sharing at least 1 domain]

SMART

SM00645; Pept_C1; 1.
SMART graphical view of domain structure.

PROSITE

PS00640; THIOL_PROTEASE_ASN; 1.
PS00139; THIOL_PROTEASE_CYS; 1.
PS00639; THIOL_PROTEASE_HIS; 1.

Other

P00785; -.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Allergen; Direct protein sequencing; Hydrolase; Protease; Signal; Thiol protease; Zymogen.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 24`	`24`	`Potential.`
`PROPEP`	`25 126`	`102`	`Activation peptide.`	`PRO_0000026398`
`CHAIN`	`127 380`	`254`	`Actinidain.`	`PRO_0000026399`
`ACT_SITE`	`151 151`
`ACT_SITE`	`288 288`
`ACT_SITE`	`308 308`
`DISULFID`	`148 191`
`DISULFID`	`182 224`
`DISULFID`	`282 332`
`CONFLICT`	`96 96`		`D -> G (in Ref. 2; CAA31435).`
`CONFLICT`	`105 105`		`R -> G (in Ref. 2; CAA31435).`
`CONFLICT`	`108 108`		`S -> G (in Ref. 2; CAA31435).`
`CONFLICT`	`124 124`		`G -> S (in Ref. 2; CAA31435).`
`CONFLICT`	`167 170`		`VTGV -> TSGS (in Ref. 3; AA sequence).`
`CONFLICT`	`181 181`		`D -> G (in Ref. 2; CAA31435).`
`CONFLICT`	`184 184`		`R -> G (in Ref. 2; CAA31435).`
`CONFLICT`	`192 192`		`N -> D (in Ref. 3; AA sequence).`
`CONFLICT`	`206 206`		`N -> D (in Ref. 3; AA sequence).`
`CONFLICT`	`212 212`		`E -> G (in Ref. 2; CAA31435).`
`CONFLICT`	`223 223`		`E -> D (in Ref. 3; AA sequence).`
`CONFLICT`	`225 225`		`N -> D (in Ref. 3; AA sequence).`
`CONFLICT`	`226 226`		`V -> L (in Ref. 2; CAA31435).`
`CONFLICT`	`227 227`		`D -> A (in Ref. 3; AA sequence).`
`CONFLICT`	`230 231`		`NE -> DQ (in Ref. 3; AA sequence).`
`CONFLICT`	`240 240`		`E -> G (in Ref. 2; CAA31435).`
`CONFLICT`	`272 272`		`Q -> H (in Ref. 2; CAA31435/CAA31529).`
`CONFLICT`	`274 274`		`S -> A (in Ref. 3; AA sequence).`
`CONFLICT`	`286 286`		`V -> I (in Ref. 2; CAA31435/CAA31529).`
`CONFLICT`	`290 291`		`VT -> IV (in Ref. 3; AA sequence).`
`CONFLICT`	`301 301`		`I -> V (in Ref. 3; AA sequence).`
`CONFLICT`	`307 307`		`K -> E (in Ref. 2; CAA31435).`
`CONFLICT`	`349 349`		`H -> Y (in Ref. 2; CAA31435/CAA31529).`
`CONFLICT`	`360 360`		`P -> S (in Ref. 2; CAA31435/CAA31529).`
`CONFLICT`	`373 373`		`D -> E (in Ref. 2; CAA31435/CAA31529).`
`CONFLICT`	`374 374`		`D -> H (in Ref. 2; CAA31529).`
`HELIX`	`133 136`	`4`
`HELIX`	`151 168`	`18`
`HELIX`	`176 182`	`7`
`HELIX`	`196 206`	`11`
`TURN`	`212 214`	`3`
`HELIX`	`226 230`	`5`
`STRAND`	`238 241`	`4`
`HELIX`	`247 256`	`10`
`STRAND`	`259 263`	`5`
`HELIX`	`268 272`	`5`
`STRAND`	`275 278`	`4`
`STRAND`	`288 298`	`11`
`STRAND`	`301 307`	`7`
`STRAND`	`319 323`	`5`
`HELIX`	`331 333`	`3`
`STRAND`	`339 342`	`4`

Sequence information

Length: 380 AA [This is the length of the unprocessed precursor]

Molecular weight: 42172 Da [This is the MW of the unprocessed precursor]

CRC64: 26BFDC612D53A50B [This is a checksum on the sequence]

        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

P00785 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools