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P00785

- ACTN_ACTCH

UniProt

P00785 - ACTN_ACTCH

Protein

Actinidain

Gene
N/A
Organism
Actinidia chinensis (Kiwi) (Yangtao)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 103 (01 Oct 2014)
      Sequence version 4 (10 Jun 2008)
      Previous versions | rss
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    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

    1. cysteine-type peptidase activity Source: UniProtKB-KW

    Keywords - Molecular functioni

    Hydrolase, Protease, Thiol protease

    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 – 1364
    Helixi151 – 16818
    Helixi176 – 1827
    Helixi190 – 1923
    Helixi196 – 20611
    Turni212 – 2143
    Helixi226 – 2305
    Beta strandi238 – 2414
    Helixi247 – 25610
    Beta strandi259 – 2635
    Helixi268 – 2725
    Beta strandi275 – 2784
    Beta strandi288 – 29811
    Beta strandi301 – 3077
    Beta strandi319 – 3235
    Helixi331 – 3333
    Beta strandi339 – 3424

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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

    MGLPKSFVSM SLLFFSTLLI LSLAFNAKNL TQRTNDEVKA MYESWLIKYG    50
    KSYNSLGEWE RRFEIFKETL RFIDEHNADT NRSYKVGLNQ FADLTDEEFR 100
    STYLRFTSGS NKTKVSNRYE PRVGQVLPSY VDWRSAGAVV DIKSQGECGG 150
    CWAFSAIATV EGINKIVTGV LISLSEQELI DCGRTQNTRG CNGGYITDGF 200
    QFIINNGGIN TEENYPYTAQ DGECNVDLQN EKYVTIDTYE NVPYNNEWAL 250
    QTAVTYQPVS VALDAAGDAF KQYSSGIFTG PCGTAVDHAV TIVGYGTEGG 300
    IDYWIVKNSW DTTWGEEGYM RILRNVGGAG TCGIATMPSY PVKYNNQNHP 350
    KPYSSLINPP AFSMSKDGPV GVDDGQRYSA 380
    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.
    The sequence CAA31529.1 differs from that shown. Reason: Frameshift at position 371.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti96 – 961D → G in CAA31435. 1 PublicationCurated
    Sequence conflicti105 – 1051R → G in CAA31435. 1 PublicationCurated
    Sequence conflicti108 – 1081S → G in CAA31435. 1 PublicationCurated
    Sequence conflicti124 – 1241G → S in CAA31435. 1 PublicationCurated
    Sequence conflicti167 – 1704VTGV → TSGS AA sequence (PubMed:687380)Curated
    Sequence conflicti181 – 1811D → G in CAA31435. 1 PublicationCurated
    Sequence conflicti184 – 1841R → G in CAA31435. 1 PublicationCurated
    Sequence conflicti192 – 1921N → D AA sequence (PubMed:687380)Curated
    Sequence conflicti206 – 2061N → D AA sequence (PubMed:687380)Curated
    Sequence conflicti212 – 2121E → G in CAA31435. 1 PublicationCurated
    Sequence conflicti223 – 2231E → D AA sequence (PubMed:687380)Curated
    Sequence conflicti225 – 2251N → D AA sequence (PubMed:687380)Curated
    Sequence conflicti226 – 2261V → L in CAA31435. 1 PublicationCurated
    Sequence conflicti227 – 2271D → A AA sequence (PubMed:687380)Curated
    Sequence conflicti230 – 2312NE → DQ AA sequence (PubMed:687380)Curated
    Sequence conflicti240 – 2401E → G in CAA31435. 1 PublicationCurated
    Sequence conflicti272 – 2721Q → H in CAA31435. 1 PublicationCurated
    Sequence conflicti272 – 2721Q → H in CAA31529. 1 PublicationCurated
    Sequence conflicti274 – 2741S → A AA sequence (PubMed:687380)Curated
    Sequence conflicti286 – 2861V → I in CAA31435. 1 PublicationCurated
    Sequence conflicti286 – 2861V → I in CAA31529. 1 PublicationCurated
    Sequence conflicti290 – 2912VT → IV AA sequence (PubMed:687380)Curated
    Sequence conflicti301 – 3011I → V AA sequence (PubMed:687380)Curated
    Sequence conflicti307 – 3071K → E in CAA31435. 1 PublicationCurated
    Sequence conflicti349 – 3491H → Y in CAA31435. 1 PublicationCurated
    Sequence conflicti349 – 3491H → Y in CAA31529. 1 PublicationCurated
    Sequence conflicti360 – 3601P → S in CAA31435. 1 PublicationCurated
    Sequence conflicti360 – 3601P → S in CAA31529. 1 PublicationCurated
    Sequence conflicti373 – 3731D → E in CAA31435. 1 PublicationCurated
    Sequence conflicti373 – 3731D → E in CAA31529. 1 PublicationCurated
    Sequence conflicti374 – 3741D → H in CAA31529. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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 [» ]
    ProteinModelPortali P00785.
    SMRi P00785. Positions 127-343.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    Allergomei 1. Act d 1.
    3052. Act d 1.0101.
    MEROPSi C01.007.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P00785.

    Family and domain databases

    InterProi 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 ]
    PANTHERi PTHR12411. PTHR12411. 1 hit.
    Pfami PF08246. Inhibitor_I29. 1 hit.
    PF00112. Peptidase_C1. 1 hit.
    [Graphical view ]
    PRINTSi PR00705. PAPAIN.
    SMARTi SM00848. Inhibitor_I29. 1 hit.
    SM00645. Pept_C1. 1 hit.
    [Graphical view ]
    PROSITEi PS00640. THIOL_PROTEASE_ASN. 1 hit.
    PS00139. THIOL_PROTEASE_CYS. 1 hit.
    PS00639. THIOL_PROTEASE_HIS. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    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: October 1, 2014
    This is version 103 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