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P05994

- PAPA4_CARPA

UniProt

P05994 - PAPA4_CARPA

Protein

Papaya proteinase 4

Gene
N/A
Organism
Carica papaya (Papaya)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 99 (01 Oct 2014)
      Sequence version 3 (01 Oct 1996)
      Previous versions | rss
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    Functioni

    Thiol protease with a substrate specificity very different from the other thiol proteases.

    Catalytic activityi

    Preferential cleavage: Gly-|-Xaa, in proteins and in small molecule substrates.

    Enzyme regulationi

    Not inhibited by cystatin.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei157 – 1571By similarity
    Active sitei291 – 2911By similarity
    Active sitei311 – 3111By similarity

    GO - Molecular functioni

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

    Keywords - Molecular functioni

    Hydrolase, Protease, Thiol protease

    Enzyme and pathway databases

    BRENDAi3.4.22.25. 1191.
    SABIO-RKP05994.

    Protein family/group databases

    MEROPSiC01.004.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Papaya proteinase 4 (EC:3.4.22.25)
    Alternative name(s):
    Glycyl endopeptidase
    Papaya peptidase B
    Papaya proteinase IV
    Short name:
    PPIV
    OrganismiCarica papaya (Papaya)
    Taxonomic identifieri3649 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesCaricaceaeCarica

    Pathology & Biotechi

    Protein family/group databases

    Allergomei1539. Car p Endoproteinase.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1818Sequence AnalysisAdd
    BLAST
    Propeptidei19 – 132114Activation peptide2 PublicationsPRO_0000026412Add
    BLAST
    Chaini133 – 348216Papaya proteinase 4PRO_0000026413Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi154 ↔ 195
    Disulfide bondi188 ↔ 227
    Disulfide bondi285 ↔ 336

    Keywords - PTMi

    Disulfide bond, Zymogen

    Structurei

    Secondary structure

    1
    348
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni139 – 1435
    Beta strandi153 – 1553
    Helixi157 – 17418
    Helixi182 – 1887
    Beta strandi190 – 1923
    Helixi200 – 21011
    Turni215 – 2173
    Helixi229 – 2324
    Beta strandi241 – 2444
    Helixi250 – 2578
    Beta strandi262 – 2665
    Helixi271 – 2744
    Beta strandi278 – 2814
    Beta strandi291 – 30111
    Beta strandi304 – 3107
    Beta strandi322 – 3265
    Helixi335 – 3373
    Beta strandi343 – 3464

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1GECX-ray2.10E133-348[»]
    ProteinModelPortaliP05994.
    SMRiP05994. Positions 38-348.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP05994.

    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.

    P05994-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAIICSFSKL LFVAICLFGH MSLSYCDFSI VGYSQDDLTS TERLIQLFNS    50
    WMLKHNKNYK NVDEKLYRFE IFKDNLKYID ERNKMINGYW LGLNEFSDLS 100
    NDEFKEKYVG SLPEDYTNQP YDEEFVNEDI VDLPESVDWR AKGAVTPVKH 150
    QGYCESCWAF STVATVEGIN KIKTGNLVEL SEQELVDCDK QSYGCNRGYQ 200
    STSLQYVAQN GIHLRAKYPY IAKQQTCRAN QVGGPKVKTN GVGRVQSNNE 250
    GSLLNAIAHQ PVSVVVESAG RDFQNYKGGI FEGSCGTKVD HAVTAVGYGK 300
    SGGKGYILIK NSWGPGWGEN GYIRIRRASG NSPGVCGVYR SSYYPIKN 348
    Length:348
    Mass (Da):39,024
    Last modified:October 1, 1996 - v3
    Checksum:i40855EDD37F68A8E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti190 – 1901K → L AA sequence (PubMed:2591528)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X78056 mRNA. Translation: CAA54974.1.
    X03970 mRNA. Translation: CAA27608.1.
    PIRiS06837.
    T09798.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X78056 mRNA. Translation: CAA54974.1 .
    X03970 mRNA. Translation: CAA27608.1 .
    PIRi S06837.
    T09798.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1GEC X-ray 2.10 E 133-348 [» ]
    ProteinModelPortali P05994.
    SMRi P05994. Positions 38-348.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    Allergomei 1539. Car p Endoproteinase.
    MEROPSi C01.004.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    BRENDAi 3.4.22.25. 1191.
    SABIO-RK P05994.

    Miscellaneous databases

    EvolutionaryTracei P05994.

    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. "Recombinant pro-regions from papain and papaya proteinase IV-are selective high affinity inhibitors of the mature papaya enzymes."
      Taylor M.A., Baker K.C., Briggs G.S., Connerton I.F., Cummings N.J., Pratt K.A., Revell D.F., Freedman R.B., Goodenough P.W.
      Protein Eng. 8:59-62(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Leaf.
    2. Cited for: PROTEIN SEQUENCE OF 133-348.
    3. "N-terminal homology in three cysteinyl proteases from Papaya latex."
      Lynn K.R., Yaguchi M.
      Biochim. Biophys. Acta 581:363-364(1979) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 133-150.
    4. "Molecular cloning of two cysteine proteinases from paw-paw (Carica papaya)."
      McKee R.A., Adams S., Matthews J.A., Smith C.J., Smith H.
      Biochem. J. 237:105-110(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 287-348.
    5. "Selective cleavage of glycyl bonds by papaya proteinase IV."
      Buttle D.J., Ritonja A., Pearl L.H., Turk V., Barrett A.J.
      FEBS Lett. 260:195-197(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBSTRATE SPECIFICITY.
    6. "Crystal structure of glycyl endopeptidase from Carica papaya: a cysteine endopeptidase of unusual substrate specificity."
      O'Hara B.P., Hemmings A.M., Buttle D.J., Pearl L.H.
      Biochemistry 34:13190-13195(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).

    Entry informationi

    Entry nameiPAPA4_CARPA
    AccessioniPrimary (citable) accession number: P05994
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1988
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 99 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Substitution of the conserved Gly residue by Glu-155 could possibly explain the unusual specificity.

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3