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P10056

- PAPA3_CARPA

UniProt

P10056 - PAPA3_CARPA

Protein

Caricain

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 101 (01 Oct 2014)
      Sequence version 2 (01 Oct 1996)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    Hydrolysis of proteins with broad specificity for peptide bonds, similar to those of papain and chymopapain.

    Sites

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

    GO - Molecular functioni

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

    Keywords - Molecular functioni

    Hydrolase, Protease, Thiol protease

    Enzyme and pathway databases

    BRENDAi3.4.22.30. 1191.

    Protein family/group databases

    MEROPSiC01.003.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Caricain (EC:3.4.22.30)
    Alternative name(s):
    Papaya peptidase A
    Papaya proteinase III
    Short name:
    PPIII
    Papaya proteinase omega
    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 – 1616Sequence AnalysisAdd
    BLAST
    Propeptidei17 – 132116Activation peptide1 PublicationPRO_0000026410Add
    BLAST
    Chaini133 – 348216CaricainPRO_0000026411Add
    BLAST

    Amino acid modifications

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

    Keywords - PTMi

    Disulfide bond, Zymogen

    Interactioni

    Subunit structurei

    Monomer.

    Structurei

    Secondary structure

    1
    348
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi40 – 5314
    Turni54 – 563
    Helixi62 – 8322
    Beta strandi88 – 914
    Turni95 – 984
    Helixi101 – 1088
    Beta strandi122 – 1243
    Turni139 – 1435
    Beta strandi153 – 1553
    Helixi157 – 17418
    Helixi182 – 1887
    Beta strandi190 – 1923
    Helixi194 – 1963
    Helixi200 – 21011
    Beta strandi212 – 2143
    Turni215 – 2173
    Helixi229 – 2313
    Beta strandi241 – 2444
    Beta strandi247 – 2493
    Helixi250 – 25910
    Beta strandi262 – 2665
    Helixi271 – 2755
    Beta strandi278 – 2814
    Beta strandi291 – 30111
    Beta strandi304 – 3107
    Beta strandi315 – 3173
    Beta strandi322 – 3265
    Beta strandi330 – 3334
    Helixi335 – 3373
    Beta strandi343 – 3464

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1C7Xmodel-A133-348[»]
    1EUXmodel-A133-348[»]
    1F1Imodel-A133-348[»]
    1MEGX-ray2.00A133-348[»]
    1PCIX-ray3.20A/B/C27-348[»]
    1PPOX-ray1.80A133-348[»]
    ProteinModelPortaliP10056.
    SMRiP10056. Positions 38-348.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP10056.

    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.

    P10056-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAMIPSISKL LFVAICLFVH MSVSFGDFSI VGYSQDDLTS TERLIQLFNS    50
    WMLNHNKFYE NVDEKLYRFE IFKDNLNYID ETNKKNNSYW LGLNEFADLS 100
    NDEFNEKYVG SLIDATIEQS YDEEFINEDT VNLPENVDWR KKGAVTPVRH 150
    QGSCGSCWAF SAVATVEGIN KIRTGKLVEL SEQELVDCER RSHGCKGGYP 200
    PYALEYVAKN GIHLRSKYPY KAKQGTCRAK QVGGPIVKTS GVGRVQPNNE 250
    GNLLNAIAKQ PVSVVVESKG RPFQLYKGGI FEGPCGTKVD HAVTAVGYGK 300
    SGGKGYILIK NSWGTAWGEK GYIRIKRAPG NSPGVCGLYK SSYYPTKN 348
    Length:348
    Mass (Da):38,788
    Last modified:October 1, 1996 - v2
    Checksum:i328F5C6BF45B4A07
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X66060 mRNA. Translation: CAA46862.1.
    X51899 mRNA. Translation: CAA36180.1.
    PIRiJN0633.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X66060 mRNA. Translation: CAA46862.1 .
    X51899 mRNA. Translation: CAA36180.1 .
    PIRi JN0633.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1C7X model - A 133-348 [» ]
    1EUX model - A 133-348 [» ]
    1F1I model - A 133-348 [» ]
    1MEG X-ray 2.00 A 133-348 [» ]
    1PCI X-ray 3.20 A/B/C 27-348 [» ]
    1PPO X-ray 1.80 A 133-348 [» ]
    ProteinModelPortali P10056.
    SMRi P10056. Positions 38-348.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    Allergomei 1539. Car p Endoproteinase.
    MEROPSi C01.003.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    BRENDAi 3.4.22.30. 1191.

    Miscellaneous databases

    EvolutionaryTracei P10056.

    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. Baker K.C., Revell D.F., Cummings N.J., Collins M.E., Goodenough P.W.
      Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Leaf.
    2. "The thiol proteinases from the latex of Carica papaya L. II. The primary structure of proteinase omega."
      Dubois T., Kleinschmidt T., Schnek A.G., Looze Y., Braunitzer G.
      Biol. Chem. Hoppe-Seyler 369:741-754(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 133-348.
    3. Collins M.E., Revell D.F., Sumner I.G., Pickersgill R.W., Goodenough P.W.
      Submitted (FEB-1990) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 237-348.
      Tissue: Leaf.
    4. "Determination of the structure of papaya protease omega."
      Pickersgill R.W., Rizkallah P., Harris G.W., Goodenough P.W.
      Acta Crystallogr. B 47:766-771(1991)
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
    5. "Crystal structure of a caricain D158E mutant in complex with E-64."
      Katerelos N.A., Taylor M.A.J., Scott M., Goodenough P.W., Pickersgill R.W.
      FEBS Lett. 392:35-39(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF MUTANT GLU-290.
    6. "The prosequence of procaricain forms an alpha-helical domain that prevents access to the substrate-binding cleft."
      Groves M.R., Taylor M.A., Scott M., Cummings N.J., Pickersgill R.W., Jenkins J.A.
      Structure 4:1193-1203(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF PRO-CARICAIN.
    7. "Theoretical model structure of a caricain D158E mutant in complex with E-64C."
      Bhattacharya S., Pal A., Bera A., Chakraborty S., Banerjee A.
      Submitted (APR-2000) to the PDB data bank
      Cited for: 3D-STRUCTURE MODELING OF 133-348.

    Entry informationi

    Entry nameiPAPA3_CARPA
    AccessioniPrimary (citable) accession number: P10056
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 101 of the entry and version 2 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. 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