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P00784

- PAPA1_CARPA

UniProt

P00784 - PAPA1_CARPA

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Protein
Papain
Gene
N/A
Organism
Carica papaya (Papaya)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

Hydrolysis of proteins with broad specificity for peptide bonds, but preference for an amino acid bearing a large hydrophobic side chain at the P2 position. Does not accept Val in P1'.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei158 – 15811 Publication
Active sitei292 – 2921
Active sitei308 – 30811 Publication

GO - Molecular functioni

  1. cysteine-type peptidase activity Source: UniProtKB-KW
Complete GO annotation...

GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase, Protease, Thiol protease

    Enzyme and pathway databases

    BRENDAi3.4.22.2. 1191.
    SABIO-RKP00784.

    Protein family/group databases

    MEROPSiC01.001.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Papain (EC:3.4.22.2)
    Alternative name(s):
    Papaya proteinase I
    Short name:
    PPI
    Allergen: Car p 1
    OrganismiCarica papaya (Papaya)
    Taxonomic identifieri3649 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesCaricaceaeCarica

    Pathology & Biotechi

    Allergenic propertiesi

    Causes an allergic reaction in human.

    Keywords - Diseasei

    Allergen

    Protein family/group databases

    Allergomei709. Car p 1.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1818 Reviewed prediction
    Add
    BLAST
    Propeptidei19 – 133115Activation peptide
    PRO_0000026406Add
    BLAST
    Chaini134 – 345212Papain
    PRO_0000026407Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi155 ↔ 1961 Publication
    Disulfide bondi189 ↔ 2281 Publication
    Disulfide bondi286 ↔ 3331 Publication

    Keywords - PTMi

    Disulfide bond, Zymogen

    Interactioni

    Protein-protein interaction databases

    MINTiMINT-1504623.

    Structurei

    Secondary structure

    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi41 – 5414
    Helixi62 – 8221
    Beta strandi88 – 914
    Turni95 – 984
    Helixi101 – 1088
    Beta strandi119 – 1246
    Turni140 – 1445
    Beta strandi154 – 1563
    Helixi158 – 17518
    Helixi183 – 1897
    Beta strandi191 – 1933
    Helixi195 – 1973
    Helixi201 – 21010
    Turni216 – 2183
    Beta strandi223 – 2253
    Turni230 – 2334
    Beta strandi241 – 2455
    Helixi251 – 26010
    Beta strandi263 – 2675
    Helixi272 – 2754
    Beta strandi279 – 2824
    Beta strandi292 – 3009
    Beta strandi303 – 3075
    Beta strandi312 – 3143
    Turni315 – 3173
    Beta strandi319 – 3235
    Beta strandi325 – 3273
    Helixi332 – 3343
    Beta strandi340 – 3434

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1BP4X-ray2.20A134-345[»]
    1BQIX-ray2.50A134-345[»]
    1CVZX-ray1.70A134-345[»]
    1EFFmodel-A134-345[»]
    1KHPX-ray2.00A134-345[»]
    1KHQX-ray1.60A134-345[»]
    1PADX-ray2.80A134-345[»]
    1PE6X-ray2.10A134-345[»]
    1PIPX-ray1.70A134-345[»]
    1POPX-ray2.10A134-345[»]
    1PPDX-ray2.00A134-345[»]
    1PPNX-ray1.60A134-345[»]
    1PPPX-ray1.90A134-345[»]
    1STFX-ray2.37E134-345[»]
    2CIOX-ray1.50A134-345[»]
    2PADX-ray2.80A134-345[»]
    3E1ZX-ray1.86B134-345[»]
    3IMAX-ray2.03A/C134-345[»]
    3LFYX-ray2.60A/C134-345[»]
    3TNXX-ray2.62A/C27-345[»]
    3USVX-ray3.80A/C27-345[»]
    4PADX-ray2.80A134-345[»]
    5PADX-ray2.80A134-345[»]
    6PADX-ray2.80A134-345[»]
    9PAPX-ray1.65A134-345[»]
    ProteinModelPortaliP00784.
    SMRiP00784. Positions 38-345.

    Miscellaneous databases

    EvolutionaryTraceiP00784.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase C1 family.

    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.

    P00784-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAMIPSISKL LFVAICLFVY MGLSFGDFSI VGYSQNDLTS TERLIQLFES    50
    WMLKHNKIYK NIDEKIYRFE IFKDNLKYID ETNKKNNSYW LGLNVFADMS 100
    NDEFKEKYTG SIAGNYTTTE LSYEEVLNDG DVNIPEYVDW RQKGAVTPVK 150
    NQGSCGSCWA FSAVVTIEGI IKIRTGNLNE YSEQELLDCD RRSYGCNGGY 200
    PWSALQLVAQ YGIHYRNTYP YEGVQRYCRS REKGPYAAKT DGVRQVQPYN 250
    EGALLYSIAN QPVSVVLEAA GKDFQLYRGG IFVGPCGNKV DHAVAAVGYG 300
    PNYILIKNSW GTGWGENGYI RIKRGTGNSY GVCGLYTSSF YPVKN 345
    Length:345
    Mass (Da):38,922
    Last modified:January 1, 1988 - v1
    Checksum:i82D9FB35EDCA12EF
    GO

    Sequence conflict

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti180 – 1801E → Q AA sequence 1 Publication
    Sequence conflicti219 – 2202YP → PY AA sequence 1 Publication
    Sequence conflicti251 – 2511E → Q AA sequence 1 Publication
    Sequence conflicti268 – 2681E → Q AA sequence 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M15203 mRNA. Translation: AAB02650.1.
    PIRiA26466. PPPA.

    Cross-referencesi

    Web resourcesi

    Worthington enzyme manual

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M15203 mRNA. Translation: AAB02650.1 .
    PIRi A26466. PPPA.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1BP4 X-ray 2.20 A 134-345 [» ]
    1BQI X-ray 2.50 A 134-345 [» ]
    1CVZ X-ray 1.70 A 134-345 [» ]
    1EFF model - A 134-345 [» ]
    1KHP X-ray 2.00 A 134-345 [» ]
    1KHQ X-ray 1.60 A 134-345 [» ]
    1PAD X-ray 2.80 A 134-345 [» ]
    1PE6 X-ray 2.10 A 134-345 [» ]
    1PIP X-ray 1.70 A 134-345 [» ]
    1POP X-ray 2.10 A 134-345 [» ]
    1PPD X-ray 2.00 A 134-345 [» ]
    1PPN X-ray 1.60 A 134-345 [» ]
    1PPP X-ray 1.90 A 134-345 [» ]
    1STF X-ray 2.37 E 134-345 [» ]
    2CIO X-ray 1.50 A 134-345 [» ]
    2PAD X-ray 2.80 A 134-345 [» ]
    3E1Z X-ray 1.86 B 134-345 [» ]
    3IMA X-ray 2.03 A/C 134-345 [» ]
    3LFY X-ray 2.60 A/C 134-345 [» ]
    3TNX X-ray 2.62 A/C 27-345 [» ]
    3USV X-ray 3.80 A/C 27-345 [» ]
    4PAD X-ray 2.80 A 134-345 [» ]
    5PAD X-ray 2.80 A 134-345 [» ]
    6PAD X-ray 2.80 A 134-345 [» ]
    9PAP X-ray 1.65 A 134-345 [» ]
    ProteinModelPortali P00784.
    SMRi P00784. Positions 38-345.
    ModBasei Search...

    Protein-protein interaction databases

    MINTi MINT-1504623.

    Chemistry

    BindingDBi P00784.
    ChEMBLi CHEMBL4779.

    Protein family/group databases

    Allergomei 709. Car p 1.
    MEROPSi C01.001.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    BRENDAi 3.4.22.2. 1191.
    SABIO-RK P00784.

    Miscellaneous databases

    EvolutionaryTracei P00784.

    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. "Cloning and sequencing of papain-encoding cDNA."
      Cohen L.W., Coghlan V.M., Dihel L.C.
      Gene 48:219-227(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "The complete amino acid sequence of papain. Additions and corrections."
      Mitchel R.E.J., Chaiken I.M., Smith E.L.
      J. Biol. Chem. 245:3485-3492(1970) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 134-345.
    3. "A reinvestigation of residues 64-68 and 175 in papain. Evidence that residues 64 and 175 are asparagine."
      Husain S.S., Lowe G.
      Biochem. J. 116:689-692(1970) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION TO 197.
    4. Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
    5. "Structure of papain refined at 1.65-A resolution."
      Kamphuis I.G., Kalk K.H., Swarte M.B.A., Drenth J.
      J. Mol. Biol. 179:233-256(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS).
    6. "The refined 2.4 A X-ray crystal structure of recombinant human stefin B in complex with the cysteine proteinase papain: a novel type of proteinase inhibitor interaction."
      Stubbs M.T., Laber B., Bode W., Huber R., Jerala R., Lenarcic B., Turk V.
      EMBO J. 9:1939-1947(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
    7. "Crystal structure of papain-succinyl-Gln-Val-Val-Ala-Ala-p-nitroanilide complex at 1.7-A resolution: noncovalent binding mode of a common sequence of endogenous thiol protease inhibitors."
      Yamamoto A., Tomoo K., Doi M., Ohishi H., Inoue M., Ishida T., Yamamoto D., Tsuboi S., Okamoto H., Okada Y.
      Biochemistry 31:11305-11309(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
    8. "Structure of monoclinic papain at 1.60-A resolution."
      Pickersgill R.W., Harris G.W., Garman E.
      Acta Crystallogr. B 48:59-67(1992)
      Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).

    Entry informationi

    Entry nameiPAPA1_CARPA
    AccessioniPrimary (citable) accession number: P00784
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 1, 1988
    Last modified: May 14, 2014
    This is version 109 of the entry and version 1 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

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