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Protein

Papain

Gene
N/A
Organism
Carica papaya (Papaya)
Status
Reviewed-Annotation score: Annotation score: 4 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
  2. serpin family protein binding Source: UniProtKB
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 – 1818Sequence AnalysisAdd
BLAST
Propeptidei19 – 133115Activation peptide1 PublicationPRO_0000026406Add
BLAST
Chaini134 – 345212PapainPRO_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

1
345
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi41 – 5414Combined sources
Helixi62 – 8221Combined sources
Beta strandi88 – 914Combined sources
Turni95 – 984Combined sources
Helixi101 – 1088Combined sources
Beta strandi119 – 1246Combined sources
Turni140 – 1445Combined sources
Beta strandi154 – 1563Combined sources
Helixi158 – 17518Combined sources
Helixi183 – 1897Combined sources
Beta strandi191 – 1933Combined sources
Helixi195 – 1973Combined sources
Helixi201 – 21010Combined sources
Turni216 – 2183Combined sources
Beta strandi223 – 2253Combined sources
Turni230 – 2334Combined sources
Beta strandi241 – 2455Combined sources
Helixi251 – 26010Combined sources
Beta strandi263 – 2675Combined sources
Helixi272 – 2754Combined sources
Beta strandi279 – 2824Combined sources
Beta strandi292 – 3009Combined sources
Beta strandi303 – 3075Combined sources
Beta strandi312 – 3143Combined sources
Turni315 – 3173Combined sources
Beta strandi319 – 3235Combined sources
Beta strandi325 – 3273Combined sources
Helixi332 – 3343Combined sources
Beta strandi340 – 3434Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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[»]
4KP9X-ray2.10A/B134-345[»]
4PADX-ray2.80A134-345[»]
5PADX-ray2.80A134-345[»]
6PADX-ray2.80A134-345[»]
9PAPX-ray1.65A134-345[»]
ProteinModelPortaliP00784.
SMRiP00784. Positions 38-345.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00784.

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.

P00784-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAMIPSISKL LFVAICLFVY MGLSFGDFSI VGYSQNDLTS TERLIQLFES
60 70 80 90 100
WMLKHNKIYK NIDEKIYRFE IFKDNLKYID ETNKKNNSYW LGLNVFADMS
110 120 130 140 150
NDEFKEKYTG SIAGNYTTTE LSYEEVLNDG DVNIPEYVDW RQKGAVTPVK
160 170 180 190 200
NQGSCGSCWA FSAVVTIEGI IKIRTGNLNE YSEQELLDCD RRSYGCNGGY
210 220 230 240 250
PWSALQLVAQ YGIHYRNTYP YEGVQRYCRS REKGPYAAKT DGVRQVQPYN
260 270 280 290 300
EGALLYSIAN QPVSVVLEAA GKDFQLYRGG IFVGPCGNKV DHAVAAVGYG
310 320 330 340
PNYILIKNSW GTGWGENGYI RIKRGTGNSY GVCGLYTSSF YPVKN
Length:345
Mass (Da):38,922
Last modified:January 1, 1988 - v1
Checksum:i82D9FB35EDCA12EF
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti180 – 1801E → Q AA sequence (PubMed:5470818).Curated
Sequence conflicti219 – 2202YP → PY AA sequence (PubMed:5470818).Curated
Sequence conflicti251 – 2511E → Q AA sequence (PubMed:5470818).Curated
Sequence conflicti268 – 2681E → Q AA sequence (PubMed:5470818).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M15203 mRNA. Translation: AAB02650.1.
PIRiA26466. PPPA.

Cross-referencesi

Web resourcesi

Worthington enzyme manual

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M15203 mRNA. Translation: AAB02650.1.
PIRiA26466. PPPA.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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[»]
4KP9X-ray2.10A/B134-345[»]
4PADX-ray2.80A134-345[»]
5PADX-ray2.80A134-345[»]
6PADX-ray2.80A134-345[»]
9PAPX-ray1.65A134-345[»]
ProteinModelPortaliP00784.
SMRiP00784. Positions 38-345.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-1504623.

Chemistry

BindingDBiP00784.
ChEMBLiCHEMBL4779.

Protein family/group databases

Allergomei709. Car p 1.
MEROPSiC01.001.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.4.22.2. 1191.
SABIO-RKP00784.

Miscellaneous databases

EvolutionaryTraceiP00784.

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]
ProtoNetiSearch...

Publicationsi

  1. "Cloning and sequencing of papain-encoding cDNA."
    Cohen L.W., Coghlan V.M., Dihel L.C.
    Gene 48:219-227(1985) [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(1969) [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(1969) [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(1983) [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(1989) [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(1991) [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(1991)
    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: April 1, 2015
This is version 113 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.