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P00784 (PAPA1_CARPA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Papain

EC=3.4.22.2
Alternative name(s):
Papaya proteinase I
Short name=PPI
Allergen=Car p 1
OrganismCarica papaya (Papaya)
Taxonomic identifier3649 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesCaricaceaeCarica

Protein attributes

Sequence length345 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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'.

Allergenic properties

Causes an allergic reaction in human.

Sequence similarities

Belongs to the peptidase C1 family.

Ontologies

Keywords
   DiseaseAllergen
   DomainSignal
   Molecular functionHydrolase
Protease
Thiol protease
   PTMDisulfide bond
Zymogen
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processproteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functioncysteine-type peptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Potential
Propeptide19 – 133115Activation peptide
PRO_0000026406
Chain134 – 345212Papain
PRO_0000026407

Sites

Active site1581 Ref.4
Active site2921
Active site3081 Ref.4

Amino acid modifications

Disulfide bond155 ↔ 196 Ref.2
Disulfide bond189 ↔ 228 Ref.2
Disulfide bond286 ↔ 333 Ref.2

Experimental info

Sequence conflict1801E → Q AA sequence Ref.2
Sequence conflict219 – 2202YP → PY AA sequence Ref.2
Sequence conflict2511E → Q AA sequence Ref.2
Sequence conflict2681E → Q AA sequence Ref.2

Secondary structure

.......................................................... 345
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00784 [UniParc].

Last modified January 1, 1988. Version 1.
Checksum: 82D9FB35EDCA12EF

FASTA34538,922
        10         20         30         40         50         60 
MAMIPSISKL LFVAICLFVY MGLSFGDFSI VGYSQNDLTS TERLIQLFES WMLKHNKIYK 

        70         80         90        100        110        120 
NIDEKIYRFE IFKDNLKYID ETNKKNNSYW LGLNVFADMS NDEFKEKYTG SIAGNYTTTE 

       130        140        150        160        170        180 
LSYEEVLNDG DVNIPEYVDW RQKGAVTPVK NQGSCGSCWA FSAVVTIEGI IKIRTGNLNE 

       190        200        210        220        230        240 
YSEQELLDCD RRSYGCNGGY PWSALQLVAQ YGIHYRNTYP YEGVQRYCRS REKGPYAAKT 

       250        260        270        280        290        300 
DGVRQVQPYN EGALLYSIAN QPVSVVLEAA GKDFQLYRGG IFVGPCGNKV DHAVAAVGYG 

       310        320        330        340 
PNYILIKNSW GTGWGENGYI RIKRGTGNSY GVCGLYTSSF YPVKN 

« Hide

References

[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]"Structure of papain."
Drenth J., Jansonius J.N., Koekoek R., Swen H.M., Wolthers B.G.
Nature 218:929-932(1968) [PubMed] [Europe PMC] [Abstract]
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).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M15203 mRNA. Translation: AAB02650.1.
PIRPPPA. A26466.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP00784.
SMRP00784. Positions 38-345.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-1504623.

Chemistry

BindingDBP00784.
ChEMBLCHEMBL4779.

Protein family/group databases

Allergome709. Car p 1.
MEROPSC01.001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BRENDA3.4.22.2. 1191.
SABIO-RKP00784.

Family and domain databases

InterProIPR025661. Pept_asp_AS.
IPR000169. Pept_cys_AS.
IPR025660. Pept_his_AS.
IPR013128. Peptidase_C1A.
IPR000668. Peptidase_C1A_C.
IPR013201. Prot_inhib_I29.
[Graphical view]
PANTHERPTHR12411. PTHR12411. 1 hit.
PfamPF08246. Inhibitor_I29. 1 hit.
PF00112. Peptidase_C1. 1 hit.
[Graphical view]
PRINTSPR00705. PAPAIN.
SMARTSM00848. Inhibitor_I29. 1 hit.
SM00645. Pept_C1. 1 hit.
[Graphical view]
PROSITEPS00640. THIOL_PROTEASE_ASN. 1 hit.
PS00139. THIOL_PROTEASE_CYS. 1 hit.
PS00639. THIOL_PROTEASE_HIS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP00784.

Entry information

Entry namePAPA1_CARPA
AccessionPrimary (citable) accession number: P00784
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 1, 1988
Last modified: February 19, 2014
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Allergens

Nomenclature of allergens and list of entries