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P05994 (PAPA4_CARPA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Papaya proteinase 4

EC=3.4.22.25
Alternative name(s):
Glycyl endopeptidase
Papaya peptidase B
Papaya proteinase IV
Short name=PPIV
OrganismCarica papaya (Papaya)
Taxonomic identifier3649 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesCaricaceaeCarica

Protein attributes

Sequence length348 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

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

Enzyme regulation

Not inhibited by cystatin.

Miscellaneous

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

Sequence similarities

Belongs to the peptidase C1 family.

Ontologies

Keywords
   DomainSignal
   Molecular functionHydrolase
Protease
Thiol protease
   PTMDisulfide bond
Zymogen
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   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 – 132114Activation peptide
PRO_0000026412
Chain133 – 348216Papaya proteinase 4
PRO_0000026413

Sites

Active site1571 By similarity
Active site2911 By similarity
Active site3111 By similarity

Amino acid modifications

Disulfide bond154 ↔ 195
Disulfide bond188 ↔ 227
Disulfide bond285 ↔ 336

Experimental info

Sequence conflict1901K → L AA sequence Ref.2

Secondary structure

..................................... 348
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P05994 [UniParc].

Last modified October 1, 1996. Version 3.
Checksum: 40855EDD37F68A8E

FASTA34839,024
        10         20         30         40         50         60 
MAIICSFSKL LFVAICLFGH MSLSYCDFSI VGYSQDDLTS TERLIQLFNS WMLKHNKNYK 

        70         80         90        100        110        120 
NVDEKLYRFE IFKDNLKYID ERNKMINGYW LGLNEFSDLS NDEFKEKYVG SLPEDYTNQP 

       130        140        150        160        170        180 
YDEEFVNEDI VDLPESVDWR AKGAVTPVKH QGYCESCWAF STVATVEGIN KIKTGNLVEL 

       190        200        210        220        230        240 
SEQELVDCDK QSYGCNRGYQ STSLQYVAQN GIHLRAKYPY IAKQQTCRAN QVGGPKVKTN 

       250        260        270        280        290        300 
GVGRVQSNNE GSLLNAIAHQ PVSVVVESAG RDFQNYKGGI FEGSCGTKVD HAVTAVGYGK 

       310        320        330        340 
SGGKGYILIK NSWGPGWGEN GYIRIRRASG NSPGVCGVYR SSYYPIKN 

« Hide

References

[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]"Papaya proteinase IV amino acid sequence."
Ritonja A., Buttle D.J., Rawlings N.D., Turk V., Barrett A.J.
FEBS Lett. 258:109-112(1989) [PubMed] [Europe PMC] [Abstract]
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).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X78056 mRNA. Translation: CAA54974.1.
X03970 mRNA. Translation: CAA27608.1.
PIRS06837.
T09798.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1GECX-ray2.10E133-348[»]
ProteinModelPortalP05994.
SMRP05994. Positions 38-348.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

Allergome1539. Car p Endoproteinase.
MEROPSC01.004.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BRENDA3.4.22.25. 1191.
SABIO-RKP05994.

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

EvolutionaryTraceP05994.

Entry information

Entry namePAPA4_CARPA
AccessionPrimary (citable) accession number: P05994
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: October 1, 1996
Last modified: May 14, 2014
This is version 98 of the entry and version 3 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