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Protein

Papaya proteinase 4

Gene
N/A
Organism
Carica papaya (Papaya)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Enzyme regulationi

Not inhibited by cystatin.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei157By similarity1
Active sitei291By similarity1
Active sitei311By similarity1

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Enzyme and pathway databases

BRENDAi3.4.22.25. 1191.
SABIO-RKP05994.

Protein family/group databases

MEROPSiI29.003.

Names & Taxonomyi

Protein namesi
Recommended name:
Papaya proteinase 4 (EC:3.4.22.25)
Alternative name(s):
Glycyl endopeptidase
Papaya peptidase B
Papaya proteinase IV
Short name:
PPIV
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)DescriptionActionsGraphical viewLength
Signal peptidei1 – 18Sequence analysisAdd BLAST18
PropeptideiPRO_000002641219 – 132Activation peptide2 PublicationsAdd BLAST114
ChainiPRO_0000026413133 – 348Papaya proteinase 4Add BLAST216

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi154 ↔ 195
Disulfide bondi188 ↔ 227
Disulfide bondi285 ↔ 336

Keywords - PTMi

Disulfide bond, Zymogen

Proteomic databases

PRIDEiP05994.

Structurei

Secondary structure

1348
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni139 – 143Combined sources5
Beta strandi153 – 155Combined sources3
Helixi157 – 174Combined sources18
Helixi182 – 188Combined sources7
Beta strandi190 – 192Combined sources3
Helixi200 – 210Combined sources11
Turni215 – 217Combined sources3
Helixi229 – 232Combined sources4
Beta strandi241 – 244Combined sources4
Helixi250 – 257Combined sources8
Beta strandi262 – 266Combined sources5
Helixi271 – 274Combined sources4
Beta strandi278 – 281Combined sources4
Beta strandi291 – 301Combined sources11
Beta strandi304 – 310Combined sources7
Beta strandi322 – 326Combined sources5
Helixi335 – 337Combined sources3
Beta strandi343 – 346Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1GECX-ray2.10E133-348[»]
ProteinModelPortaliP05994.
SMRiP05994.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP05994.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase C1 family.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

KOiK20740.

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.

P05994-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAIICSFSKL LFVAICLFGH MSLSYCDFSI VGYSQDDLTS TERLIQLFNS
60 70 80 90 100
WMLKHNKNYK NVDEKLYRFE IFKDNLKYID ERNKMINGYW LGLNEFSDLS
110 120 130 140 150
NDEFKEKYVG SLPEDYTNQP YDEEFVNEDI VDLPESVDWR AKGAVTPVKH
160 170 180 190 200
QGYCESCWAF STVATVEGIN KIKTGNLVEL SEQELVDCDK QSYGCNRGYQ
210 220 230 240 250
STSLQYVAQN GIHLRAKYPY IAKQQTCRAN QVGGPKVKTN GVGRVQSNNE
260 270 280 290 300
GSLLNAIAHQ PVSVVVESAG RDFQNYKGGI FEGSCGTKVD HAVTAVGYGK
310 320 330 340
SGGKGYILIK NSWGPGWGEN GYIRIRRASG NSPGVCGVYR SSYYPIKN
Length:348
Mass (Da):39,024
Last modified:October 1, 1996 - v3
Checksum:i40855EDD37F68A8E
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti190K → L AA sequence (PubMed:2591528).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X78056 mRNA. Translation: CAA54974.1.
X03970 mRNA. Translation: CAA27608.1.
PIRiS06837.
T09798.

Genome annotation databases

KEGGiag:CAA54974.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X78056 mRNA. Translation: CAA54974.1.
X03970 mRNA. Translation: CAA27608.1.
PIRiS06837.
T09798.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1GECX-ray2.10E133-348[»]
ProteinModelPortaliP05994.
SMRiP05994.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

Allergomei1539. Car p Endoproteinase.
MEROPSiI29.003.

Proteomic databases

PRIDEiP05994.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:CAA54974.

Phylogenomic databases

KOiK20740.

Enzyme and pathway databases

BRENDAi3.4.22.25. 1191.
SABIO-RKP05994.

Miscellaneous databases

EvolutionaryTraceiP05994.

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...

Entry informationi

Entry nameiPAPA4_CARPA
AccessioniPrimary (citable) accession number: P05994
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: October 1, 1996
Last modified: November 2, 2016
This is version 106 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

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

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

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 one 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.