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Protein

Papaya proteinase 4

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

Functioni

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

Miscellaneous

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

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

Keywordsi

Molecular functionHydrolase, Protease, Thiol protease

Enzyme and pathway databases

BRENDAi3.4.22.25 1191
SABIO-RKiP05994

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 Cari 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

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

InterProiView protein in InterPro
IPR025661 Pept_asp_AS
IPR000169 Pept_cys_AS
IPR025660 Pept_his_AS
IPR013128 Peptidase_C1A
IPR000668 Peptidase_C1A_C
IPR013201 Prot_inhib_I29
PANTHERiPTHR12411 PTHR12411, 1 hit
PfamiView protein in Pfam
PF08246 Inhibitor_I29, 1 hit
PF00112 Peptidase_C1, 1 hit
PRINTSiPR00705 PAPAIN
SMARTiView protein in SMART
SM00848 Inhibitor_I29, 1 hit
SM00645 Pept_C1, 1 hit
PROSITEiView protein in PROSITE
PS00640 THIOL_PROTEASE_ASN, 1 hit
PS00139 THIOL_PROTEASE_CYS, 1 hit
PS00639 THIOL_PROTEASE_HIS, 1 hit

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
UniGeneiCpp.1572

Genome annotation databases

KEGGiag:CAA54974

Similar proteinsi

Entry informationi

Entry nameiPAPA4_CARPA
AccessioniPrimary (citable) accession number: P05994
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: October 1, 1996
Last modified: May 23, 2018
This is version 109 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

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

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