SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P05994

- PAPA4_CARPA

UniProt

P05994 - PAPA4_CARPA

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Papaya proteinase 4
Gene
N/A
Organism
Carica papaya (Papaya)
Status
Reviewed - 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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei157 – 1571 By similarity
Active sitei291 – 2911 By similarity
Active sitei311 – 3111 By similarity

GO - Molecular functioni

  1. cysteine-type peptidase activity Source: UniProtKB-KW
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

MEROPSiC01.004.

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)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818 Reviewed prediction
Add
BLAST
Propeptidei19 – 132114Activation peptide
PRO_0000026412Add
BLAST
Chaini133 – 348216Papaya proteinase 4
PRO_0000026413Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi154 ↔ 195
Disulfide bondi188 ↔ 227
Disulfide bondi285 ↔ 336

Keywords - PTMi

Disulfide bond, Zymogen

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni139 – 1435
Beta strandi153 – 1553
Helixi157 – 17418
Helixi182 – 1887
Beta strandi190 – 1923
Helixi200 – 21011
Turni215 – 2173
Helixi229 – 2324
Beta strandi241 – 2444
Helixi250 – 2578
Beta strandi262 – 2665
Helixi271 – 2744
Beta strandi278 – 2814
Beta strandi291 – 30111
Beta strandi304 – 3107
Beta strandi322 – 3265
Helixi335 – 3373
Beta strandi343 – 3464

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GECX-ray2.10E133-348[»]
ProteinModelPortaliP05994.
SMRiP05994. Positions 38-348.

Miscellaneous databases

EvolutionaryTraceiP05994.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase C1 family.

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.

P05994-1 [UniParc]FASTAAdd to Basket

« Hide

MAIICSFSKL LFVAICLFGH MSLSYCDFSI VGYSQDDLTS TERLIQLFNS    50
WMLKHNKNYK NVDEKLYRFE IFKDNLKYID ERNKMINGYW LGLNEFSDLS 100
NDEFKEKYVG SLPEDYTNQP YDEEFVNEDI VDLPESVDWR AKGAVTPVKH 150
QGYCESCWAF STVATVEGIN KIKTGNLVEL SEQELVDCDK QSYGCNRGYQ 200
STSLQYVAQN GIHLRAKYPY IAKQQTCRAN QVGGPKVKTN GVGRVQSNNE 250
GSLLNAIAHQ PVSVVVESAG RDFQNYKGGI FEGSCGTKVD HAVTAVGYGK 300
SGGKGYILIK NSWGPGWGEN GYIRIRRASG NSPGVCGVYR SSYYPIKN 348
Length:348
Mass (Da):39,024
Last modified:October 1, 1996 - v3
Checksum:i40855EDD37F68A8E
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti190 – 1901K → L AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X78056 mRNA. Translation: CAA54974.1.
X03970 mRNA. Translation: CAA27608.1.
PIRiS06837.
T09798.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X78056 mRNA. Translation: CAA54974.1 .
X03970 mRNA. Translation: CAA27608.1 .
PIRi S06837.
T09798.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1GEC X-ray 2.10 E 133-348 [» ]
ProteinModelPortali P05994.
SMRi P05994. Positions 38-348.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

Allergomei 1539. Car p Endoproteinase.
MEROPSi C01.004.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

BRENDAi 3.4.22.25. 1191.
SABIO-RK P05994.

Miscellaneous databases

EvolutionaryTracei P05994.

Family and domain databases

InterProi IPR025661. Pept_asp_AS.
IPR000169. Pept_cys_AS.
IPR025660. Pept_his_AS.
IPR013128. Peptidase_C1A.
IPR000668. Peptidase_C1A_C.
IPR013201. Prot_inhib_I29.
[Graphical view ]
PANTHERi PTHR12411. PTHR12411. 1 hit.
Pfami PF08246. Inhibitor_I29. 1 hit.
PF00112. Peptidase_C1. 1 hit.
[Graphical view ]
PRINTSi PR00705. PAPAIN.
SMARTi SM00848. Inhibitor_I29. 1 hit.
SM00645. Pept_C1. 1 hit.
[Graphical view ]
PROSITEi PS00640. THIOL_PROTEASE_ASN. 1 hit.
PS00139. THIOL_PROTEASE_CYS. 1 hit.
PS00639. THIOL_PROTEASE_HIS. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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. 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).

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: May 14, 2014
This is version 98 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

External Data

Dasty 3

Similar proteinsi