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P10056

- PAPA3_CARPA

UniProt

P10056 - PAPA3_CARPA

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Protein

Caricain

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

Functioni

Catalytic activityi

Hydrolysis of proteins with broad specificity for peptide bonds, similar to those of papain and chymopapain.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei157 – 1571
Active sitei291 – 2911
Active sitei311 – 3111

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

BRENDAi3.4.22.30. 1191.

Protein family/group databases

MEROPSiC01.003.

Names & Taxonomyi

Protein namesi
Recommended name:
Caricain (EC:3.4.22.30)
Alternative name(s):
Papaya peptidase A
Papaya proteinase III
Short name:
PPIII
Papaya proteinase omega
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 – 1616Sequence AnalysisAdd
BLAST
Propeptidei17 – 132116Activation peptide1 PublicationPRO_0000026410Add
BLAST
Chaini133 – 348216CaricainPRO_0000026411Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Disulfide bond, Zymogen

Interactioni

Subunit structurei

Monomer.

Structurei

Secondary structure

1
348
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi40 – 5314
Turni54 – 563
Helixi62 – 8322
Beta strandi88 – 914
Turni95 – 984
Helixi101 – 1088
Beta strandi122 – 1243
Turni139 – 1435
Beta strandi153 – 1553
Helixi157 – 17418
Helixi182 – 1887
Beta strandi190 – 1923
Helixi194 – 1963
Helixi200 – 21011
Beta strandi212 – 2143
Turni215 – 2173
Helixi229 – 2313
Beta strandi241 – 2444
Beta strandi247 – 2493
Helixi250 – 25910
Beta strandi262 – 2665
Helixi271 – 2755
Beta strandi278 – 2814
Beta strandi291 – 30111
Beta strandi304 – 3107
Beta strandi315 – 3173
Beta strandi322 – 3265
Beta strandi330 – 3334
Helixi335 – 3373
Beta strandi343 – 3464

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1C7Xmodel-A133-348[»]
1EUXmodel-A133-348[»]
1F1Imodel-A133-348[»]
1MEGX-ray2.00A133-348[»]
1PCIX-ray3.20A/B/C27-348[»]
1PPOX-ray1.80A133-348[»]
ProteinModelPortaliP10056.
SMRiP10056. Positions 38-348.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP10056.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase C1 family.PROSITE-ProRule annotation

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.

P10056-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAMIPSISKL LFVAICLFVH MSVSFGDFSI VGYSQDDLTS TERLIQLFNS
60 70 80 90 100
WMLNHNKFYE NVDEKLYRFE IFKDNLNYID ETNKKNNSYW LGLNEFADLS
110 120 130 140 150
NDEFNEKYVG SLIDATIEQS YDEEFINEDT VNLPENVDWR KKGAVTPVRH
160 170 180 190 200
QGSCGSCWAF SAVATVEGIN KIRTGKLVEL SEQELVDCER RSHGCKGGYP
210 220 230 240 250
PYALEYVAKN GIHLRSKYPY KAKQGTCRAK QVGGPIVKTS GVGRVQPNNE
260 270 280 290 300
GNLLNAIAKQ PVSVVVESKG RPFQLYKGGI FEGPCGTKVD HAVTAVGYGK
310 320 330 340
SGGKGYILIK NSWGTAWGEK GYIRIKRAPG NSPGVCGLYK SSYYPTKN
Length:348
Mass (Da):38,788
Last modified:October 1, 1996 - v2
Checksum:i328F5C6BF45B4A07
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X66060 mRNA. Translation: CAA46862.1.
X51899 mRNA. Translation: CAA36180.1.
PIRiJN0633.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X66060 mRNA. Translation: CAA46862.1 .
X51899 mRNA. Translation: CAA36180.1 .
PIRi JN0633.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1C7X model - A 133-348 [» ]
1EUX model - A 133-348 [» ]
1F1I model - A 133-348 [» ]
1MEG X-ray 2.00 A 133-348 [» ]
1PCI X-ray 3.20 A/B/C 27-348 [» ]
1PPO X-ray 1.80 A 133-348 [» ]
ProteinModelPortali P10056.
SMRi P10056. Positions 38-348.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

Allergomei 1539. Car p Endoproteinase.
MEROPSi C01.003.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

BRENDAi 3.4.22.30. 1191.

Miscellaneous databases

EvolutionaryTracei P10056.

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. Baker K.C., Revell D.F., Cummings N.J., Collins M.E., Goodenough P.W.
    Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Leaf.
  2. "The thiol proteinases from the latex of Carica papaya L. II. The primary structure of proteinase omega."
    Dubois T., Kleinschmidt T., Schnek A.G., Looze Y., Braunitzer G.
    Biol. Chem. Hoppe-Seyler 369:741-754(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 133-348.
  3. Collins M.E., Revell D.F., Sumner I.G., Pickersgill R.W., Goodenough P.W.
    Submitted (FEB-1990) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 237-348.
    Tissue: Leaf.
  4. "Determination of the structure of papaya protease omega."
    Pickersgill R.W., Rizkallah P., Harris G.W., Goodenough P.W.
    Acta Crystallogr. B 47:766-771(1991)
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
  5. "Crystal structure of a caricain D158E mutant in complex with E-64."
    Katerelos N.A., Taylor M.A.J., Scott M., Goodenough P.W., Pickersgill R.W.
    FEBS Lett. 392:35-39(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF MUTANT GLU-290.
  6. "The prosequence of procaricain forms an alpha-helical domain that prevents access to the substrate-binding cleft."
    Groves M.R., Taylor M.A., Scott M., Cummings N.J., Pickersgill R.W., Jenkins J.A.
    Structure 4:1193-1203(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF PRO-CARICAIN.
  7. "Theoretical model structure of a caricain D158E mutant in complex with E-64C."
    Bhattacharya S., Pal A., Bera A., Chakraborty S., Banerjee A.
    Submitted (APR-2000) to the PDB data bank
    Cited for: 3D-STRUCTURE MODELING OF 133-348.

Entry informationi

Entry nameiPAPA3_CARPA
AccessioniPrimary (citable) accession number: P10056
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: October 1, 1996
Last modified: October 1, 2014
This is version 101 of the entry and version 2 of the sequence. [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

External Data

Dasty 3