Skip Header

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

P00784

- PAPA1_CARPA

UniProt

P00784 - PAPA1_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

Papain

Gene
N/A
Organism
Carica papaya (Papaya)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

Catalytic activityi

Hydrolysis of proteins with broad specificity for peptide bonds, but preference for an amino acid bearing a large hydrophobic side chain at the P2 position. Does not accept Val in P1'.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei158 – 15811 Publication
Active sitei292 – 2921
Active sitei308 – 30811 Publication

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

BRENDAi3.4.22.2. 1191.
SABIO-RKP00784.

Protein family/group databases

MEROPSiC01.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Papain (EC:3.4.22.2)
Alternative name(s):
Papaya proteinase I
Short name:
PPI
Allergen: Car p 1
OrganismiCarica papaya (Papaya)
Taxonomic identifieri3649 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesCaricaceaeCarica

Pathology & Biotechi

Allergenic propertiesi

Causes an allergic reaction in human.

Keywords - Diseasei

Allergen

Protein family/group databases

Allergomei709. Car p 1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Sequence AnalysisAdd
BLAST
Propeptidei19 – 133115Activation peptide1 PublicationPRO_0000026406Add
BLAST
Chaini134 – 345212PapainPRO_0000026407Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi155 ↔ 1961 Publication
Disulfide bondi189 ↔ 2281 Publication
Disulfide bondi286 ↔ 3331 Publication

Keywords - PTMi

Disulfide bond, Zymogen

Interactioni

Protein-protein interaction databases

MINTiMINT-1504623.

Structurei

Secondary structure

1
345
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi41 – 5414Combined sources
Helixi62 – 8221Combined sources
Beta strandi88 – 914Combined sources
Turni95 – 984Combined sources
Helixi101 – 1088Combined sources
Beta strandi119 – 1246Combined sources
Turni140 – 1445Combined sources
Beta strandi154 – 1563Combined sources
Helixi158 – 17518Combined sources
Helixi183 – 1897Combined sources
Beta strandi191 – 1933Combined sources
Helixi195 – 1973Combined sources
Helixi201 – 21010Combined sources
Turni216 – 2183Combined sources
Beta strandi223 – 2253Combined sources
Turni230 – 2334Combined sources
Beta strandi241 – 2455Combined sources
Helixi251 – 26010Combined sources
Beta strandi263 – 2675Combined sources
Helixi272 – 2754Combined sources
Beta strandi279 – 2824Combined sources
Beta strandi292 – 3009Combined sources
Beta strandi303 – 3075Combined sources
Beta strandi312 – 3143Combined sources
Turni315 – 3173Combined sources
Beta strandi319 – 3235Combined sources
Beta strandi325 – 3273Combined sources
Helixi332 – 3343Combined sources
Beta strandi340 – 3434Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BP4X-ray2.20A134-345[»]
1BQIX-ray2.50A134-345[»]
1CVZX-ray1.70A134-345[»]
1EFFmodel-A134-345[»]
1KHPX-ray2.00A134-345[»]
1KHQX-ray1.60A134-345[»]
1PADX-ray2.80A134-345[»]
1PE6X-ray2.10A134-345[»]
1PIPX-ray1.70A134-345[»]
1POPX-ray2.10A134-345[»]
1PPDX-ray2.00A134-345[»]
1PPNX-ray1.60A134-345[»]
1PPPX-ray1.90A134-345[»]
1STFX-ray2.37E134-345[»]
2CIOX-ray1.50A134-345[»]
2PADX-ray2.80A134-345[»]
3E1ZX-ray1.86B134-345[»]
3IMAX-ray2.03A/C134-345[»]
3LFYX-ray2.60A/C134-345[»]
3TNXX-ray2.62A/C27-345[»]
3USVX-ray3.80A/C27-345[»]
4KP9X-ray2.10A/B134-345[»]
4PADX-ray2.80A134-345[»]
5PADX-ray2.80A134-345[»]
6PADX-ray2.80A134-345[»]
9PAPX-ray1.65A134-345[»]
ProteinModelPortaliP00784.
SMRiP00784. Positions 38-345.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00784.

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.

P00784-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAMIPSISKL LFVAICLFVY MGLSFGDFSI VGYSQNDLTS TERLIQLFES
60 70 80 90 100
WMLKHNKIYK NIDEKIYRFE IFKDNLKYID ETNKKNNSYW LGLNVFADMS
110 120 130 140 150
NDEFKEKYTG SIAGNYTTTE LSYEEVLNDG DVNIPEYVDW RQKGAVTPVK
160 170 180 190 200
NQGSCGSCWA FSAVVTIEGI IKIRTGNLNE YSEQELLDCD RRSYGCNGGY
210 220 230 240 250
PWSALQLVAQ YGIHYRNTYP YEGVQRYCRS REKGPYAAKT DGVRQVQPYN
260 270 280 290 300
EGALLYSIAN QPVSVVLEAA GKDFQLYRGG IFVGPCGNKV DHAVAAVGYG
310 320 330 340
PNYILIKNSW GTGWGENGYI RIKRGTGNSY GVCGLYTSSF YPVKN
Length:345
Mass (Da):38,922
Last modified:January 1, 1988 - v1
Checksum:i82D9FB35EDCA12EF
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti180 – 1801E → Q AA sequence (PubMed:5470818)Curated
Sequence conflicti219 – 2202YP → PY AA sequence (PubMed:5470818)Curated
Sequence conflicti251 – 2511E → Q AA sequence (PubMed:5470818)Curated
Sequence conflicti268 – 2681E → Q AA sequence (PubMed:5470818)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M15203 mRNA. Translation: AAB02650.1.
PIRiA26466. PPPA.

Cross-referencesi

Web resourcesi

Worthington enzyme manual

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M15203 mRNA. Translation: AAB02650.1 .
PIRi A26466. PPPA.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1BP4 X-ray 2.20 A 134-345 [» ]
1BQI X-ray 2.50 A 134-345 [» ]
1CVZ X-ray 1.70 A 134-345 [» ]
1EFF model - A 134-345 [» ]
1KHP X-ray 2.00 A 134-345 [» ]
1KHQ X-ray 1.60 A 134-345 [» ]
1PAD X-ray 2.80 A 134-345 [» ]
1PE6 X-ray 2.10 A 134-345 [» ]
1PIP X-ray 1.70 A 134-345 [» ]
1POP X-ray 2.10 A 134-345 [» ]
1PPD X-ray 2.00 A 134-345 [» ]
1PPN X-ray 1.60 A 134-345 [» ]
1PPP X-ray 1.90 A 134-345 [» ]
1STF X-ray 2.37 E 134-345 [» ]
2CIO X-ray 1.50 A 134-345 [» ]
2PAD X-ray 2.80 A 134-345 [» ]
3E1Z X-ray 1.86 B 134-345 [» ]
3IMA X-ray 2.03 A/C 134-345 [» ]
3LFY X-ray 2.60 A/C 134-345 [» ]
3TNX X-ray 2.62 A/C 27-345 [» ]
3USV X-ray 3.80 A/C 27-345 [» ]
4KP9 X-ray 2.10 A/B 134-345 [» ]
4PAD X-ray 2.80 A 134-345 [» ]
5PAD X-ray 2.80 A 134-345 [» ]
6PAD X-ray 2.80 A 134-345 [» ]
9PAP X-ray 1.65 A 134-345 [» ]
ProteinModelPortali P00784.
SMRi P00784. Positions 38-345.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

MINTi MINT-1504623.

Chemistry

BindingDBi P00784.
ChEMBLi CHEMBL4779.

Protein family/group databases

Allergomei 709. Car p 1.
MEROPSi C01.001.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

BRENDAi 3.4.22.2. 1191.
SABIO-RK P00784.

Miscellaneous databases

EvolutionaryTracei P00784.

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. "Cloning and sequencing of papain-encoding cDNA."
    Cohen L.W., Coghlan V.M., Dihel L.C.
    Gene 48:219-227(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The complete amino acid sequence of papain. Additions and corrections."
    Mitchel R.E.J., Chaiken I.M., Smith E.L.
    J. Biol. Chem. 245:3485-3492(1970) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 134-345.
  3. "A reinvestigation of residues 64-68 and 175 in papain. Evidence that residues 64 and 175 are asparagine."
    Husain S.S., Lowe G.
    Biochem. J. 116:689-692(1970) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION TO 197.
  4. Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
  5. "Structure of papain refined at 1.65-A resolution."
    Kamphuis I.G., Kalk K.H., Swarte M.B.A., Drenth J.
    J. Mol. Biol. 179:233-256(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS).
  6. "The refined 2.4 A X-ray crystal structure of recombinant human stefin B in complex with the cysteine proteinase papain: a novel type of proteinase inhibitor interaction."
    Stubbs M.T., Laber B., Bode W., Huber R., Jerala R., Lenarcic B., Turk V.
    EMBO J. 9:1939-1947(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
  7. "Crystal structure of papain-succinyl-Gln-Val-Val-Ala-Ala-p-nitroanilide complex at 1.7-A resolution: noncovalent binding mode of a common sequence of endogenous thiol protease inhibitors."
    Yamamoto A., Tomoo K., Doi M., Ohishi H., Inoue M., Ishida T., Yamamoto D., Tsuboi S., Okamoto H., Okada Y.
    Biochemistry 31:11305-11309(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
  8. "Structure of monoclinic papain at 1.60-A resolution."
    Pickersgill R.W., Harris G.W., Garman E.
    Acta Crystallogr. B 48:59-67(1992)
    Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).

Entry informationi

Entry nameiPAPA1_CARPA
AccessioniPrimary (citable) accession number: P00784
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 1, 1988
Last modified: November 26, 2014
This is version 112 of the entry and version 1 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. Allergens
    Nomenclature of allergens and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Peptidase families
    Classification of peptidase families and list of entries
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3