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Protein

Peptidase 1

Gene

DERP1

Organism
Dermatophagoides pteronyssinus (European house dust mite)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Thiol protease, with a preference for substrates with a large hydrophobic side chain in the P2 position, or with basic residues.

Catalytic activityi

Broad endopeptidase specificity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei132 – 1321By similarity
Active sitei268 – 2681By similarity
Active sitei288 – 2881By similarity

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Enzyme and pathway databases

BRENDAi3.4.22.65. 1873.

Protein family/group databases

MEROPSiC01.073.

Names & Taxonomyi

Protein namesi
Recommended name:
Peptidase 1 (EC:3.4.22.65)
Alternative name(s):
Allergen Der p I
Major mite fecal allergen Der p 1
Allergen: Der p 1
Gene namesi
Name:DERP1
OrganismiDermatophagoides pteronyssinus (European house dust mite)
Taxonomic identifieri6956 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaChelicerataArachnidaAcariAcariformesSarcoptiformesAstigmataPsoroptidiaAnalgoideaPyroglyphidaeDermatophagoidinaeDermatophagoides

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Allergenic propertiesi

Causes an allergic reaction in human. Common symptoms of mite allergy are bronchial asthma, allergic rhinitis and conjunctivitis. Binds to IgE in 80% of patients with house dust allergy.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi132 – 1321C → A: Loss of activity.
Mutagenesisi150 – 1501N → E: Loss of N-glycosylation.

Keywords - Diseasei

Allergen

Protein family/group databases

Allergomei1232. Der p 1.0111.
310. Der p 1.

Chemistry

ChEMBLiCHEMBL3351204.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 18181 PublicationAdd
BLAST
Propeptidei19 – 9880Activation peptide3 PublicationsPRO_0000026376Add
BLAST
Chaini99 – 320222Peptidase 1PRO_0000026377Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi102 ↔ 215
Disulfide bondi129 ↔ 169
Glycosylationi150 – 1501N-linked (GlcNAc...)1 Publication
Disulfide bondi163 ↔ 201

Post-translational modificationi

N-glycosylated. N-glycanase treatment does not completely remove carbohydrates, suggesting that the protein contains additional glycosylation sites.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Interactioni

Chemistry

BindingDBiP08176.

Structurei

Secondary structure

1
320
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi26 – 327Combined sources
Helixi40 – 6021Combined sources
Turni66 – 694Combined sources
Helixi72 – 798Combined sources
Helixi83 – 9311Combined sources
Turni114 – 1185Combined sources
Beta strandi128 – 1303Combined sources
Helixi132 – 14918Combined sources
Helixi157 – 1637Combined sources
Helixi174 – 18411Combined sources
Beta strandi186 – 1883Combined sources
Helixi189 – 1913Combined sources
Beta strandi212 – 2165Combined sources
Helixi222 – 23211Combined sources
Beta strandi236 – 2438Combined sources
Helixi245 – 2495Combined sources
Beta strandi253 – 2553Combined sources
Beta strandi266 – 27813Combined sources
Beta strandi281 – 2877Combined sources
Turni292 – 2954Combined sources
Beta strandi299 – 3035Combined sources
Helixi308 – 3103Combined sources
Turni311 – 3133Combined sources
Beta strandi316 – 3194Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1XKGX-ray1.61A19-320[»]
2AS8X-ray1.95A/B99-320[»]
3RVWX-ray1.95A99-320[»]
3RVXX-ray2.50A99-320[»]
4PP1X-ray3.00A/B99-320[»]
4PP2X-ray2.74E/F99-320[»]
ProteinModelPortaliP08176.
SMRiP08176. Positions 22-320.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08176.

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.
PfamiPF00112. 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.

P08176-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKIVLAIASL LALSAVYARP SSIKTFEEYK KAFNKSYATF EDEEAARKNF
60 70 80 90 100
LESVKYVQSN GGAINHLSDL SLDEFKNRFL MSAEAFEHLK TQFDLNAETN
110 120 130 140 150
ACSINGNAPA EIDLRQMRTV TPIRMQGGCG SCWAFSGVAA TESAYLAYRN
160 170 180 190 200
QSLDLAEQEL VDCASQHGCH GDTIPRGIEY IQHNGVVQES YYRYVAREQS
210 220 230 240 250
CRRPNAQRFG ISNYCQIYPP NVNKIREALA QTHSAIAVII GIKDLDAFRH
260 270 280 290 300
YDGRTIIQRD NGYQPNYHAV NIVGYSNAQG VDYWIVRNSW DTNWGDNGYG
310 320
YFAANIDLMM IEEYPYVVIL
Length:320
Mass (Da):36,104
Last modified:February 1, 1995 - v2
Checksum:iA0B1F4DD09791DFE
GO

Sequence cautioni

The sequence AAA28296 differs from that shown. Reason: Erroneous initiation. Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti148 – 1481Y → H.
Natural varianti179 – 1791E → K.
Natural varianti222 – 2221V → A.1 Publication
Natural varianti234 – 2341S → T.
Natural varianti313 – 3131E → Q.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U11695 mRNA. Translation: AAB60215.1.
M24794 mRNA. Translation: AAA28296.1. Different initiation.
X65197 Genomic DNA. Translation: CAA46317.1.
PIRiJQ0337.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U11695 mRNA. Translation: AAB60215.1.
M24794 mRNA. Translation: AAA28296.1. Different initiation.
X65197 Genomic DNA. Translation: CAA46317.1.
PIRiJQ0337.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1XKGX-ray1.61A19-320[»]
2AS8X-ray1.95A/B99-320[»]
3RVWX-ray1.95A99-320[»]
3RVXX-ray2.50A99-320[»]
4PP1X-ray3.00A/B99-320[»]
4PP2X-ray2.74E/F99-320[»]
ProteinModelPortaliP08176.
SMRiP08176. Positions 22-320.
ModBaseiSearch...
MobiDBiSearch...

Chemistry

BindingDBiP08176.
ChEMBLiCHEMBL3351204.

Protein family/group databases

Allergomei1232. Der p 1.0111.
310. Der p 1.
MEROPSiC01.073.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.4.22.65. 1873.

Miscellaneous databases

EvolutionaryTraceiP08176.

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.
PfamiPF00112. 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 nameiPEPT1_DERPT
AccessioniPrimary (citable) accession number: P08176
Secondary accession number(s): Q24616
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: February 1, 1995
Last modified: May 11, 2016
This is version 115 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

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

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.