Reviewed, UniProtKB/Swiss-Prot P08176 (PEPT1_DERPT)

Names and origin

Protein names

Recommended name:
    Peptidase 1
    EC=3.4.22.65
Alternative name(s):
    Major mite fecal allergen Der p 1
    Allergen Der p I
    Allergen=Der p 1

Gene names

Name:

DERP1

Organism

Dermatophagoides pteronyssinus (House-dust mite)

Taxonomic identifier

6956 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Chelicerata › Arachnida › Acari › Acariformes › Sarcoptiformes › Astigmata › Psoroptidia › Analgoidea › Pyroglyphidae › Dermatophagoidinae › Dermatophagoides

Protein attributes

Sequence length	320 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Thiol protease, with a preference for substrates with a large hydrophobic side chain in the P2 position, or with basic residues.
Catalytic activity	Broad endopeptidase specificity.
Subcellular location	Secreted.
Post-translational modification	N-glycosylated. N-glycanase treatment does not completely remove carbohydrates, suggesting that the protein contains additional glycosylation sites. Ref.9
Allergenic properties	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.
Sequence similarities	Belongs to the peptidase C1 family.

Ontologies

Keywords
Cellular component	Secreted
Coding sequence diversity	Polymorphism
Disease	Allergen
Domain	Signal
Molecular function	Hydrolase Protease Thiol protease
PTM	Disulfide bond Glycoprotein Zymogen
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	proteolysis Inferred from electronic annotation. Source: InterPro
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	cysteine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 18

18

Propeptide

19 – 98

80

Activation peptide Ref.6 Ref.7

PRO_0000026376

Chain

99 – 320

222

Peptidase 1

PRO_0000026377

Sites

Active site

132

1

By similarity

Active site

268

1

By similarity

Active site

288

1

By similarity

Amino acid modifications

Glycosylation

150

1

N-linked (GlcNAc...) Ref.9

Disulfide bond

102 ↔ 215

Disulfide bond

129 ↔ 169

Disulfide bond

163 ↔ 201

Natural variations

Natural variant

148

1

Y → H

Natural variant

179

1

E → K

Natural variant

222

1

V → A Ref.7

Natural variant

234

1

S → T

Natural variant

313

1

E → Q

Experimental info

Mutagenesis

132

1

C → A: Loss of activity.

Mutagenesis

150

1

N → E: Loss of N-glycosylation.

Secondary structure

1

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320

Helix Strand Turn

Details...

Helix

26 – 32

7

Helix

40 – 60

21

Turn

66 – 69

4

Helix

72 – 79

8

Helix

83 – 93

11

Turn

114 – 118

5

Beta strand

128 – 130

3

Helix

132 – 149

18

Helix

157 – 163

7

Helix

174 – 184

11

Beta strand

186 – 188

3

Helix

189 – 191

3

Beta strand

212 – 216

5

Helix

222 – 232

11

Beta strand

236 – 243

8

Helix

245 – 249

5

Beta strand

253 – 255

3

Beta strand

266 – 278

13

Beta strand

281 – 287

7

Beta strand

299 – 303

5

Helix

308 – 310

3

Turn

311 – 313

3

Beta strand

316 – 319

4

Sequences

	Sequence		Length	Mass (Da)
	P08176-1 [UniParc]. Last modified February 1, 1995. Version 2. Checksum: A0B1F4DD09791DFE	FASTA	320	36,104
	10 20 30 40 50 60 MKIVLAIASL LALSAVYARP SSIKTFEEYK KAFNKSYATF EDEEAARKNF LESVKYVQSN 70 80 90 100 110 120 GGAINHLSDL SLDEFKNRFL MSAEAFEHLK TQFDLNAETN ACSINGNAPA EIDLRQMRTV 130 140 150 160 170 180 TPIRMQGGCG SCWAFSGVAA TESAYLAYRN QSLDLAEQEL VDCASQHGCH GDTIPRGIEY 190 200 210 220 230 240 IQHNGVVQES YYRYVAREQS CRRPNAQRFG ISNYCQIYPP NVNKIREALA QTHSAIAVII 250 260 270 280 290 300 GIKDLDAFRH YDGRTIIQRD NGYQPNYHAV NIVGYSNAQG VDYWIVRNSW DTNWGDNGYG 310 320 YFAANIDLMM IEEYPYVVIL

References

[1]	"Sequence polymorphisms of cDNA clones encoding the mite allergen Der p I." Chua K.Y., Kehal P.K., Thomas W.R. Int. Arch. Allergy Immunol. 101:364-368(1993) [PubMed: 8353459] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], POLYMORPHISM.
[2]	"Sequence analysis of cDNA coding for a major house dust mite allergen, Der p 1. Homology with cysteine proteases." Chua K.Y., Stewart G.A., Thomas W.R., Simpson R.J., Dilworth R.J., Plozza T.M., Turner K.J. J. Exp. Med. 167:175-182(1988) [PubMed: 3335830] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 76-320.
[3]	"Cloning and expression of DNA coding for the major house dust mite allergen Der p 1 in Escherichia coli." Thomas W.R., Stewart G.A., Simpson R.J., Chua K.Y., Plozza T.M., Dilworth R.J., Nisbet A., Turner K.J. Int. Arch. Allergy Appl. Immunol. 85:127-129(1988) [PubMed: 3276629] [Abstract] Cited for: NUCLEOTIDE SEQUENCE OF 81-176.
[4]	"Sequence analysis of cDNA coding for a major house dust mite allergen, Der f I." Dilworth R.J., Chua K.Y., Thomas W.R. Clin. Exp. Allergy 21:25-32(1991) [PubMed: 2021874] [Abstract] Cited for: SEQUENCE REVISION TO 232-241.
[5]	"Molecular characterisation of group I allergen Eur m I from house dust mite Euroglyphus maynei." Kent N.A., Hill M.R., Keen J.N., Holland P.W., Hart B.J. Int. Arch. Allergy Immunol. 99:150-152(1992) [PubMed: 1483062] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 99-308.
[6]	"The binding of mouse hybridoma and human IgE antibodies to the major fecal allergen, Der p I, of Dermatophagoides pteronyssinus. Relative binding site location and species specificity studied by solid-phase inhibition assays with radiolabeled antigen." Lind P., Hansen O.C., Horn N. J. Immunol. 140:4256-4262(1988) [PubMed: 3372999] [Abstract] Cited for: PROTEIN SEQUENCE OF 99-127.
[7]	"Structural studies on the allergen Der p1 from the house dust mite Dermatophagoides pteronyssinus: similarity with cysteine proteinases." Simpson R.J., Nice E.C., Moritz R.L., Stewart G.A. Protein Seq. Data Anal. 2:17-21(1989) [PubMed: 2911558] [Abstract] Cited for: PROTEIN SEQUENCE OF 99-139; 177-192; 208-224 AND 260-277, VARIANT ALA-222.
[8]	"Comparative modelling of major house dust mite allergen Der p I: structure validation using an extended environmental amino acid propensity table." Topham C.M., Srinivasan N., Thorpe C.J., Overington J.P., Kalsheker N.A. Protein Eng. 7:869-894(1994) [PubMed: 7971950] [Abstract] Cited for: 3D-STRUCTURE MODELING.
[9]	"The crystal structure of recombinant proDer p 1, a major house dust mite proteolytic allergen." Meno K., Thorsted P.B., Ipsen H., Kristensen O., Larsen J.N., Spangfort M.D., Gajhede M., Lund K. J. Immunol. 175:3835-3845(2005) [PubMed: 16148130] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.61 ANGSTROMS) OF 22-320 OF MUTANT ALA-132/GLU-150, PROTEIN SEQUENCE OF N-TERMINUS, GLYCOSYLATION AT ASN-150.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

U11695 mRNA. Translation: AAB60215.1.
M24794 mRNA. Translation: AAA28296.1. Different initiation.
X65197 Genomic DNA. Translation: CAA46317.1.

PIR

JQ0337.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1XKG	X-ray	1.61	A	19-320	[»]
2AS8	X-ray	1.95	A/B	99-320	[»]

SMR

P08176. Positions 22-320.

ModBase

Search...

Protein family/group databases

MEROPS

C01.073.

Enzyme and pathway databases

BRENDA

3.4.22.65. 273873.

Family and domain databases

InterPro

IPR000169. Pept_cys_AS.
IPR013128. Peptidase_C1A.
IPR000668. Peptidase_C1A_C.
IPR013201. Prot_inhib_I29.
[Graphical view]

PANTHER

PTHR12411. Peptidase_C1A. 1 hit.

Pfam

PF08246. Inhibitor_I29. 1 hit.
PF00112. Peptidase_C1. 1 hit.
[Graphical view]

PRINTS

PR00705. PAPAIN.

ProDom

PD000158. Peptidase_C1. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00645. Pept_C1. 1 hit.
[Graphical view]

PROSITE

PS00640. THIOL_PROTEASE_ASN. 1 hit.
PS00139. THIOL_PROTEASE_CYS. 1 hit.
PS00639. THIOL_PROTEASE_HIS. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

PEPT1_DERPT

Accession

Primary (citable) accession number: P08176
Secondary accession number(s): Q24616

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	February 1, 1995
Last modified:	June 16, 2009
This is version 89 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)