ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry P08176


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name PEPT1_DERPT
Primary accession number P08176
Secondary accession number Q24616
Integrated into Swiss-Prot on August 1, 1988
Sequence was last modified on February 1, 1995 (Sequence version 2)
Annotations were last modified on    November 4, 2008 (Entry version 84)
Name and origin of the protein
Protein name Peptidase 1 [Precursor]
Synonyms EC 3.4.22.65
Major mite fecal allergen Der p 1
Allergen Der p I
Allergen Der p 1
Gene name
Name: DERP1
From
Dermatophagoides pteronyssinus (House-dust mite) [TaxID: 6956] 
Taxonomy Eukaryota; Metazoa; Arthropoda; Chelicerata; Arachnida; Acari; Acariformes; Sarcoptiformes; Astigmata; Psoroptidia; Analgoidea; Pyroglyphidae; Dermatophagoidinae; Dermatophagoides.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND POLYMORPHISM.
PubMed=8353459 [NCBI, ExPASy, EBI, Israel, Japan]
Chua K.Y., Kehal P.K., Thomas W.R.;
"Sequence polymorphisms of cDNA clones encoding the mite allergen Der p I.";
Int. Arch. Allergy Immunol. 101:364-368(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 76-320.
DOI=10.1084/jem.167.1.175; PubMed=3335830 [NCBI, ExPASy, EBI, Israel, Japan]
Chua K.Y., Stewart G.A., Thomas W.R., Simpson R.J., Dilworth R.J., Plozza T.M., Turner K.J.;
"Sequence analysis of cDNA coding for a major house dust mite allergen, Der p 1. Homology with cysteine proteases.";
J. Exp. Med. 167:175-182(1988).
[3]
NUCLEOTIDE SEQUENCE OF 81-176.
PubMed=3276629 [NCBI, ExPASy, EBI, Israel, Japan]
Thomas W.R., Stewart G.A., Simpson R.J., Chua K.Y., Plozza T.M., Dilworth R.J., Nisbet A., Turner K.J.;
"Cloning and expression of DNA coding for the major house dust mite allergen Der p 1 in Escherichia coli.";
Int. Arch. Allergy Appl. Immunol. 85:127-129(1988).
[4]
SEQUENCE REVISION TO 232-241.
PubMed=2021874 [NCBI, ExPASy, EBI, Israel, Japan]
Dilworth R.J., Chua K.Y., Thomas W.R.;
"Sequence analysis of cDNA coding for a major house dust mite allergen, Der f I.";
Clin. Exp. Allergy 21:25-32(1991).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 99-308.
PubMed=1483062 [NCBI, ExPASy, EBI, Israel, Japan]
Kent N.A., Hill M.R., Keen J.N., Holland P.W., Hart B.J.;
"Molecular characterisation of group I allergen Eur m I from house dust mite Euroglyphus maynei.";
Int. Arch. Allergy Immunol. 99:150-152(1992).
[6]
PROTEIN SEQUENCE OF 99-127.
PubMed=3372999 [NCBI, ExPASy, EBI, Israel, Japan]
Lind P., Hansen O.C., Horn N.;
"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.";
J. Immunol. 140:4256-4262(1988).
[7]
PROTEIN SEQUENCE OF 99-139; 177-192; 208-224 AND 260-277, AND VARIANT ALA-222.
PubMed=2911558 [NCBI, ExPASy, EBI, Israel, Japan]
Simpson R.J., Nice E.C., Moritz R.L., Stewart G.A.;
"Structural studies on the allergen Der p1 from the house dust mite Dermatophagoides pteronyssinus: similarity with cysteine proteinases.";
Protein Seq. Data Anal. 2:17-21(1989).
[8]
3D-STRUCTURE MODELING.
DOI=10.1093/protein/7.7.869; PubMed=7971950 [NCBI, ExPASy, EBI, Israel, Japan]
Topham C.M., Srinivasan N., Thorpe C.J., Overington J.P., Kalsheker N.A.;
"Comparative modelling of major house dust mite allergen Der p I: structure validation using an extended environmental amino acid propensity table.";
Protein Eng. 7:869-894(1994).
[9]
X-RAY CRYSTALLOGRAPHY (1.61 ANGSTROMS) OF 22-320 OF MUTANT ALA-132/GLU-150, PROTEIN SEQUENCE OF N-TERMINUS, AND GLYCOSYLATION AT ASN-150.
PubMed=16148130 [NCBI, ExPASy, EBI, Israel, Japan]
Meno K., Thorsted P.B., Ipsen H., Kristensen O., Larsen J.N., Spangfort M.D., Gajhede M., Lund K.;
"The crystal structure of recombinant proDer p 1, a major house dust mite proteolytic allergen.";
J. Immunol. 175:3835-3845(2005).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
U11695; AAB60215.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M24794; AAA28296.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X65197; CAA46317.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR JQ0337; JQ0337.
3D structure databases
PDB
1XKG; X-ray; 1.61 A; A=19-320.[ExPASy / RCSB / EBI]
2AS8; X-ray; 1.95 A; A/B=99-320.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1XKG; -.
2AS8; -.
SMR P08176; 22-320.
ModBase P08176.
Protein family/group databases
MEROPS C01.073; -.
Ontologies
GO
GO:0005576; Cellular component: extracellular region (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR000169; Pept_cys_AS.
IPR013128; Peptidase_C1A.
IPR000668; Peptidase_C1A_C.
IPR013201; Prot_inhib_I29.
Graphical view of domain structure.
PANTHER PTHR12411; Peptidase_C1A; 1.
Pfam PF08246; Inhibitor_I29; 1.
PF00112; Peptidase_C1; 1.
Pfam graphical view of domain structure.
PRINTS PR00705; PAPAIN.
ProDom PD000158; Peptidase_C1; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00645; Pept_C1; 1.
SMART graphical view of domain structure.
PROSITE PS00640; THIOL_PROTEASE_ASN; 1.
PS00139; THIOL_PROTEASE_CYS; 1.
PS00639; THIOL_PROTEASE_HIS; 1.
BLOCKS P08176.
ProtoNet P08176.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Allergen; Direct protein sequencing; Glycoprotein; Hydrolase; Polymorphism; Protease; Secreted; Signal; Thiol protease; Zymogen.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    18  18      
PROPEP   19    98  80     Activation peptide. PRO_0000026376
CHAIN   99   320  222     Peptidase 1. PRO_0000026377
ACT_SITE   132   132        By similarity. 
ACT_SITE   268   268        By similarity. 
ACT_SITE   288   288        By similarity. 
CARBOHYD   150   150        N-linked (GlcNAc...). 
DISULFID   102   215         
DISULFID   129   169         
DISULFID   163   201         
VARIANT   148   148  1     Y -> H. 
VARIANT   179   179  1     E -> K. 
VARIANT   222   222  1     V -> A. 
VARIANT   234   234  1     S -> T. 
VARIANT   313   313  1     E -> Q. 
MUTAGEN   132   132        C->A: Loss of activity. 
MUTAGEN   150   150        N->E: Loss of N-glycosylation. 
HELIX   26    32  7      
HELIX   40    60  21      
TURN   66    69  4      
HELIX   72    79  8      
HELIX   83    93  11      
TURN   114   118  5      
STRAND   128   130  3      
HELIX   132   149  18      
HELIX   157   163  7      
HELIX   174   184  11      
STRAND   186   188  3      
HELIX   189   191  3      
STRAND   212   216  5      
HELIX   222   232  11      
STRAND   236   243  8      
HELIX   245   249  5      
STRAND   253   255  3      
STRAND   266   278  13      
STRAND   281   287  7      
STRAND   299   303  5      
HELIX   308   310  3      
TURN   311   313  3      
STRAND   316   319  4      
Sequence information
Length: 320 AA [This is the length of the unprocessed precursor] Molecular weight: 36104 Da [This is the MW of the unprocessed precursor] CRC64: A0B1F4DD09791DFE [This is a checksum on the sequence]
        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 

P08176 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ch flag SIB Switzerland Mirror sites: Australia  Brazil  Canada  China  Korea
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!