DERF6_DERFA
ID DERF6_DERFA Reviewed; 279 AA.
AC P49276; Q9NJS0;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2001, sequence version 2.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Mite allergen Der f 6;
DE EC=3.4.21.-;
DE AltName: Full=Allergen Der f VI;
DE AltName: Full=DF5;
DE AltName: Allergen=Der f 6;
DE Flags: Precursor;
GN Name=DERF6;
OS Dermatophagoides farinae (American house dust mite).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Acariformes; Sarcoptiformes; Astigmata; Psoroptidia; Analgoidea;
OC Pyroglyphidae; Dermatophagoidinae; Dermatophagoides.
OX NCBI_TaxID=6954;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10381565;
RA Kawamoto S., Mizuguchi Y., Morimoto K., Aki T., Shigeta S., Yasueda H.,
RA Wada T., Suzuki O., Jyo T., Ono K.;
RT "Cloning and expression of Der f 6, a serine protease allergen from the
RT house dust mite, Dermatophagoides farinae.";
RL Biochim. Biophys. Acta 1454:201-207(1999).
RN [2]
RP PROTEIN SEQUENCE OF 50-69.
RX PubMed=8334537; DOI=10.1111/j.1365-2222.1993.tb00343.x;
RA Yasueda H., Mita H., Akiyama K., Shida T., Ando T., Sugiyama S.,
RA Yamakawa H.;
RT "Allergens from Dermatophagoides mites with chymotryptic activity.";
RL Clin. Exp. Allergy 23:384-390(1993).
CC -!- FUNCTION: Protease that shows specificity similar to chymotrypsin.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- ALLERGEN: Causes an allergic reaction in human. Common symptoms of mite
CC allergy are bronchial asthma, allergic rhinitis and conjunctivitis.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
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DR EMBL; AF125187; AAF28423.1; -; mRNA.
DR AlphaFoldDB; P49276; -.
DR SMR; P49276; -.
DR Allergome; 306; Der f 6.
DR Allergome; 3255; Der f 6.0101.
DR MEROPS; S01.245; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 1.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 1: Evidence at protein level;
KW Allergen; Direct protein sequencing; Disulfide bond; Hydrolase; Protease;
KW Secreted; Serine protease; Signal; Zymogen.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..49
FT /evidence="ECO:0000269|PubMed:8334537"
FT /id="PRO_0000028147"
FT CHAIN 50..279
FT /note="Mite allergen Der f 6"
FT /id="PRO_0000028148"
FT DOMAIN 50..279
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 94
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 140
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 233
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT DISULFID 79..95
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 204..220
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 229..255
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT CONFLICT 50
FT /note="V -> A (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 279 AA; 30535 MW; 5B29B6C46F185E56 CRC64;
MIKIFLVTIL IVITVTVDAR FPRSLQPKWA YLDSNEFPRS KIGDSPIAGV VGGQDADLAE
APFQISLLKD YLIMKRHMCG GSLISESTVV TAAHCTYGQK ASSLSVRYGT NQRTSSSYGD
LKVKPIIQHE SYEQDQTQTD KTIIILPNPV VPSTNVQMNE IETEDIVDGD KVTIYGWGLT
DGNGKDLPDK LQKGSMTIVG NDRCNEKWGS INAIHPGMIC ALDKTQSGCN GDSGGPLVSA
NRKLTGIVSW GPSKCPPGEY MSVFTRPKYY LDWITKNIV