ID   DERF3_DERFA             Reviewed;         259 AA.
AC   P49275; Q23940; Q94508;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   27-MAR-2024, entry version 88.
DE   RecName: Full=Mite allergen Der f 3;
DE            EC=3.4.21.-;
DE   AltName: Full=Allergen Der f III;
DE   AltName: Allergen=Der f 3;
DE   Flags: Precursor;
GN   Name=DERF3;
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=8543021; DOI=10.1016/0014-5793(95)01291-5;
RA   Nishiyama C., Yasuhara T., Yuuki T., Okumura Y.;
RT   "Cloning and expression in Escherichia coli of cDNA encoding house dust
RT   mite allergen Der f 3, serine protease from Dermatophagoides farinae.";
RL   FEBS Lett. 377:62-66(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 28-259.
RX   PubMed=8563488; DOI=10.1159/000237212;
RA   Smith W.A., Thomas W.R.;
RT   "Comparative analysis of the genes encoding group 3 allergens from
RT   Dermatophagoides pteronyssinus and Dermatophagoides farinae.";
RL   Int. Arch. Allergy Immunol. 109:133-140(1996).
RN   [3]
RP   PROTEIN SEQUENCE OF 28-47.
RX   PubMed=2732406; DOI=10.1016/0091-6749(89)90447-8;
RA   Heymann P.W., Chapman M.D., Aalberse R.C., Fox J.W., Platts-Mills T.A.E.;
RT   "Antigenic and structural analysis of group II allergens (Der f II and Der
RT   p II) from house dust mites (Dermatophagoides spp).";
RL   J. Allergy Clin. Immunol. 83:1055-1067(1989).
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; D63858; BAA09920.1; -; mRNA.
DR   EMBL; U54781; AAA99805.1; -; Genomic_DNA.
DR   PIR; S68424; S68424.
DR   AlphaFoldDB; P49275; -.
DR   SMR; P49275; -.
DR   Allergome; 303; Der f 3.
DR   Allergome; 3304; Der f 3.0101.
DR   MEROPS; S01.234; -.
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; Trypsin-like serine proteases; 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   PANTHER; PTHR24264; TRYPSIN-RELATED; 1.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 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..16
FT                   /evidence="ECO:0000255"
FT   PROPEP          17..27
FT                   /evidence="ECO:0000269|PubMed:2732406"
FT                   /id="PRO_0000028143"
FT   CHAIN           28..259
FT                   /note="Mite allergen Der f 3"
FT                   /id="PRO_0000028144"
FT   DOMAIN          28..258
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        67
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        112
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        212
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   SITE            206
FT                   /note="Required for specificity"
FT   DISULFID        52..68
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        179..196
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        208..234
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   CONFLICT        35
FT                   /note="Q -> K (in Ref. 2; AAA99805)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        35
FT                   /note="Q -> L (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        42
FT                   /note="Q -> E (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        46..47
FT                   /note="QS -> EV (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        136
FT                   /note="A -> P (in Ref. 2; AAA99805)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        219
FT                   /note="V -> I (in Ref. 2; AAA99805)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   259 AA;  27674 MW;  043A62B26C4C57D7 CRC64;
     MMILTIVVLL AANILATPIL PSSPNATIVG GVKAQAGDCP YQISLQSSSH FCGGSILDEY
     WILTAAHCVN GQSAKKLSIR YNTLKHASGG EKIQVAEIYQ HENYDSMTID NDVALIKLKT
     PMTLDQTNAK PVPLPAQGSD VKVGDKIRVS GWGYLQEGSY SLPSELQRVD IDVVSREQCD
     QLYSKAGADV SENMICGGDV ANGGVDSCQG DSGGPVVDVA TKQIVGIVSW GYGCARKGYP
     GVYTRVGNFV DWIESKRSQ
//