CH901_DAVTA
ID CH901_DAVTA Reviewed; 518 AA.
AC B7ZK61;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 25-MAY-2022, entry version 57.
DE RecName: Full=Subtilisin-like serine protease Cla h 9.0101 {ECO:0000305};
DE EC=3.4.21.- {ECO:0000250|UniProtKB:Q9Y749};
DE AltName: Full=Vacuolar serine protease {ECO:0000303|PubMed:19162325, ECO:0000312|EMBL:AAX14379.1};
DE AltName: Allergen=Cla h 9.0101 {ECO:0000305};
DE Flags: Precursor;
OS Davidiella tassiana (Mycosphaerella tassiana) (Cladosporium herbarum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Cladosporiales; Cladosporiaceae; Cladosporium.
OX NCBI_TaxID=29918 {ECO:0000312|EMBL:AAX14379.1};
RN [1] {ECO:0000312|EMBL:AAX14379.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 142-148, 3D-STRUCTURE
RP MODELING OF 146-444, ALLERGEN, AND REGION.
RX PubMed=19162325; DOI=10.1016/j.molimm.2008.11.017;
RA Poll V., Denk U., Shen H.D., Panzani R.C., Dissertori O., Lackner P.,
RA Hemmer W., Mari A., Crameri R., Lottspeich F., Rid R., Richter K.,
RA Breitenbach M., Simon-Nobbe B.;
RT "The vacuolar serine protease, a cross-reactive allergen from Cladosporium
RT herbarum.";
RL Mol. Immunol. 46:1360-1373(2009).
CC -!- FUNCTION: Serine protease. {ECO:0000250|UniProtKB:Q9Y749}.
CC -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE in 15.5%
CC of 110 patients sensitized to C.herbarum.
CC {ECO:0000269|PubMed:19162325}.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000255,
CC ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Ser-139 or Glu-142 is the start of the
CC chain. {ECO:0000305|PubMed:19162325}.
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DR EMBL; AY787775; AAX14379.1; -; mRNA.
DR AlphaFoldDB; B7ZK61; -.
DR SMR; B7ZK61; -.
DR Allergome; 224; Cla h 9.
DR Allergome; 3208; Cla h 9.0101.
DR GO; GO:0019863; F:IgE binding; IDA:UniProtKB.
DR GO; GO:0004252; F:serine-type endopeptidase activity; ISS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; ISS:UniProtKB.
DR CDD; cd04077; Peptidases_S8_PCSK9_ProteinaseK_like; 1.
DR Gene3D; 3.30.70.80; -; 1.
DR Gene3D; 3.40.50.200; -; 1.
DR InterPro; IPR034193; PCSK9_ProteinaseK-like.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR010259; S8pro/Inhibitor_I9.
DR InterPro; IPR037045; S8pro/Inhibitor_I9_sf.
DR Pfam; PF05922; Inhibitor_I9; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; SSF52743; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 1: Evidence at protein level;
KW Allergen; Direct protein sequencing; Glycoprotein; Hydrolase;
KW IgE-binding protein; Protease; Serine protease; Signal; Zymogen.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT PROPEP 17..138
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:Q9HF04, ECO:0000255"
FT /id="PRO_0000446898"
FT CHAIN 139..459
FT /note="Subtilisin-like serine protease Cla h 9.0101"
FT /evidence="ECO:0000250|UniProtKB:Q9HF04, ECO:0000305"
FT /id="PRO_5002867142"
FT PROPEP 460..518
FT /note="Removed in mature form"
FT /evidence="ECO:0000305"
FT /id="PRO_0000446899"
FT DOMAIN 44..136
FT /note="Inhibitor I9"
FT /evidence="ECO:0000255"
FT DOMAIN 148..454
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT REGION 244..298
FT /note="IgE-binding"
FT /evidence="ECO:0000269|PubMed:19162325"
FT ACT_SITE 184
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 216
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 382
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT SITE 317
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:Q5JIZ5"
FT CARBOHYD 246
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 286
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 449
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 518 AA; 55242 MW; FD98E0FC244F52C9 CRC64;
MRGALAGLSL ATLATASPVL VNSIHNDAAP IISASNAKEI ADNYMIKFKD HVTQNLAAEH
HGWVQDLHEK TQVAKTELRK RSQSPMVDDI FNGLKHTYNI AGGLMGYAGH FDEDVIEQIR
RHPDVELVER DQEVHVLGSE SEVEKNAPWG LARISHRDSL SFGTFNKYLY TEDGGEGVDV
YVVDTGTNVD HVDFEGRASW GKTIPQGDAD EDGNGHGTHC SGTVAGKKYG VAKKAHVKAV
KVLRSNGSGS MSDVVKGVEY AAESHLEQVS ITKKGKRKGF KGSTANMSLG GGKSPILDKA
VNAAVDAGIH FAVAAGNDNA DSCNYSPAAA ENAVTVGAST LADERAYFSN YGKCNDIFAP
GLNIQSTWIG SKYAVNTISG TSMASPHVAG LLAYLLSLQP AKDSAFAVAD ISPKKLKANL
ISIATVGALT DVPSNTANIL AWNGGGESNY SAIVEKGGYK ATHRPTMLEE IESEAKVASK
KVYSEGDELA HKVAELTEKV EDLIAGELKD MFRELKRE
