ID   RM201_RHOMI             Reviewed;         342 AA.
AC   Q32ZM1;
DT   08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 58.
DE   RecName: Full=Subtilisin-like serine protease Rho m 2.0101 {ECO:0000305};
DE            EC=3.4.21.- {ECO:0000250|UniProtKB:Q9Y749};
DE   AltName: Full=Vacuolar serine protease {ECO:0000303|PubMed:16179794, ECO:0000312|EMBL:AAT37679.1};
DE   AltName: Allergen=Rho m 2.0101 {ECO:0000305};
DE   Flags: Precursor; Fragment;
OS   Rhodotorula mucilaginosa (Yeast) (Rhodotorula rubra).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX   NCBI_TaxID=5537 {ECO:0000312|EMBL:AAT37679.1};
RN   [1] {ECO:0000312|EMBL:AAT37679.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 31-39; 125-132; 136-147;
RP   165-175 AND 231-238, AND ALLERGEN.
RX   PubMed=16179794; DOI=10.1159/000088435;
RA   Chou H., Tam M.F., Lee S.S., Tai H.Y., Chang C.Y., Chou C.T., Shen H.D.;
RT   "A vacuolar serine protease (Rho m 2) is a major allergen of Rhodotorula
RT   mucilaginosa and belongs to a class of highly conserved pan-fungal
RT   allergens.";
RL   Int. Arch. Allergy Immunol. 138:134-141(2005).
CC   -!- FUNCTION: Serine protease. {ECO:0000250|UniProtKB:Q9Y749}.
CC   -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE in 57% of
CC       44 patients suffering from bronchial asthma.
CC       {ECO:0000269|PubMed:16179794}.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000255,
CC       ECO:0000255|RuleBase:RU003355, ECO:0000305}.
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DR   EMBL; AY547285; AAT37679.1; -; mRNA.
DR   AlphaFoldDB; Q32ZM1; -.
DR   SMR; Q32ZM1; -.
DR   Allergome; 2413; Rho m 2.
DR   Allergome; 3466; Rho m 2.0101.
DR   GO; GO:0110165; C:cellular anatomical entity; IEA:UniProt.
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; 3.40.50.200; -; 1.
DR   InterPro; IPR034193; PCSK9_ProteinaseK-like.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR   InterPro; IPR022398; Peptidase_S8_His-AS.
DR   InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR   InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF52743; SSF52743; 1.
DR   PROSITE; PS51892; SUBTILASE; 1.
DR   PROSITE; PS00136; SUBTILASE_ASP; 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; Protease;
KW   Serine protease; Zymogen.
FT   PROPEP          <1..30
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000305|PubMed:16179794"
FT                   /id="PRO_0000447002"
FT   CHAIN           31..342
FT                   /note="Subtilisin-like serine protease Rho m 2.0101"
FT                   /evidence="ECO:0000305|PubMed:16179794"
FT                   /id="PRO_0000447003"
FT   DOMAIN          <1..30
FT                   /note="Inhibitor I9"
FT                   /evidence="ECO:0000305"
FT   DOMAIN          39..342
FT                   /note="Peptidase S8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        75
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        107
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        267
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   CARBOHYD        137
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        171
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        335
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CONFLICT        137
FT                   /note="N -> S (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        141
FT                   /note="S -> T (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        146
FT                   /note="I -> L (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        146
FT                   /note="I -> V (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   NON_TER         1
FT                   /evidence="ECO:0000305, ECO:0000312|EMBL:AAT37679.1"
SQ   SEQUENCE   342 AA;  35848 MW;  716224F419A1CD81 CRC64;
     TMELLEDLIE QVRQLPMVNF IEKNSLVHAN EFTVAKGAPW GLARISHRDP LSLGSFDQYL
     YDSNGGTGVT SYVIDTGVNV HHEQFEGRAK WGKTIPQGDE DEDGNGHGTH CAGTIGSNAY
     GVAKNAEIVA VKVLRSNGSG SMSDVIKGVE FAVKSHQDSV KKGKNSFSTA NMSLGGGKSP
     ALDLAVNAAV KAGLHFAVAA GNENQDACNT SPASAENAIT VGASTISDAR AYFSNYGKCV
     DIFAPGLNIL STYIGSDAAT AYLSGTSMAS PHIAGLLTYY LSLQPSSDSE FFIGAEGITP
     AQLKKNLIAF GTPDVLADIP ADTPNILAFN GAGQNLTKFW GH