RNMG_ASPFU
ID RNMG_ASPFU Reviewed; 176 AA.
AC P67875; P04389; P19792; Q4WEA6;
DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 25-MAY-2022, entry version 98.
DE RecName: Full=Ribonuclease mitogillin;
DE EC=3.1.27.-;
DE AltName: Full=Allergen Asp f I;
DE AltName: Full=Allergen I/a;
DE AltName: Full=IgE-binding ribotoxin;
DE AltName: Full=Major allergen Asp f 1;
DE AltName: Allergen=Asp f 1;
DE Flags: Precursor;
GN Name=mitF; Synonyms=aspF1; ORFNames=AFUA_5G02330;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=CBS 143.89;
RX PubMed=1943712; DOI=10.1111/j.1365-2958.1991.tb01930.x;
RA Lamy B., Moutaouakil M., Latge J.P., Davies J.;
RT "Secretion of a potential virulence factor, a fungal ribonucleotoxin,
RT during human aspergillosis infections.";
RL Mol. Microbiol. 5:1811-1815(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1431110;
RA Arruda L.K., Mann B.J., Chapman M.D.;
RT "Selective expression of a major allergen and cytotoxin, Asp f I, in
RT Aspergillus fumigatus. Implications for the immunopathogenesis of
RT Aspergillus-related diseases.";
RL J. Immunol. 149:3354-3359(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 28-176.
RX PubMed=1624793;
RA Moser M., Crameri R., Menz G., Schneider T., Dudler T., Virchow C.,
RA Gmachl M., Blaser K., Suter M.;
RT "Cloning and expression of recombinant Aspergillus fumigatus allergen I/a
RT (rAsp f I/a) with IgE binding and type I skin test activity.";
RL J. Immunol. 149:454-460(1992).
RN [5]
RP PRELIMINARY PROTEIN SEQUENCE OF 28-176.
RC STRAIN=5167;
RX PubMed=2230656; DOI=10.1084/jem.172.5.1529;
RA Arruda L.K., Platts-Mills T.A.E., Fox J.W., Chapman M.D.;
RT "Aspergillus fumigatus allergen I, a major IgE-binding protein, is a member
RT of the mitogillin family of cytotoxins.";
RL J. Exp. Med. 172:1529-1532(1990).
RN [6]
RP PROTEIN SEQUENCE OF 28-48.
RC STRAIN=AF-285 / Indian isolate;
RA Sarma P.U., Bir N., Fairwell T.;
RL Submitted (AUG-1999) to UniProtKB.
CC -!- FUNCTION: This purine-specific ribonuclease cleaves 28S RNA in
CC eukaryotic ribosomes, inhibits protein synthesis, and shows antitumor
CC activity.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE. May
CC promote colonization through cytotoxic activity and by causing
CC inflammatory reactions involving IgE antibodies. Binds also to IgG.
CC -!- SIMILARITY: Belongs to the ribonuclease U2 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X58278; CAA41217.1; -; Genomic_DNA.
DR EMBL; M83781; AAB07779.1; -; Genomic_DNA.
DR EMBL; AAHF01000011; EAL86071.1; -; Genomic_DNA.
DR EMBL; S39330; AAB22442.1; -; mRNA.
DR PIR; A46497; A46497.
DR RefSeq; XP_748109.1; XM_743016.1.
DR AlphaFoldDB; P67875; -.
DR SMR; P67875; -.
DR STRING; 746128.CADAFUBP00004977; -.
DR Allergome; 3107; Asp f 1.0101.
DR Allergome; 62; Asp f 1.
DR ABCD; P67875; 2 sequenced antibodies.
DR EnsemblFungi; EAL86071; EAL86071; AFUA_5G02330.
DR GeneID; 3505541; -.
DR KEGG; afm:AFUA_5G02330; -.
DR VEuPathDB; FungiDB:Afu5g02330; -.
DR eggNOG; ENOG502SV0S; Eukaryota.
DR HOGENOM; CLU_1768332_0_0_1; -.
DR InParanoid; P67875; -.
DR OMA; SSYPHWF; -.
DR OrthoDB; 1464399at2759; -.
DR Proteomes; UP000002530; Chromosome 5.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004521; F:endoribonuclease activity; IEA:InterPro.
DR GO; GO:0019863; F:IgE binding; IDA:AspGD.
DR GO; GO:0004540; F:ribonuclease activity; IDA:AspGD.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0017148; P:negative regulation of translation; IEA:UniProtKB-KW.
DR GO; GO:0060300; P:regulation of cytokine activity; IMP:AspGD.
DR InterPro; IPR004025; Fun_ribotoxin.
DR InterPro; IPR000026; Gua-sp_ribonuclease_N1/T1/U2.
DR InterPro; IPR016191; Ribonuclease/ribotoxin.
DR PIRSF; PIRSF037430; RNase_U2; 1.
DR PRINTS; PR01704; FUNRIBOTOXIN.
DR SUPFAM; SSF53933; SSF53933; 1.
PE 1: Evidence at protein level;
KW Allergen; Direct protein sequencing; Disulfide bond; Hydrolase; Nuclease;
KW Protein synthesis inhibitor; Reference proteome; Secreted; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000269|Ref.6"
FT CHAIN 28..176
FT /note="Ribonuclease mitogillin"
FT /id="PRO_0000030837"
FT ACT_SITE 76
FT /evidence="ECO:0000250"
FT ACT_SITE 122
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 163
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT DISULFID 32..174
FT DISULFID 102..158
FT CONFLICT 52
FT /note="S -> N (in Ref. 2; CAA41217/AAB07779)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 176 AA; 19595 MW; AAD431C57939E42C CRC64;
MVAIKNLFLL AATAVSVLAA PSPLDARATW TCINQQLNPK TNKWEDKRLL YSQAKAESNS
HHAPLSDGKT GSSYPHWFTN GYDGNGKLIK GRTPIKFGKA DCDRPPKHSQ NGMGKDDHYL
LEFPTFPDGH DYKFDSKKPK EDPGPARVIY TYPNKVFCGI VAHQRGNQGD LRLCSH
