RLT1_RHIO9
ID RLT1_RHIO9 Reviewed; 147 AA.
AC I1C083;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 1.
DT 23-FEB-2022, entry version 24.
DE RecName: Full=Mucoricin {ECO:0000303|PubMed:33462434};
DE EC=3.2.2.22 {ECO:0000269|PubMed:33462434};
DE AltName: Full=Ricin-like toxin {ECO:0000303|PubMed:33462434};
DE AltName: Full=rRNA N-glycosidase {ECO:0000305};
GN Name=RLT1 {ECO:0000303|PubMed:33462434};
GN ORFNames=RO3G_06568 {ECO:0000312|EMBL:EIE81863.1};
OS Rhizopus delemar (strain RA 99-880 / ATCC MYA-4621 / FGSC 9543 / NRRL
OS 43880) (Mucormycosis agent) (Rhizopus arrhizus var. delemar).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Rhizopodaceae; Rhizopus.
OX NCBI_TaxID=246409 {ECO:0000312|Proteomes:UP000009138};
RN [1] {ECO:0000312|Proteomes:UP000009138}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RA 99-880 / ATCC MYA-4621 / FGSC 9543 / NRRL 43880
RC {ECO:0000312|Proteomes:UP000009138};
RX PubMed=19578406; DOI=10.1371/journal.pgen.1000549;
RA Ma L.-J., Ibrahim A.S., Skory C., Grabherr M.G., Burger G., Butler M.,
RA Elias M., Idnurm A., Lang B.F., Sone T., Abe A., Calvo S.E.,
RA Corrochano L.M., Engels R., Fu J., Hansberg W., Kim J.-M., Kodira C.D.,
RA Koehrsen M.J., Liu B., Miranda-Saavedra D., O'Leary S.,
RA Ortiz-Castellanos L., Poulter R., Rodriguez-Romero J., Ruiz-Herrera J.,
RA Shen Y.-Q., Zeng Q., Galagan J., Birren B.W., Cuomo C.A., Wickes B.L.;
RT "Genomic analysis of the basal lineage fungus Rhizopus oryzae reveals a
RT whole-genome duplication.";
RL PLoS Genet. 5:E1000549-E1000549(2009).
RN [2] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE,
RP INDUCTION, DISRUPTION PHENOTYPE, AND BIOTECHNOLOGY.
RX PubMed=33462434; DOI=10.1038/s41564-020-00837-0;
RA Soliman S.S.M., Baldin C., Gu Y., Singh S., Gebremariam T., Swidergall M.,
RA Alqarihi A., Youssef E.G., Alkhazraji S., Pikoulas A., Perske C.,
RA Venkataramani V., Rich A., Bruno V.M., Hotopp J.D., Mantis N.J.,
RA Edwards J.E. Jr., Filler S.G., Chamilos G., Vitetta E.S., Ibrahim A.S.;
RT "Mucoricin is a ricin-like toxin that is critical for the pathogenesis of
RT mucormycosis.";
RL Nat. Microbiol. 6:313-326(2021).
CC -!- FUNCTION: N-glycosylase that inhibits protein synthesis in the host by
CC depurinating ribosomal rRNA, and thus acts as a ribosomal inactivating
CC protein (RIP) (PubMed:33462434). Promotes vascular permeability in the
CC host and induces necrosis and apoptosis of host alveolar epithelial
CC cells (PubMed:33462434). {ECO:0000269|PubMed:33462434}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of the N-glycosidic bond at one specific
CC adenosine on the 28S rRNA.; EC=3.2.2.22;
CC Evidence={ECO:0000269|PubMed:33462434};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:33462434}.
CC -!- DEVELOPMENTAL STAGE: Induced during germination and expressed during
CC hyphal growth (at protein level) (PubMed:33462434). Not expressed in
CC spores (at protein level) (PubMed:33462434).
CC {ECO:0000269|PubMed:33462434}.
CC -!- INDUCTION: Repressed by hypoxic conditions.
CC {ECO:0000269|PubMed:33462434}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown decreases cytotoxicity in
CC vitro and decreases virulence in a mouse model of infection
CC (PubMed:33462434). RNAi-mediated knockdown has no effect on the
CC germination or cell population growth of the fungus (PubMed:33462434).
CC {ECO:0000269|PubMed:33462434}.
CC -!- BIOTECHNOLOGY: Antibodies against the toxin protects mice from
CC mucormycosis and thus could potentially be used to treat the disease.
CC {ECO:0000305|PubMed:33462434}.
CC -!- SIMILARITY: Belongs to the ribosome-inactivating protein family. Type 1
CC RIP subfamily. {ECO:0000305}.
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DR EMBL; CH476735; EIE81863.1; -; Genomic_DNA.
DR SMR; I1C083; -.
DR EnsemblFungi; EIE81863; EIE81863; RO3G_06568.
DR VEuPathDB; FungiDB:RO3G_06568; -.
DR eggNOG; ENOG502SDNC; Eukaryota.
DR InParanoid; I1C083; -.
DR OMA; WRYEDGY; -.
DR OrthoDB; 1310627at2759; -.
DR Proteomes; UP000009138; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0030598; F:rRNA N-glycosylase activity; IDA:UniProtKB.
DR GO; GO:0090729; F:toxin activity; IDA:UniProtKB.
DR GO; GO:0045007; P:depurination; IDA:UniProtKB.
DR GO; GO:0044073; P:modulation by symbiont of host translation; IC:UniProtKB.
DR GO; GO:0017148; P:negative regulation of translation; IEA:UniProtKB-KW.
DR CDD; cd00161; RICIN; 1.
DR InterPro; IPR035992; Ricin_B-like_lectins.
DR InterPro; IPR000772; Ricin_B_lectin.
DR Pfam; PF00652; Ricin_B_lectin; 1.
DR SMART; SM00458; RICIN; 1.
DR SUPFAM; SSF50370; SSF50370; 1.
DR PROSITE; PS50231; RICIN_B_LECTIN; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Protein synthesis inhibitor; Reference proteome; Secreted;
KW Toxin; Virulence.
FT CHAIN 1..147
FT /note="Mucoricin"
FT /id="PRO_0000453624"
FT DOMAIN 4..143
FT /note="Ricin B-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
SQ SEQUENCE 147 AA; 17138 MW; 24B44728443A16B9 CRC64;
MYFEEGRLFF IKSQFNGRVL DVEDGSTEDD ANIIVYTQKY EDCLNQLWRY ENGYFINAKS
AKVLDIRGGE MQPESQIIQY AQKMVEEAAN QRWAIDEDGY IFCEARPDLV LDIQGAEDED
CVPVILYERR EGEVSANQRW ELVPFEG
