PIT2_USTMA
ID PIT2_USTMA Reviewed; 120 AA.
AC A0A0D1EAR7;
DT 31-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2015, sequence version 1.
DT 25-MAY-2022, entry version 22.
DE RecName: Full=Secreted effector PIT2 {ECO:0000303|PubMed:17080091};
DE AltName: Full=Proteins important for tumors 2 {ECO:0000303|PubMed:21692877};
DE Flags: Precursor;
GN Name=PIT2 {ECO:0000303|PubMed:21692877}; ORFNames=UMAG_01375;
OS Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX NCBI_TaxID=237631;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=521 / FGSC 9021;
RX PubMed=17080091; DOI=10.1038/nature05248;
RA Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J.,
RA Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H.,
RA Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G.,
RA Snetselaar K., McCann M., Perez-Martin J., Feldbruegge M., Basse C.W.,
RA Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L.,
RA Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L.,
RA Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N.,
RA Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B.,
RA Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J.,
RA Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P.,
RA Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G.,
RA Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A.,
RA Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M.,
RA Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M.,
RA Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E.,
RA Birren B.W.;
RT "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT maydis.";
RL Nature 444:97-101(2006).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=521 / FGSC 9021;
RA Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP INDUCTION, FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX PubMed=21692877; DOI=10.1111/j.1365-2958.2011.07728.x;
RA Doehlemann G., Reissmann S., Assmann D., Fleckenstein M., Kahmann R.;
RT "Two linked genes encoding a secreted effector and a membrane protein are
RT essential for Ustilago maydis-induced tumour formation.";
RL Mol. Microbiol. 81:751-766(2011).
RN [4]
RP INTERACTION WITH HOST CP1A; CP1B; XCP2 AND CP2, FUNCTION, DOMAIN, AND
RP MUTAGENESIS OF 51-ARG--PHE-55.
RX PubMed=23459172; DOI=10.1371/journal.ppat.1003177;
RA Mueller A.N., Ziemann S., Treitschke S., Assmann D., Doehlemann G.;
RT "Compatibility in the Ustilago maydis-maize interaction requires inhibition
RT of host cysteine proteases by the fungal effector Pit2.";
RL PLoS Pathog. 9:E1003177-E1003177(2013).
RN [5]
RP INDUCTION, AND SUBCELLULAR LOCATION.
RX PubMed=27093436; DOI=10.1371/journal.pone.0153861;
RA Hampel M., Jakobi M., Schmitz L., Meyer U., Finkernagel F., Doehlemann G.,
RA Heimel K.;
RT "Unfolded protein response (UPR) regulator Cib1 controls expression of
RT genes encoding secreted virulence factors in Ustilago maydis.";
RL PLoS ONE 11:E0153861-E0153861(2016).
RN [6]
RP FUNCTION, DOMAIN, CLEAVAGE BY HOST CYSTEINE PROTEASES, AND MUTAGENESIS OF
RP ARG-50 AND TRP-51.
RX PubMed=30952847; DOI=10.1038/s41467-019-09472-8;
RA Misas Villamil J.C., Mueller A.N., Demir F., Meyer U., Oekmen B.,
RA Schulze Hueynck J., Breuer M., Dauben H., Win J., Huesgen P.F.,
RA Doehlemann G.;
RT "A fungal substrate mimicking molecule suppresses plant immunity via an
RT inter-kingdom conserved motif.";
RL Nat. Commun. 10:1576-1576(2019).
CC -!- FUNCTION: Secreted effector required for virulence (PubMed:21692877,
CC PubMed:23459172). Functions as an inhibitor of a set of apoplastic
CC maize papain-like cysteine proteases (PLCPs) including CP1A, CP1B, XCP2
CC and CP2, whose activity is directly linked with salicylic-acid-
CC associated plant defenses (PubMed:23459172). Acts as a substrate
CC mimicking molecule for apoplastic PLCPs and its processing releases the
CC embedded inhibitor peptide PID14, which in turn blocks PLCPs to
CC modulate host immunity (PubMed:30952847). {ECO:0000269|PubMed:21692877,
CC ECO:0000269|PubMed:23459172, ECO:0000269|PubMed:30952847}.
CC -!- SUBUNIT: Interacts with host cysteine proteases CP1A, CP1B, XCP2 and
CC CP2. {ECO:0000269|PubMed:23459172}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21692877,
CC ECO:0000269|PubMed:27093436}. Note=Secreted to the biotrophic
CC interface. {ECO:0000269|PubMed:21692877}.
CC -!- INDUCTION: Expression is highly up-regulated during all stages of
CC pathogenic development (PubMed:21692877). Expression is positively
CC regulated by the unfolded protein response (UPR) signaling via the
CC binding of CIB1 to the UPRE motif localized at the PIT1/PIT2 promoter
CC (PubMed:27093436). {ECO:0000269|PubMed:21692877,
CC ECO:0000269|PubMed:27093436}.
CC -!- DOMAIN: The PID14 protease inhibitor domain is sufficient for
CC inhibition of host cysteine proteases. {ECO:0000269|PubMed:23459172,
CC ECO:0000269|PubMed:30952847}.
CC -!- PTM: Cleaved by host target papain-like cysteine proteases (PLCPs) to
CC release the embedded inhibitor peptide PID14.
CC {ECO:0000269|PubMed:30952847}.
CC -!- DISRUPTION PHENOTYPE: Keeps the ability to penetrate maize epidermis
CC and to grow intracellularly at sites of infection but fails to spread
CC and induce tumors in infected leaves. {ECO:0000269|PubMed:21692877}.
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DR EMBL; CM003141; KIS71480.1; -; Genomic_DNA.
DR RefSeq; XP_011387264.1; XM_011388962.1.
DR AlphaFoldDB; A0A0D1EAR7; -.
DR EnsemblFungi; KIS71480; KIS71480; UMAG_01375.
DR GeneID; 23562420; -.
DR KEGG; uma:UMAG_01375; -.
DR VEuPathDB; FungiDB:UMAG_01375; -.
DR eggNOG; ENOG502TK2Y; Eukaryota.
DR OrthoDB; 1652226at2759; -.
DR Proteomes; UP000000561; Chromosome 2.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
PE 1: Evidence at protein level;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..120
FT /note="Secreted effector PIT2"
FT /id="PRO_5002245312"
FT REGION 46..59
FT /note="PID14 protease inhibitor domain"
FT /evidence="ECO:0000269|PubMed:23459172"
FT MUTAGEN 50
FT /note="R->A: Impairs the virulence; when associated with A-
FT 51."
FT /evidence="ECO:0000269|PubMed:30952847"
FT MUTAGEN 51..55
FT /note="WWFGF->GGAGG: Loses protease inhibition activity and
FT impairs the formation of tumors in plant leaves."
FT /evidence="ECO:0000269|PubMed:23459172"
FT MUTAGEN 51
FT /note="W->A: Impairs the virulence; when associated with A-
FT 50."
FT /evidence="ECO:0000269|PubMed:30952847"
SQ SEQUENCE 120 AA; 13424 MW; 885EADD9020A8C0B CRC64;
MLFRSAFVLL IVAFASACLV QHVQAKQIPV RRSLSTDASM SSAAGKLNRR WWFGFTGSLG
KEPDNGQVQI KIIPDALIIK NPPANKDDLN KLIENLKRKH PRFKTVVMPT DPNGDVVIWE
