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SFI3_PHYIT
ID   SFI3_PHYIT              Reviewed;         127 AA.
AC   D0N6D2;
DT   08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2009, sequence version 1.
DT   03-AUG-2022, entry version 41.
DE   RecName: Full=RxLR effector protein SFI3 {ECO:0000303|PubMed:24763622};
DE   AltName: Full=Suppressor of early Flg22-induced immune response 3 {ECO:0000303|PubMed:24763622};
DE   Flags: Precursor;
GN   Name=SFI3 {ECO:0000303|PubMed:24763622};
GN   Synonyms=PexRD16 {ECO:0000303|PubMed:19794118}; ORFNames=PITG_06087;
OS   Phytophthora infestans (strain T30-4) (Potato late blight agent).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=403677;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T30-4;
RX   PubMed=19741609; DOI=10.1038/nature08358;
RG   The Broad Institute Genome Sequencing Platform;
RA   Haas B.J., Kamoun S., Zody M.C., Jiang R.H., Handsaker R.E., Cano L.M.,
RA   Grabherr M., Kodira C.D., Raffaele S., Torto-Alalibo T., Bozkurt T.O.,
RA   Ah-Fong A.M., Alvarado L., Anderson V.L., Armstrong M.R., Avrova A.,
RA   Baxter L., Beynon J., Boevink P.C., Bollmann S.R., Bos J.I., Bulone V.,
RA   Cai G., Cakir C., Carrington J.C., Chawner M., Conti L., Costanzo S.,
RA   Ewan R., Fahlgren N., Fischbach M.A., Fugelstad J., Gilroy E.M., Gnerre S.,
RA   Green P.J., Grenville-Briggs L.J., Griffith J., Grunwald N.J., Horn K.,
RA   Horner N.R., Hu C.H., Huitema E., Jeong D.H., Jones A.M., Jones J.D.,
RA   Jones R.W., Karlsson E.K., Kunjeti S.G., Lamour K., Liu Z., Ma L.,
RA   Maclean D., Chibucos M.C., McDonald H., McWalters J., Meijer H.J.,
RA   Morgan W., Morris P.F., Munro C.A., O'Neill K., Ospina-Giraldo M.,
RA   Pinzon A., Pritchard L., Ramsahoye B., Ren Q., Restrepo S., Roy S.,
RA   Sadanandom A., Savidor A., Schornack S., Schwartz D.C., Schumann U.D.,
RA   Schwessinger B., Seyer L., Sharpe T., Silvar C., Song J., Studholme D.J.,
RA   Sykes S., Thines M., van de Vondervoort P.J., Phuntumart V., Wawra S.,
RA   Weide R., Win J., Young C., Zhou S., Fry W., Meyers B.C., van West P.,
RA   Ristaino J., Govers F., Birch P.R., Whisson S.C., Judelson H.S.,
RA   Nusbaum C.;
RT   "Genome sequence and analysis of the Irish potato famine pathogen
RT   Phytophthora infestans.";
RL   Nature 461:393-398(2009).
RN   [2]
RP   IDENTIFICATION, AND DOMAIN.
RX   PubMed=19794118; DOI=10.1105/tpc.109.068247;
RA   Oh S.K., Young C., Lee M., Oliva R., Bozkurt T.O., Cano L.M., Win J.,
RA   Bos J.I., Liu H.Y., van Damme M., Morgan W., Choi D., Van der Vossen E.A.,
RA   Vleeshouwers V.G., Kamoun S.;
RT   "In planta expression screens of Phytophthora infestans RXLR effectors
RT   reveal diverse phenotypes, including activation of the Solanum
RT   bulbocastanum disease resistance protein Rpi-blb2.";
RL   Plant Cell 21:2928-2947(2009).
RN   [3]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=24763622; DOI=10.1371/journal.ppat.1004057;
RA   Zheng X., McLellan H., Fraiture M., Liu X., Boevink P.C., Gilroy E.M.,
RA   Chen Y., Kandel K., Sessa G., Birch P.R., Brunner F.;
RT   "Functionally redundant RXLR effectors from Phytophthora infestans act at
RT   different steps to suppress early flg22-triggered immunity.";
RL   PLoS Pathog. 10:E1004057-E1004057(2014).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 49-127, SUBUNIT, FUNCTION,
RP   SUBCELLULAR LOCATION, INTERACTION WITH HOST UBK, AND MUTAGENESIS OF LEU-86;
RP   LEU-100 AND LEU-103.
RX   PubMed=30536576; DOI=10.1111/nph.15635;
RA   He Q., McLellan H., Hughes R.K., Boevink P.C., Armstrong M., Lu Y.,
RA   Banfield M.J., Tian Z., Birch P.R.J.;
RT   "Phytophthora infestans effector SFI3 targets potato UBK to suppress early
RT   immune transcriptional responses.";
RL   New Phytol. 222:438-454(2019).
CC   -!- FUNCTION: Effector that suppresses flg22-induced post-translational MAP
CC       kinase activation in potato and tomato, but not in Arabidopsis. The
CC       perception of highly conserved pathogen- or microbe-associated
CC       molecular patterns (PAMPs/MAMPs), such as flg22, triggers converging
CC       signaling pathways recruiting MAP kinase cascades and inducing
CC       transcriptional re-programming, yielding a generic antimicrobial
CC       response (PubMed:24763622, PubMed:30536576). Does not suppress
CC       programmed cell death triggered by the P.infestans elicitin infestin-1
CC       (INF1), or by co-expression of tomato Cf4 with Cladosporium fulvum Avr4
CC       (PubMed:30536576). Suppresses early pattern-triggered immunity (PTI)
CC       via interaction with the U-box-kinase protein UBK, a positive regulator
CC       of specific PTI pathways in both potato and Nicotiana benthamiana
CC       (PubMed:30536576). {ECO:0000269|PubMed:24763622,
CC       ECO:0000269|PubMed:30536576}.
CC   -!- SUBUNIT: Forms an unusual trans-homodimer (PubMed:30536576). Interacts
CC       with host UBK (PubMed:30536576). {ECO:0000269|PubMed:30536576}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24763622}. Host
CC       nucleus, host nucleolus {ECO:0000269|PubMed:24763622}. Host nucleus
CC       {ECO:0000269|PubMed:30536576}. Note=Forms a ring around the nucleolus.
CC       {ECO:0000269|PubMed:24763622}.
CC   -!- DOMAIN: The WY-domain is involved in the homodimerization leading to a
CC       novel trans WY-domain configuration in which the Trp and Tyr residues
CC       are derived from separate monomers. {ECO:0000269|PubMed:30536576}.
CC   -!- DOMAIN: The RxLR-dEER motif acts to carry the protein into the host
CC       cell cytoplasm through binding to cell surface phosphatidylinositol-3-
CC       phosphate. {ECO:0000305|PubMed:19794118}.
CC   -!- SIMILARITY: Belongs to the RxLR effector family. {ECO:0000305}.
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DR   EMBL; DS028126; EEY70623.1; -; Genomic_DNA.
DR   RefSeq; XP_002998277.1; XM_002998231.1.
DR   PDB; 6GU1; X-ray; 1.70 A; A/B=49-127.
DR   PDBsum; 6GU1; -.
DR   AlphaFoldDB; D0N6D2; -.
DR   SMR; D0N6D2; -.
DR   EnsemblProtists; PITG_06087T0; PITG_06087T0; PITG_06087.
DR   GeneID; 9472246; -.
DR   KEGG; pif:PITG_06087; -.
DR   VEuPathDB; FungiDB:PITG_06087; -.
DR   eggNOG; ENOG502RFDT; Eukaryota.
DR   HOGENOM; CLU_1974887_0_0_1; -.
DR   InParanoid; D0N6D2; -.
DR   OMA; FYTAMEK; -.
DR   OrthoDB; 1648902at2759; -.
DR   PHI-base; PHI:4202; -.
DR   Proteomes; UP000006643; Partially assembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0044196; C:host cell nucleolus; IEA:UniProtKB-SubCell.
PE   1: Evidence at protein level;
KW   3D-structure; Host nucleus; Reference proteome; Secreted; Signal;
KW   Virulence.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..127
FT                   /note="RxLR effector protein SFI3"
FT                   /id="PRO_5003012132"
FT   REGION          72..107
FT                   /note="WY-domain"
FT                   /evidence="ECO:0000305|PubMed:30536576"
FT   MOTIF           40..62
FT                   /note="RxLR-dEER"
FT                   /evidence="ECO:0000305|PubMed:19794118"
FT   MUTAGEN         86
FT                   /note="L->D: Disrupts homooligomerization, prevents
FT                   association with UBK, impairs nucleolar localization and
FT                   accumulates in the nucleoplasm with cytoplasmic background;
FT                   when associated with D-100 or D-103."
FT                   /evidence="ECO:0000269|PubMed:30536576"
FT   MUTAGEN         100
FT                   /note="L->D: Disrupts homooligomerization, prevents
FT                   association with UBK, impairs nucleolar localization and
FT                   accumulates in the nucleoplasm with cytoplasmic background;
FT                   when associated with D-86."
FT                   /evidence="ECO:0000269|PubMed:30536576"
FT   MUTAGEN         103
FT                   /note="L->D: Disrupts homooligomerization, prevents
FT                   association with UBK, impairs nucleolar localization and
FT                   accumulates in the nucleoplasm with cytoplasmic background;
FT                   when associated with D-86."
FT                   /evidence="ECO:0000269|PubMed:30536576"
FT   HELIX           64..74
FT                   /evidence="ECO:0007829|PDB:6GU1"
FT   HELIX           79..116
FT                   /evidence="ECO:0007829|PDB:6GU1"
SQ   SEQUENCE   127 AA;  14388 MW;  585EB6F34B155692 CRC64;
     MRFLLVAVVA MMALVSSSTA AVAETSNDIN TMNNNQEFAR SLRNTEERSI AAILAEAGEE
     DRAAWRINYR AWYKAKLTPT QVKTVLGVSQ AEMNNVAKQL QRLYLGYYSF YTAMEKKKEE
     KKRLATP
 
 
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