CR108_PHYSO
ID CR108_PHYSO Reviewed; 820 AA.
AC A0A0M5K865;
DT 05-JUN-2019, integrated into UniProtKB/Swiss-Prot.
DT 09-DEC-2015, sequence version 1.
DT 25-MAY-2022, entry version 14.
DE RecName: Full=Crinkler effector protein 108 {ECO:0000303|PubMed:26714171};
DE Flags: Precursor;
GN Name=CRN108 {ECO:0000303|PubMed:26714171};
OS Phytophthora sojae (Soybean stem and root rot agent) (Phytophthora
OS megasperma f. sp. glycines).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=67593;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], DOMAIN, INDUCTION, FUNCTION, SUBCELLULAR
RP LOCATION, AND MUTAGENESIS OF 120-LYS--ARG-123; LEU-766; GLY-768 AND
RP VAL-769.
RC STRAIN=P6497;
RX PubMed=26714171; DOI=10.1371/journal.ppat.1005348;
RA Song T., Ma Z., Shen D., Li Q., Li W., Su L., Ye T., Zhang M., Wang Y.,
RA Dou D.;
RT "An oomycete CRN effector reprograms expression of plant HSP genes by
RT targeting their promoters.";
RL PLoS Pathog. 11:E1005348-E1005348(2015).
CC -!- FUNCTION: Secreted effector that suppresses plant basal defense and
CC promotes plant susceptibility via targeting promoters of host HSP gene
CC and thus inhibiting their expression. CRN108 binds directly to heat
CC shock elements (HSEs) 5'-GAAnnTTC-3' and interferes with the
CC association of the HSE with the plant heat shock transcription factors,
CC which initializes HSP gene expression in response to stress.
CC {ECO:0000269|PubMed:26714171}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:26714171}. Host
CC nucleus {ECO:0000269|PubMed:26714171}.
CC -!- INDUCTION: Expressed at a high level during the early stages of
CC infection. {ECO:0000269|PubMed:26714171}.
CC -!- DOMAIN: The CRN proteins have modular architectures that include a
CC signal peptide, a conserved N-terminus, and highly diverse C-terminal
CC domains. The conserved CRN N-terminus harbors a distinct LXLFLAK motif,
CC which is followed by the conserved DWL domain. A highly conserved
CC HVLVXXP motif marks the end of the CRN N-terminal domains and forms a
CC junction where diverse C-terminal domains are fused. The conserved CRN
CC N-terminus mediates the translocation into the plant host cells.
CC {ECO:0000305|PubMed:26714171}.
CC -!- DOMAIN: The C-terminal DC effector region contains a helix-hairpin-
CC helix (HhH) DNA-binding domain involved in the binding to heat shock
CC elements (HSEs), which are conserved in the promoter regions of HSP
CC genes at promoters of targeted heat shock protein coding genes.
CC {ECO:0000269|PubMed:26714171}.
CC -!- SIMILARITY: Belongs to the Crinkler effector family. {ECO:0000305}.
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DR EMBL; KT726855; ALD51957.1; -; mRNA.
DR AlphaFoldDB; A0A0M5K865; -.
DR VEuPathDB; FungiDB:PHYSODRAFT_348355; -.
DR PHI-base; PHI:5392; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR InterPro; IPR045379; Crinkler_N.
DR InterPro; IPR010994; RuvA_2-like.
DR Pfam; PF20147; Crinkler; 1.
DR SUPFAM; SSF47781; SSF47781; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Glycoprotein; Host nucleus; Secreted; Signal; Virulence.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..820
FT /note="Crinkler effector protein 108"
FT /id="PRO_0000447424"
FT REGION 18..55
FT /note="LQLFLAK domain"
FT /evidence="ECO:0000305|PubMed:26714171"
FT REGION 58..111
FT /note="DWL domain"
FT /evidence="ECO:0000305|PubMed:26714171"
FT REGION 125..820
FT /note="C-terminal DC effector domain"
FT /evidence="ECO:0000305|PubMed:26714171"
FT REGION 754..791
FT /note="HhH DNA-binding domain"
FT /evidence="ECO:0000305|PubMed:26714171"
FT MOTIF 112..117
FT /note="HVLVXXP motif"
FT /evidence="ECO:0000305|PubMed:26714171"
FT MOTIF 118..124
FT /note="Host nuclear localization signal"
FT /evidence="ECO:0000269|PubMed:26714171"
FT CARBOHYD 268
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 371
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 703
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT MUTAGEN 120..123
FT /note="KKRR->AAAA: Abolishes accumulation in the host
FT nucleus and fails to significantly promote plant
FT susceptibility to P.capsici infection and to suppress
FT callose deposition and ROS accumulation in N.benthamiana."
FT /evidence="ECO:0000269|PubMed:26714171"
FT MUTAGEN 766
FT /note="L->A: Does not affect accumulation in the host
FT nucleus but fails to significantly promote plant
FT susceptibility to P.capsici infection and to suppress
FT callose deposition and ROS accumulation in N.benthamiana;
FT when associated with A-768 and A-769."
FT /evidence="ECO:0000269|PubMed:26714171"
FT MUTAGEN 768
FT /note="G->A: Does not affect accumulation in the host
FT nucleus but fails to significantly promote plant
FT susceptibility to P.capsici infection and to suppress
FT callose deposition and ROS accumulation in N.benthamiana;
FT when associated with A-768 and A-769."
FT /evidence="ECO:0000269|PubMed:26714171"
FT MUTAGEN 769
FT /note="V->A: Does not affect accumulation in the host
FT nucleus but fails to significantly promote plant
FT susceptibility to P.capsici infection and to suppress
FT callose deposition and ROS accumulation in N.benthamiana;
FT when associated with A-768 and A-769."
FT /evidence="ECO:0000269|PubMed:26714171"
SQ SEQUENCE 820 AA; 91945 MW; 3F6EBE141D26EC99 CRC64;
MVKLYCAVVG VAGSAFSVRV DESDTVDDLK DAIKAKKPND FKDIDADKLE LYVAKRDGVW
LTEADVKSGV ADITGLVRLE VVRAKLFSVG LSDEVVSEVD AQEEAAGRGP VNVLVVVPMK
KRRVDAGVDE ERRFFDTRDF PPLLAPPQRG ATVESPEAQW EKLLNSLEWK EPKRLCASSG
QNWPYQGESE LAGHLVEPLA LHYTAWYLQN EDKQNHAINL VLSGPGTGKS RMLDQMKGLM
CAAAARSNNR KLKERMENAF VFSVTFENGT SATGSLLDRD NPEFDISYRM LYQLSKDRPN
WKKFAKTLKS YRSLELDIEA AIGILAKLKG IDDVKKMTVI LCVDGLQKLV NDGTKSCDFY
RVLASVCSFL NSSRAFAVCV CSATIQSPVD KALSDSPQKR VFLVPPPLRG HEVLPTKTRI
EKQLVDDMGG HGRALETLQL FLSHYTKDQL EEMDPTWMFE KVCDALRLQY GDIFASPFFQ
DPYNCREVLA AILSRRRYKL FDRIGRTDMT VDCLRSFGLF RWGAEGHLEC AFILLVLLMQ
KLPKKLGEVD NFDDHLTRTV LVWQRFEQFV AFYRRVKSIA YCETPVALSS FHAGARFGAI
QDIIITEPTS RTVVEALRQE DTKSSSDDST CFTNRDGGVK ISDMDTIVIN GASASAGDLF
MRVQLKVGRQ NVQCNEVIQC KLLQTKQKIH EDAYAKERAK AANESSDVFL LVTPAQATEF
DLPPRCGLVS ANEFGRYFGP FTSRAYRSFL EPPNINTASF HELRRLEGVG DATAAKIIAE
RTIRRFSNLE DALNRLVPSK KGKTAMILSR MHYDDDEADL
