CRN63_PHYSP
ID CRN63_PHYSP Reviewed; 450 AA.
AC G4YRT1; E9M7A0;
DT 18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT 25-JAN-2012, sequence version 1.
DT 25-MAY-2022, entry version 22.
DE RecName: Full=Crinkler effector protein 63 {ECO:0000303|PubMed:21071601};
DE Flags: Precursor;
GN Name=CRN63 {ECO:0000303|PubMed:21071601}; ORFNames=PHYSODRAFT_253824;
OS Phytophthora sojae (strain P6497) (Soybean stem and root rot agent)
OS (Phytophthora megasperma f. sp. glycines).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=1094619;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], INDUCTION, FUNCTION, DISRUPTION PHENOTYPE,
RP DOMAIN, AND SUBCELLULAR LOCATION.
RC STRAIN=P6497;
RX PubMed=21071601; DOI=10.1104/pp.110.166470;
RA Liu T., Ye W., Ru Y., Yang X., Gu B., Tao K., Lu S., Dong S., Zheng X.,
RA Shan W., Wang Y., Dou D.;
RT "Two host cytoplasmic effectors are required for pathogenesis of
RT Phytophthora sojae by suppression of host defenses.";
RL Plant Physiol. 155:490-501(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P6497;
RX PubMed=16946064; DOI=10.1126/science.1128796;
RA Tyler B.M., Tripathy S., Zhang X., Dehal P., Jiang R.H.Y., Aerts A.,
RA Arredondo F.D., Baxter L., Bensasson D., Beynon J.L., Chapman J.,
RA Damasceno C.M.B., Dorrance A.E., Dou D., Dickerman A.W., Dubchak I.L.,
RA Garbelotto M., Gijzen M., Gordon S.G., Govers F., Grunwald N.J., Huang W.,
RA Ivors K.L., Jones R.W., Kamoun S., Krampis K., Lamour K.H., Lee M.-K.,
RA McDonald W.H., Medina M., Meijer H.J.G., Nordberg E.K., Maclean D.J.,
RA Ospina-Giraldo M.D., Morris P.F., Phuntumart V., Putnam N.H., Rash S.,
RA Rose J.K.C., Sakihama Y., Salamov A.A., Savidor A., Scheuring C.F.,
RA Smith B.M., Sobral B.W.S., Terry A., Torto-Alalibo T.A., Win J., Xu Z.,
RA Zhang H., Grigoriev I.V., Rokhsar D.S., Boore J.L.;
RT "Phytophthora genome sequences uncover evolutionary origins and mechanisms
RT of pathogenesis.";
RL Science 313:1261-1266(2006).
RN [3]
RP FUNCTION, MUTAGENESIS OF LYS-329, SUBUNIT, AND INTERACTION WITH CRN79 AND
RP CRN115.
RX PubMed=27243217; DOI=10.1038/srep26951;
RA Li Q., Zhang M., Shen D., Liu T., Chen Y., Zhou J.M., Dou D.;
RT "A Phytophthora sojae effector PsCRN63 forms homo-/hetero-dimers to
RT suppress plant immunity via an inverted association manner.";
RL Sci. Rep. 6:26951-26951(2016).
CC -!- FUNCTION: Secreted effector that, with CRN115, is critical to
CC pathogenesis by modulating host defenses (PubMed:21071601). Induces
CC cell death in plant host cells (PubMed:21071601). Suppresses callose
CC deposition and affects expression of defense-related genes including
CC two salicylic acid (SA) signal-induced and antimicrobial PR genes (PR1
CC and PR2), and genes involved in jasmonic acid (JA)/ethylene (ET)-
CC mediated defense pathway (ERF1, ORA59, PDF1.2) (PubMed:27243217).
CC CRN115 and CRN63 may share the same molecular host targets that are
CC involved in the cell death signal transduction pathway and that their
CC differential activities are dependent on plant nuclear localization or
CC not (PubMed:21071601). Does not affect MAPK activation and BIK1
CC phosphorylation and acts downstream of the MAPK cascades in PTI
CC signaling (PubMed:27243217). {ECO:0000269|PubMed:21071601,
CC ECO:0000269|PubMed:27243217}.
CC -!- SUBUNIT: Forms a homodimer via an inverted association manner
CC (PubMed:27243217). Forms heterodimers with CRN79 and CRN115
CC (PubMed:27243217). {ECO:0000269|PubMed:27243217}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21071601}. Host
CC nucleus, host nucleoplasm {ECO:0000269|PubMed:21071601}.
CC -!- INDUCTION: Expression is constitutively high and slightly induced
CC during the late infection stages (approximately 1.5-fold).
CC {ECO:0000269|PubMed:21071601}.
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:21071601}.
CC -!- DOMAIN: The C-terminal effector region is sufficient for its activity
CC within the host cell. {ECO:0000269|PubMed:21071601}.
CC -!- DOMAIN: The predicted NLS is required for its function to induces cell
CC death in plant host cells. {ECO:0000269|PubMed:21071601}.
CC -!- DISRUPTION PHENOTYPE: Leads to a reduction of virulence on soybean.
CC {ECO:0000269|PubMed:21071601}.
CC -!- SIMILARITY: Belongs to the Crinkler effector family. {ECO:0000305}.
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DR EMBL; HQ231783; ADU87013.1; -; mRNA.
DR EMBL; JH159152; EGZ22908.1; -; Genomic_DNA.
DR RefSeq; XP_009518196.1; XM_009519901.1.
DR AlphaFoldDB; G4YRT1; -.
DR EnsemblProtists; EGZ22908; EGZ22908; PHYSODRAFT_253824.
DR GeneID; 20638420; -.
DR KEGG; psoj:PHYSODRAFT_253824; -.
DR HOGENOM; CLU_054504_1_0_1; -.
DR InParanoid; G4YRT1; -.
DR OMA; IIECGKE; -.
DR OrthoDB; 1287796at2759; -.
DR Proteomes; UP000002640; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0044095; C:host cell nucleoplasm; IEA:UniProtKB-SubCell.
DR InterPro; IPR045379; Crinkler_N.
DR Pfam; PF20147; Crinkler; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Host nucleus; Reference proteome; Secreted; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..450
FT /note="Crinkler effector protein 63"
FT /id="PRO_0000447894"
FT REGION 18..55
FT /note="LQLFLAK domain"
FT /evidence="ECO:0000305|PubMed:21071601"
FT REGION 58..117
FT /note="DWL domain"
FT /evidence="ECO:0000305|PubMed:21071601"
FT REGION 125..450
FT /note="Effector domain"
FT /evidence="ECO:0000305|PubMed:21071601"
FT MOTIF 118..124
FT /note="HVLVXXP motif"
FT /evidence="ECO:0000305|PubMed:21071601"
FT MOTIF 218..224
FT /note="Nuclear localization signal (NLS)"
FT /evidence="ECO:0000305|PubMed:21071601"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 342
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT MUTAGEN 329
FT /note="K->E: Completely abolishes the cell death-inducing
FT activity."
FT /evidence="ECO:0000269|PubMed:27243217"
SQ SEQUENCE 450 AA; 49755 MW; 9ED594BE3B3B6033 CRC64;
MVKLFCAIVG AAGSAFPVDI DAGQSAGDLK DAIKAKNPAT ITCDAKDLQL SLAKTADGAW
LPDDDQAALD LEDGKVHEDI QALIDGEKMK ATWTIEDVLT ANNMTKRKGR APKSRQIHVL
VVVPEGAFGS ASETSKMDQL VEKVDKMYEQ TVLGKRKYVH SEVTSTQGRQ LLNDLDIRVE
FVRTVPFDAG EGSSVDPYEW KRVIIENGEE VVLTEEQQRK RYRRYVEHNI GAVLKEKQLC
VIGVERGTNI LTVKVPGREI ELAGRTDLLI LSDLVAMRPT EVQYLPGVKM LIEVKRDVKA
SNDFQALSEL IALDLLVDDP VMALLTDLKG EWIFFWVAEK INSSARIHKA AINKPGEAFE
VIRALLVQPP TAPADTDTTE IKLPCFQSPV KRLKLRKALP PIGEGGDNGG IRESIERYYD
IASMLGPDIE MARAVARQVT RSIPTFSYFS
