CR115_PHYSP
ID CR115_PHYSP Reviewed; 449 AA.
AC E9M7A1; G4Z462;
DT 18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 25-MAY-2022, entry version 15.
DE RecName: Full=Crinkler effector protein 115 {ECO:0000303|PubMed:21071601};
DE Flags: Precursor;
GN Name=CRN115; ORFNames=PHYSODRAFT_330091;
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 GLU-328, SUBUNIT, AND INTERACTION WITH CRN63.
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 CRN63, is critical to
CC pathogenesis by modulating host defenses (PubMed:21071601). Suppresses
CC cell death elicited by the P.sojae necrosis-inducing protein or CRN63
CC (PubMed:21071601). CRN115 and CRN63 may share the same molecular host
CC targets that are involved in the cell death signal transduction pathway
CC and that their differential activities are dependent on plant nuclear
CC localization or not (PubMed:21071601). {ECO:0000269|PubMed:21071601}.
CC -!- SUBUNIT: Forms a homodimer via an inverted association manner
CC (Probable). Forms a heteroodimer with CRN63 (PubMed:27243217).
CC {ECO:0000269|PubMed:27243217, ECO:0000305|PubMed:27243217}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21071601}. Host cell
CC {ECO:0000269|PubMed:21071601}.
CC -!- INDUCTION: Expression is the highest at the mycelium stage.
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 not required for its function to suppress
CC CRN63- or NIP-derived cell death. {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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EGZ22256.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; HQ231784; ADU87014.1; -; mRNA.
DR EMBL; JH159153; EGZ22256.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_009524973.1; XM_009526678.1.
DR AlphaFoldDB; E9M7A1; -.
DR EnsemblProtists; EGZ22256; EGZ22256; PHYSODRAFT_330091.
DR GeneID; 20646050; -.
DR KEGG; psoj:PHYSODRAFT_330091; -.
DR HOGENOM; CLU_054504_1_0_1; -.
DR Proteomes; UP000002640; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0043657; C:host cell; IEA:UniProtKB-SubCell.
DR InterPro; IPR045379; Crinkler_N.
DR Pfam; PF20147; Crinkler; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Reference proteome; Secreted; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..449
FT /note="Crinkler effector protein 115"
FT /id="PRO_0000447895"
FT REGION 18..54
FT /note="LQLFLAK domain"
FT /evidence="ECO:0000305|PubMed:21071601"
FT REGION 57..116
FT /note="DWL domain"
FT /evidence="ECO:0000305|PubMed:21071601"
FT REGION 124..449
FT /note="Effector domain"
FT /evidence="ECO:0000305|PubMed:21071601"
FT MOTIF 117..123
FT /note="HVLVXXP motif"
FT /evidence="ECO:0000305|PubMed:21071601"
FT MOTIF 217..223
FT /note="Nuclear localization signal (NLS)"
FT /evidence="ECO:0000305|PubMed:21071601"
FT CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 341
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT MUTAGEN 328
FT /note="E->K: Allows CRN115 to induce cell death in host
FT cells."
FT /evidence="ECO:0000269|PubMed:27243217"
SQ SEQUENCE 449 AA; 49875 MW; F22848B4F6E90273 CRC64;
MVKLFCAIVG VAGSAFPVDI DGGQSVGDLK KAIKAESEDI TIPAKDLKLF LAKTEGGAWL
PDDDQAALDL EDGKVHEDIQ ALIDGEKMKA TWTIEDVLTA NNMTKRKGRA PKSRQIHVLV
VVPEGAFGSA SETSKMDQLV EKVDKMYEQT VLGKRKYVHS EVTSTQGRQL LNDLDIRVEF
VRTVPFDAGE GSSVDPYEWK RVIIENGEEV VLTEEQQRKR YRRYVEHNIG TVLKETQLCV
IGVERGTNIL TVKVPGREIE LAGRTDLLIL SDLVAMRPTE VQYLPGVKML IEVKRDVKAS
NDFQALSELI ALDLLVDDPV MALLTDLEGE WIFFWVAEKI NSSARIHKAA INKPGEAFEV
IRALLVQPPT APADTDTTEI KLPYFQSPVK RLKLRKALPP IGEGGDNGGI RESIERYYDI
ASMLGPDIEM ARAVARQVTR SIPTFSYFS
