ID   CR161_PHYSP             Reviewed;         443 AA.
AC   G4YUT3;
DT   18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT   14-DEC-2011, sequence version 1.
DT   25-MAY-2022, entry version 22.
DE   RecName: Full=Crinkler effector protein 161;
DE   Flags: Precursor;
GN   Name=CRN161 {ECO:0000303|PubMed:26546319}; ORFNames=PHYSODRAFT_480289;
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 [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   [2]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=26546319; DOI=10.1093/pcp/pcv164;
RA   Rajput N.A., Zhang M., Shen D., Liu T., Zhang Q., Ru Y., Sun P., Dou D.;
RT   "Overexpression of a Phytophthora cytoplasmic CRN effector confers
RT   resistance to disease, salinity and drought in Nicotiana benthamiana.";
RL   Plant Cell Physiol. 56:2423-2435(2015).
CC   -!- FUNCTION: Secreted effector that exhibits strong cell death suppression
CC       activity and suppresses cell death induced by a variety of effectors
CC       including CRN63, Avh241 and Avr3a (PubMed:26546319). Protects host
CC       plants from biotic and abiotic stresses such as salinity and drought by
CC       up-regulation of many defense-related genes, including ABC
CC       transporters, Cytochrome P450 monooxygenases and receptor-like kinases
CC       (RLKs) (PubMed:26546319). Enhances also resistance to Phytophtora
CC       pathogens (PubMed:26546319). {ECO:0000269|PubMed:26546319}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:26546319}. Host
CC       nucleus {ECO:0000269|PubMed:26546319}.
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:26546319}.
CC   -!- SIMILARITY: Belongs to the Crinkler effector family. {ECO:0000305}.
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DR   EMBL; JH159152; EGZ26008.1; -; Genomic_DNA.
DR   RefSeq; XP_009521296.1; XM_009523001.1.
DR   AlphaFoldDB; G4YUT3; -.
DR   EnsemblProtists; EGZ26008; EGZ26008; PHYSODRAFT_480289.
DR   GeneID; 20655240; -.
DR   KEGG; psoj:PHYSODRAFT_480289; -.
DR   Proteomes; UP000002640; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   InterPro; IPR045379; Crinkler_N.
DR   Pfam; PF20147; Crinkler; 1.
PE   3: Inferred from homology;
KW   Host nucleus; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..443
FT                   /note="Crinkler effector protein 161"
FT                   /id="PRO_0000447896"
FT   REGION          18..56
FT                   /note="LQLFLAK domain"
FT                   /evidence="ECO:0000305|PubMed:26546319"
FT   REGION          57..126
FT                   /note="DWL domain"
FT                   /evidence="ECO:0000305|PubMed:26546319"
FT   REGION          134..439
FT                   /note="Effector domain"
FT                   /evidence="ECO:0000305|PubMed:26546319"
FT   MOTIF           127..133
FT                   /note="HVLVXXP motif"
FT                   /evidence="ECO:0000305|PubMed:26546319"
FT   MOTIF           161..170
FT                   /note="Nuclear localization signal 1"
FT                   /evidence="ECO:0000305|PubMed:26546319"
FT   MOTIF           384..393
FT                   /note="Nuclear localization signal 2"
FT                   /evidence="ECO:0000305|PubMed:26546319"
SQ   SEQUENCE   443 AA;  49707 MW;  495A64A390ED67EF CRC64;
     MVKLSCVIVG VPGDPFQVEI DEICELVAGL KDAIKKEKPD SIKCDADKLQ LFKAAKEDRT
     FSASGAEEEK KDFRWLKAAS DDVKKLKHGE KTAAIEAVVR KDQVLRGKET VSDVLMGMES
     PSISQIHVLV VLPEDSESEG GTSAQPAEKE RLLKFLREQA ADKKRKRYWH SEMDMDQGWE
     LLDDFDLTVK PVSTVHAEAD PADSFNWQSD LVQDGQEVVL TEEQQRGRYR EYVERNIGAV
     LKENKLCVTA VDEGENVLSV DVPKLGIELR GRTDLLVLSD IVEETSDYLM HLPEVKMLIE
     VKRDAEASDF QALSELIALD ILAEDPVMAL LTDLNQSWKF FWVSKKSDDS DCICKATIKS
     PGEAFQVIRA LLTASAETKL PCFHQPLKRL KLSQHRGYKN AECLQQYYKV AEVSGPDYEL
     ARAVAEHLVR SMPGYCCANE SEP