CRN15_PHYIN
ID CRN15_PHYIN Reviewed; 615 AA.
AC Q2M3Z8;
DT 05-JUN-2019, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2006, sequence version 1.
DT 25-MAY-2022, entry version 22.
DE RecName: Full=Crinkler effector protein 15 {ECO:0000303|PubMed:16380277};
DE Flags: Precursor;
GN Name=CRN15 {ECO:0000303|PubMed:16380277};
OS Phytophthora infestans (Potato late blight agent) (Botrytis infestans).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=4787;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Isolate 88069;
RX PubMed=16380277; DOI=10.1016/j.fgb.2005.10.003;
RA Win J., Kanneganti T.D., Torto-Alalibo T., Kamoun S.;
RT "Computational and comparative analyses of 150 full-length cDNA sequences
RT from the oomycete plant pathogen Phytophthora infestans.";
RL Fungal Genet. Biol. 43:20-33(2006).
RN [2]
RP DOMAIN, AND SUBCELLULAR LOCATION.
RX PubMed=20847293; DOI=10.1073/pnas.1008491107;
RA Schornack S., van Damme M., Bozkurt T.O., Cano L.M., Smoker M., Thines M.,
RA Gaulin E., Kamoun S., Huitema E.;
RT "Ancient class of translocated oomycete effectors targets the host
RT nucleus.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:17421-17426(2010).
CC -!- FUNCTION: Secreted effector that elicits necrosis in host plants, a
CC characteristic of plant innate immunity. {ECO:0000305|PubMed:20847293}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20847293}. Host
CC nucleus {ECO:0000269|PubMed:20847293}.
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:0000269|PubMed:20847293}.
CC -!- SIMILARITY: Belongs to the Crinkler effector family. {ECO:0000305}.
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DR EMBL; AY961463; AAY43409.1; -; mRNA.
DR AlphaFoldDB; Q2M3Z8; -.
DR VEuPathDB; FungiDB:PITG_14309; -.
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 InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF20147; Crinkler; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; Host nucleus; Secreted; Signal; Virulence.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..615
FT /note="Crinkler effector protein 15"
FT /id="PRO_0000447410"
FT REGION 18..54
FT /note="LQLFLAK domain"
FT /evidence="ECO:0000305|PubMed:20847293"
FT REGION 55..136
FT /note="DWL domain"
FT /evidence="ECO:0000305|PubMed:20847293"
FT MOTIF 137..143
FT /note="HVLVXXP motif"
FT /evidence="ECO:0000305|PubMed:20847293"
FT CARBOHYD 531
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 615 AA; 69062 MW; 133A2824D80AC3F2 CRC64;
MVKLVCAIVG VAGSAFPVDI DASQLVGDLK KAIKAENAMT FTGDAKDLQL FLAKQPVDDE
SGKEVVPVYR PSAEEMKEES FKWLPDEHRA ALKLVEGESD DYIHALTAGE PILGSKTLTT
WFYTKNNMEL PSSEQIHVLV VVPEQGSSVP TVSQDGVFDH CINPFFLQFR TVDKVGDWLE
FSSLLPLTRR QKLYIRSSYQ VIANHALFNP NVGMVKYAVV TGTPGVGKSV FVYYVLWRLI
KEKKRVLLFD NNGLFYFDGS TMLICLALPS KFNEQFWSPD LWCLVDSMDP TSIPGLPYRL
CSVLLASTPR RDCIGEFKKQ PPTADVFYMP LWSKEELATI APMYPHAAAV WENRFDCLGG
VPRLVLQDIE TDPQALLMSA CSSCSLDDCI MLVSIYSEIN SKTKIVQTLI HIHSQEPYRK
YKVVYASDLA MQLIVRTKWR FDRAKLQSLL GSSDGNPLAQ SLCGYIFEFY SMDRLEQGGT
FVYRELFSGK RKRTPADGTI DIPRSSQPRQ VAERVEVGQH AKQLYVPGTS NYTAIDAWMP
QFGGFQMTVG KTHDIKGGAA DDLAKLGQNG NRLFFLLPPL YYKTFTKKTP QTIKQYAILV
PYPEVRNELS ASTLQ