ID   CRN1_PHYIN              Reviewed;         431 AA.
AC   Q8H6Z6;
DT   05-JUN-2019, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 35.
DE   RecName: Full=Crinkler effector protein 1 {ECO:0000303|PubMed:12840044};
DE   Flags: Precursor;
GN   Name=CRN1 {ECO:0000303|PubMed:12840044};
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], INDUCTION, AND FUNCTION.
RC   STRAIN=DDR7602;
RX   PubMed=12840044; DOI=10.1101/gr.910003;
RA   Torto T.A., Li S., Styer A., Huitema E., Testa A., Gow N.A., van West P.,
RA   Kamoun S.;
RT   "EST mining and functional expression assays identify extracellular
RT   effector proteins from the plant pathogen Phytophthora.";
RL   Genome Res. 13:1675-1685(2003).
CC   -!- FUNCTION: Secreted effector that elicits necrosis in host plants, a
CC       characteristic of plant innate immunity. {ECO:0000305|PubMed:12840044}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12840044}. Host cell
CC       {ECO:0000269|PubMed:12840044}.
CC   -!- INDUCTION: Expressed during colonization of tomato leaves by
CC       P.infestans. {ECO:0000269|PubMed:12840044}.
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:12840044}.
CC   -!- SIMILARITY: Belongs to the Crinkler effector family. {ECO:0000305}.
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DR   EMBL; AF424675; AAN31500.1; -; mRNA.
DR   AlphaFoldDB; Q8H6Z6; -.
DR   VEuPathDB; FungiDB:PITG_12641; -.
DR   PHI-base; PHI:656; -.
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   2: Evidence at transcript level;
KW   Glycoprotein; Secreted; Signal; Virulence.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..431
FT                   /note="Crinkler effector protein 1"
FT                   /id="PRO_0000447425"
FT   REGION          18..54
FT                   /note="LQLFLAK domain"
FT                   /evidence="ECO:0000305|PubMed:12840044"
FT   REGION          55..113
FT                   /note="DWL domain"
FT                   /evidence="ECO:0000305|PubMed:12840044"
FT   MOTIF           114..121
FT                   /note="HVLVXXP motif"
FT                   /evidence="ECO:0000305|PubMed:12840044"
FT   CARBOHYD        23
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        37
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        265
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   431 AA;  47907 MW;  F3FE7AE2E54B33C7 CRC64;
     MVTLYCVVVG VAGSAFPVDI DENKSVGHLK DAIKEKNAST ITCDAKNLQL FLAKKKKGAG
     VRLTENDVKD GVSDTSDLKL LGVAGAPLSL VGLSEKDVKF VPTLEDVESM NTPVHVLVVV
     PEQDGTISKE MSAATSPLTV EQVEMSMNKV LRERDEKASA YSFSDLNTAM EERIVKKMRL
     TENIPDVKEP VDTSIAGYSW IPKIVESEES QRAGYMEYLQ QHLKTLIDRG DFLLDDIAGD
     KSVLNIVDPR LPFAMKGTAD VLLINRTAKN PLIKLAGVSL VIELKKKVEP GHVPQAIGQL
     VSCSMKAPLN CYPLSLLTDL NDHWHFSWFS DKHVLTQVTL KYPKNAFRFI EAAVLGRTDS
     APPPPSFMPG SFKTIKVDDF LPQPVDARAE EMMERYELMA DVVEPEFLMA RRMDYARQLV
     QSMPMYSYMY T