CRN16_PHYIN
ID CRN16_PHYIN Reviewed; 618 AA.
AC Q2M3Z7;
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 16 {ECO:0000303|PubMed:16380277};
DE Flags: Precursor;
GN Name=CRN16 {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; AY961464; AAY43410.1; -; mRNA.
DR AlphaFoldDB; Q2M3Z7; -.
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..19
FT /evidence="ECO:0000255"
FT CHAIN 20..618
FT /note="Crinkler effector protein 16"
FT /id="PRO_0000447411"
FT REGION 18..57
FT /note="LQLFLAK domain"
FT /evidence="ECO:0000305|PubMed:20847293"
FT REGION 58..139
FT /note="DWL domain"
FT /evidence="ECO:0000305|PubMed:20847293"
FT MOTIF 140..146
FT /note="HVLVXXP motif"
FT /evidence="ECO:0000305|PubMed:20847293"
FT CARBOHYD 534
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 618 AA; 69388 MW; 644983AC568CEECA CRC64;
MVVVSLQCAI VGQAGSSFDV EIDDGAKVSK LKDAIKAKKP NDFKVVDADK LHLFLAKQPV
EDESGKEVVP VYRPSAEEMK EENLKWLPDE HRAALKLVEG ESDDYIHALT AGEPILGSKT
LTTWFYTKNN MELPSSEQIH VLVVVPEQGF SVPTVSQDGV FDHCINPFFL QFRTVDKVGD
WLEFSSLLPL TRRQKLYIRS SYQVIANHAL FNPNVGMVKY AVVTGTPGVG KSVFVYYVLW
RLIKEKKRVL LFDNNGLFYF DGSTMLICLA LPSKFNEQFW SPDLWCLVDS MDPTSIPGLP
YRLCSVLLAS TPRRDCIGEF KKQPPTADVF YMPLWSKEEL ATIAPMYPHA AAVWENRFDC
LGGVPRLVLQ DIGTNPQALL MSACSSCSLD DCIVLASIHS GVNSKTTIVQ TLIHIRSQEP
YREYKVVYAS DLAMQLIVRT KWQHDRAKLQ SLLGSSDGNP LAQSLCGYIF EFYSMDRLEQ
GGTFVYRELF SKKRKRTPAD GTIDIPRSSQ PRQVAERVEV GQHAKQLYVP GTSNYTAIDA
WMPQFGGFQM TVGKTHDIKG GAADDLAKLG QNGNRLFFLL PPLYYKTFTK KTPQTIKQYA
ILVPYPEVRN ELSASTLQ