CRN8_PHYIN
ID CRN8_PHYIN Reviewed; 599 AA.
AC Q2M405;
DT 05-JUN-2019, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Crinkler effector protein 8 {ECO:0000303|PubMed:16380277};
DE EC=2.7.11.1 {ECO:0000269|PubMed:22927814};
DE Flags: Precursor;
GN Name=CRN8 {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 FUNCTION.
RX PubMed=19741609; DOI=10.1038/nature08358;
RG The Broad Institute Genome Sequencing Platform;
RA Haas B.J., Kamoun S., Zody M.C., Jiang R.H., Handsaker R.E., Cano L.M.,
RA Grabherr M., Kodira C.D., Raffaele S., Torto-Alalibo T., Bozkurt T.O.,
RA Ah-Fong A.M., Alvarado L., Anderson V.L., Armstrong M.R., Avrova A.,
RA Baxter L., Beynon J., Boevink P.C., Bollmann S.R., Bos J.I., Bulone V.,
RA Cai G., Cakir C., Carrington J.C., Chawner M., Conti L., Costanzo S.,
RA Ewan R., Fahlgren N., Fischbach M.A., Fugelstad J., Gilroy E.M., Gnerre S.,
RA Green P.J., Grenville-Briggs L.J., Griffith J., Grunwald N.J., Horn K.,
RA Horner N.R., Hu C.H., Huitema E., Jeong D.H., Jones A.M., Jones J.D.,
RA Jones R.W., Karlsson E.K., Kunjeti S.G., Lamour K., Liu Z., Ma L.,
RA Maclean D., Chibucos M.C., McDonald H., McWalters J., Meijer H.J.,
RA Morgan W., Morris P.F., Munro C.A., O'Neill K., Ospina-Giraldo M.,
RA Pinzon A., Pritchard L., Ramsahoye B., Ren Q., Restrepo S., Roy S.,
RA Sadanandom A., Savidor A., Schornack S., Schwartz D.C., Schumann U.D.,
RA Schwessinger B., Seyer L., Sharpe T., Silvar C., Song J., Studholme D.J.,
RA Sykes S., Thines M., van de Vondervoort P.J., Phuntumart V., Wawra S.,
RA Weide R., Win J., Young C., Zhou S., Fry W., Meyers B.C., van West P.,
RA Ristaino J., Govers F., Birch P.R., Whisson S.C., Judelson H.S.,
RA Nusbaum C.;
RT "Genome sequence and analysis of the Irish potato famine pathogen
RT Phytophthora infestans.";
RL Nature 461:393-398(2009).
RN [3]
RP DOMAIN, FUNCTION, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, ACTIVE SITE,
RP PHOSPHORYLATION AT SER-249; SER-281; SER-385; SER-474 AND SER-587,
RP MUTAGENESIS OF SER-249; SER-281; SER-385; ARG-469; ASP-470; SER-474 AND
RP SER-587, AND SUBUNIT.
RX PubMed=22927814; DOI=10.1371/journal.ppat.1002875;
RA van Damme M., Bozkurt T.O., Cakir C., Schornack S., Sklenar J., Jones A.M.,
RA Kamoun S.;
RT "The Irish potato famine pathogen Phytophthora infestans translocates the
RT CRN8 kinase into host plant cells.";
RL PLoS Pathog. 8:E1002875-E1002875(2012).
RN [4]
RP DOMAIN, SUBCELLULAR LOCATION, AND FUNCTION.
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 induces cell death when expressed in
CC host plants (PubMed:19741609, PubMed:22927814, PubMed:20847293). Acts
CC as a kinase and is able to autophosphorylate, however its cell death
CC inducing-abiliy is not a direct result of its kinase activity, but
CC rather a consequence of the phosphorylated state of the five identified
CC serine residues in the CRN8 protein (PubMed:22927814).
CC {ECO:0000269|PubMed:19741609, ECO:0000269|PubMed:20847293,
CC ECO:0000269|PubMed:22927814}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000269|PubMed:22927814};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000305|PubMed:16380277};
CC -!- SUBUNIT: Dimerizes in host plants. {ECO:0000269|PubMed:22927814}.
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 effector domains are fused. The
CC conserved CRN N-terminus mediates the translocation into the plant host
CC cells. {ECO:0000269|PubMed:20847293}.
CC -!- DOMAIN: The whole D2 effector domain that contains a protein functional
CC kinase domain, as well as the C-terminal NLS are required for cell
CC death induction. {ECO:0000269|PubMed:19741609,
CC ECO:0000269|PubMed:22927814}.
CC -!- PTM: Autophosphorylated at Ser-249, Ser-281, Ser-385, Ser-474 and Ser-
CC 587. Additional serines or threonines are also targeted for
CC phosphorylation. {ECO:0000269|PubMed:22927814}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the Crinkler effector
CC family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the protein kinase
CC superfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY961456; AAY43402.1; -; mRNA.
DR AlphaFoldDB; Q2M405; -.
DR SMR; Q2M405; -.
DR iPTMnet; Q2M405; -.
DR VEuPathDB; FungiDB:PITG_12094; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR InterPro; IPR045379; Crinkler_N.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR040976; Pkinase_fungal.
DR Pfam; PF20147; Crinkler; 1.
DR Pfam; PF17667; Pkinase_fungal; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Host nucleus; Kinase; Phosphoprotein; Secreted;
KW Serine/threonine-protein kinase; Signal; Transferase; Virulence.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..599
FT /note="Crinkler effector protein 8"
FT /id="PRO_0000447409"
FT DOMAIN 289..590
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000269|PubMed:22927814"
FT REGION 18..52
FT /note="LQLFLAK domain"
FT /evidence="ECO:0000305|PubMed:22927814"
FT REGION 53..109
FT /note="DWL domain"
FT /evidence="ECO:0000305|PubMed:22927814"
FT REGION 117..590
FT /note="C-terminal D2 effector domain"
FT /evidence="ECO:0000305|PubMed:22927814"
FT REGION 577..599
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 110..116
FT /note="HVLVXXP motif"
FT /evidence="ECO:0000305|PubMed:22927814"
FT MOTIF 590..599
FT /note="Host nuclear localization signal"
FT /evidence="ECO:0000269|PubMed:22927814"
FT COMPBIAS 577..591
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 470
FT /note="Proton acceptor"
FT /evidence="ECO:0000269|PubMed:22927814"
FT MOD_RES 249
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22927814"
FT MOD_RES 281
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22927814"
FT MOD_RES 385
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22927814"
FT MOD_RES 474
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22927814"
FT MOD_RES 587
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22927814"
FT CARBOHYD 23
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT MUTAGEN 249
FT /note="S->A: Impairs host cell death induction; when
FT associated with A-281, A-385, A-474 and A-587."
FT /evidence="ECO:0000269|PubMed:22927814"
FT MUTAGEN 281
FT /note="S->A: Impairs host cell death induction; when
FT associated with A-249, A-385, A-474 and A-587."
FT /evidence="ECO:0000269|PubMed:22927814"
FT MUTAGEN 385
FT /note="S->A: Impairs host cell death induction; when
FT associated with A-249, A-281, A-474 and A-587."
FT /evidence="ECO:0000269|PubMed:22927814"
FT MUTAGEN 469
FT /note="R->A: Destabilizes the CRN8 protein and impairs
FT autophosphorylation and host cell death induction; when
FT associated with A-470."
FT /evidence="ECO:0000269|PubMed:22927814"
FT MUTAGEN 470
FT /note="D->A: Destabilizes the CRN8 protein and impairs
FT autophosphorylation and host cell death induction; when
FT associated with A-469."
FT /evidence="ECO:0000269|PubMed:22927814"
FT MUTAGEN 470
FT /note="D->A: Impairs autophosphorylation but does not
FT affect host cell death induction."
FT /evidence="ECO:0000269|PubMed:22927814"
FT MUTAGEN 474
FT /note="S->A: Impairs host cell death induction; when
FT associated with A-249, A-291, A-385 and A-587."
FT /evidence="ECO:0000269|PubMed:22927814"
FT MUTAGEN 587
FT /note="S->A: Impairs host cell death induction; when
FT associated with A-249, A-291, A-385 and A-474."
FT /evidence="ECO:0000269|PubMed:22927814"
SQ SEQUENCE 599 AA; 67268 MW; 5258452242BA845E CRC64;
MVTLFCAVVG VAGSTFPVDI NENKSVGHLK KAIKEEKMYQ FPADELQLFL AKAGGNAWLS
SLTEDVKKLK KGEKTALVKS LTQEEKELQG EDPISECLEG MDPPKVKQIH VLVALPPGTS
SAPISDGTDL WLSRFQHSEV AKLTLLPTRG DLNEFIGQPL PVKIGLPQSV FQAWSSPLIL
GQLLRDKLFE LNDISPCEFL KDSVFSAAFL YPQVDGDATE SAFHYFWDSI IRVVLGFVFR
RAYVNRDSSR KSSSGLKRPD FLFALDHICV FRGEEKEPRT SITVPREELS KKLVWSYGGV
PYVFGYAASG FELELFAIYQ DVTGNVKTHL IGGFNLQHAP ERFRLVLALL NLCLLFPAIV
QNCPASAGTE FMDIHRANGV KVRLSPIFVD KIFHTQEEYR RVKQIYDSLK AYGVPCADAV
VTVDSDQLRL TLKPRGIEMK PCSLSELFVA LGNVLEALVV LHRNGWMHRD IRWSNVIKHI
DRVEWFLIDF ADAAQSPQKY PSGDHLTHDE HASDIFMEGG SHTTAVDLWA VGYLVKTSKI
EREWTAEPER ALFLDRLMNP DPSARPTADE ALQLLSRFER EAAEQESQGK GVRKKHRRA
