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RXL17_HYAAE
ID   RXL17_HYAAE             Reviewed;         305 AA.
AC   M4BMH6; G3C9N5;
DT   16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2013, sequence version 1.
DT   25-MAY-2022, entry version 15.
DE   RecName: Full=RxLR effector protein 17 {ECO:0000303|PubMed:22072967};
DE   Flags: Precursor;
GN   Name=RxL17 {ECO:0000303|PubMed:22072967};
OS   Hyaloperonospora arabidopsidis (strain Emoy2) (Downy mildew agent)
OS   (Peronospora arabidopsidis).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Hyaloperonospora.
OX   NCBI_TaxID=559515;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 25-305, AND FUNCTION.
RC   STRAIN=Emoy2;
RX   PubMed=22072967; DOI=10.1371/journal.ppat.1002348;
RA   Fabro G., Steinbrenner J., Coates M., Ishaque N., Baxter L.,
RA   Studholme D.J., Koerner E., Allen R.L., Piquerez S.J., Rougon-Cardoso A.,
RA   Greenshields D., Lei R., Badel J.L., Caillaud M.C., Sohn K.H.,
RA   Van den Ackerveken G., Parker J.E., Beynon J., Jones J.D.;
RT   "Multiple candidate effectors from the oomycete pathogen Hyaloperonospora
RT   arabidopsidis suppress host plant immunity.";
RL   PLoS Pathog. 7:E1002348-E1002348(2011).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Emoy2;
RX   PubMed=21148394; DOI=10.1126/science.1195203;
RA   Baxter L., Tripathy S., Ishaque N., Boot N., Cabral A., Kemen E.,
RA   Thines M., Ah-Fong A., Anderson R., Badejoko W., Bittner-Eddy P.,
RA   Boore J.L., Chibucos M.C., Coates M., Dehal P., Delehaunty K., Dong S.,
RA   Downton P., Dumas B., Fabro G., Fronick C., Fuerstenberg S.I., Fulton L.,
RA   Gaulin E., Govers F., Hughes L., Humphray S., Jiang R.H., Judelson H.,
RA   Kamoun S., Kyung K., Meijer H., Minx P., Morris P., Nelson J.,
RA   Phuntumart V., Qutob D., Rehmany A., Rougon-Cardoso A., Ryden P.,
RA   Torto-Alalibo T., Studholme D., Wang Y., Win J., Wood J., Clifton S.W.,
RA   Rogers J., Van den Ackerveken G., Jones J.D., McDowell J.M., Beynon J.,
RA   Tyler B.M.;
RT   "Signatures of adaptation to obligate biotrophy in the Hyaloperonospora
RT   arabidopsidis genome.";
RL   Science 330:1549-1551(2010).
RN   [3]
RP   IDENTIFICATION.
RC   STRAIN=Emoy2;
RG   EnsemblProtists;
RL   Submitted (JUN-2015) to UniProtKB.
RN   [4]
RP   INTERACTION WITH HOST AT1G14340.
RX   PubMed=21798943; DOI=10.1126/science.1203659;
RG   European Union Effectoromics Consortium;
RA   Mukhtar M.S., Carvunis A.-R., Dreze M., Epple P., Steinbrenner J.,
RA   Moore J., Tasan M., Galli M., Hao T., Nishimura M.T., Pevzner S.J.,
RA   Donovan S.E., Ghamsari L., Santhanam B., Romero V., Poulin M.M.,
RA   Gebreab F., Gutierrez B.J., Tam S., Monachello D., Boxem M., Harbort C.J.,
RA   McDonald N., Gai L., Chen H., He Y., Vandenhaute J., Roth F.P., Hill D.E.,
RA   Ecker J.R., Vidal M., Beynon J., Braun P., Dangl J.L.;
RT   "Independently evolved virulence effectors converge onto hubs in a plant
RT   immune system network.";
RL   Science 333:596-601(2011).
RN   [5]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=21914011; DOI=10.1111/j.1365-313x.2011.04787.x;
RA   Caillaud M.C., Piquerez S.J., Fabro G., Steinbrenner J., Ishaque N.,
RA   Beynon J., Jones J.D.;
RT   "Subcellular localization of the Hpa RxLR effector repertoire identifies a
RT   tonoplast-associated protein HaRxL17 that confers enhanced plant
RT   susceptibility.";
RL   Plant J. 69:252-265(2012).
RN   [6]
RP   SUBCELLULAR LOCATION, FUNCTION, AND DOMAIN.
RX   PubMed=22301983; DOI=10.4161/psb.7.1.18450;
RA   Caillaud M.C., Piquerez S.J., Jones J.D.;
RT   "Characterization of the membrane-associated HaRxL17 Hpa effector
RT   candidate.";
RL   Plant Signal. Behav. 7:145-149(2012).
CC   -!- FUNCTION: Secreted effector that confers enhanced plant susceptibility
CC       during both compatible and incompatible interactions between the
CC       pathogen and its host (PubMed:22072967, PubMed:21914011). Promotes the
CC       sexual reproduction of the pathogen in the plant host
CC       (PubMed:21914011). {ECO:0000269|PubMed:21914011,
CC       ECO:0000269|PubMed:22072967}.
CC   -!- SUBUNIT: Interacts with host A.thaliana At1G14340.
CC       {ECO:0000269|PubMed:22301983}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21914011,
CC       ECO:0000269|PubMed:22301983}. Host cell membrane
CC       {ECO:0000269|PubMed:21914011, ECO:0000269|PubMed:22301983}.
CC       Note=Localizes to the membrane around haustoria also called
CC       extrahaustorial membrane (EHM) at early and late stages of infection.
CC       {ECO:0000269|PubMed:21914011, ECO:0000269|PubMed:22301983}.
CC   -!- DOMAIN: The RxLR-dEER motif is required for the delivery of the
CC       effector to the host cell cytoplasm but does not bind
CC       phosphatidylinositol monophosphates. {ECO:0000305|PubMed:22072967}.
CC   -!- DOMAIN: The C-terminal region (residues 247 to 269) consists of one W
CC       motif, a conserved motif found in already well characterized effectors
CC       that may be involved in the interaction with host proteins.
CC       {ECO:0000305|PubMed:22301983}.
CC   -!- SIMILARITY: Belongs to the RxLR effector family. {ECO:0000305}.
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DR   EMBL; HE574733; CCC55811.1; -; mRNA.
DR   EMBL; JH598420; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; M4BMH6; -.
DR   EnsemblProtists; HpaT807613; HpaP807613; HpaG807613.
DR   VEuPathDB; FungiDB:HpaG807613; -.
DR   HOGENOM; CLU_913523_0_0_1; -.
DR   PHI-base; PHI:4847; -.
DR   PHI-base; PHI:4852; -.
DR   Proteomes; UP000011713; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Glycoprotein; Host cell membrane; Host membrane; Membrane;
KW   Reference proteome; Secreted; Signal; Virulence.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..305
FT                   /note="RxLR effector protein 17"
FT                   /id="PRO_5004049285"
FT   REGION          247..269
FT                   /note="W motif"
FT                   /evidence="ECO:0000305|PubMed:22301983"
FT   MOTIF           45..60
FT                   /note="RxLR-dEER"
FT                   /evidence="ECO:0000305|PubMed:22072967"
FT   CARBOHYD        207
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        227
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   305 AA;  33946 MW;  20CCECFB230CEA48 CRC64;
     MQSILWFALI ASVVFLVLVD LASGLNGLET LSSGADVDEL TTATRLLRAA HLDRKLSEER
     AFISGESIGS WWTKVTEWLR VKFELIIAYI KQLRVKSNDV KDDAATNDAA HAKDDAAANK
     AARAKDDASR ATYEAARANY EAARAYDDAT RAQDVAALEA ARAIEATDIA AYTGANAEYE
     QSMFLNGFVK TIDLHNEKNA PIMTRLNKSL DEAKKSSTFR EIADGVNESK VALVVHEKQD
     GYLLWILHLK WAVEAKSPKD VVERILKDLG THDVPHLQER AEQVKKAYTI FLLYVERMSR
     ATHPK
 
 
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