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AVH52_PHYSP
ID   AVH52_PHYSP             Reviewed;         122 AA.
AC   G4ZSG0;
DT   08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT   25-JAN-2012, sequence version 1.
DT   25-MAY-2022, entry version 26.
DE   RecName: Full=RxLR effector protein Avh52 {ECO:0000303|PubMed:21653195};
DE   AltName: Full=Avirulence homolog protein 52 {ECO:0000303|PubMed:21653195};
DE   Flags: Precursor;
GN   Name=Avh52 {ECO:0000303|PubMed:21653195}; ORFNames=PHYSODRAFT_355041;
OS   Phytophthora sojae (strain P6497) (Soybean stem and root rot agent)
OS   (Phytophthora megasperma f. sp. glycines).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=1094619;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P6497;
RX   PubMed=16946064; DOI=10.1126/science.1128796;
RA   Tyler B.M., Tripathy S., Zhang X., Dehal P., Jiang R.H.Y., Aerts A.,
RA   Arredondo F.D., Baxter L., Bensasson D., Beynon J.L., Chapman J.,
RA   Damasceno C.M.B., Dorrance A.E., Dou D., Dickerman A.W., Dubchak I.L.,
RA   Garbelotto M., Gijzen M., Gordon S.G., Govers F., Grunwald N.J., Huang W.,
RA   Ivors K.L., Jones R.W., Kamoun S., Krampis K., Lamour K.H., Lee M.-K.,
RA   McDonald W.H., Medina M., Meijer H.J.G., Nordberg E.K., Maclean D.J.,
RA   Ospina-Giraldo M.D., Morris P.F., Phuntumart V., Putnam N.H., Rash S.,
RA   Rose J.K.C., Sakihama Y., Salamov A.A., Savidor A., Scheuring C.F.,
RA   Smith B.M., Sobral B.W.S., Terry A., Torto-Alalibo T.A., Win J., Xu Z.,
RA   Zhang H., Grigoriev I.V., Rokhsar D.S., Boore J.L.;
RT   "Phytophthora genome sequences uncover evolutionary origins and mechanisms
RT   of pathogenesis.";
RL   Science 313:1261-1266(2006).
RN   [2]
RP   IDENTIFICATION, FUNCTION, AND DOMAIN.
RX   PubMed=21653195; DOI=10.1105/tpc.111.086082;
RA   Wang Q., Han C., Ferreira A.O., Yu X., Ye W., Tripathy S., Kale S.D.,
RA   Gu B., Sheng Y., Sui Y., Wang X., Zhang Z., Cheng B., Dong S., Shan W.,
RA   Zheng X., Dou D., Tyler B.M., Wang Y.;
RT   "Transcriptional programming and functional interactions within the
RT   Phytophthora sojae RXLR effector repertoire.";
RL   Plant Cell 23:2064-2086(2011).
RN   [3]
RP   FUNCTION.
RX   PubMed=26163574; DOI=10.1105/tpc.15.00390;
RA   Ma Z., Song T., Zhu L., Ye W., Wang Y., Shao Y., Dong S., Zhang Z., Dou D.,
RA   Zheng X., Tyler B.M., Wang Y.;
RT   "A Phytophthora sojae glycoside hydrolase 12 protein is a major virulence
RT   factor during soybean infection and is recognized as a PAMP.";
RL   Plant Cell 27:2057-2072(2015).
RN   [4]
RP   FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH HOST TAP1, SUBCELLULAR
RP   LOCATION, DOMAIN, AND MUTAGENESIS OF 69-SER--VAL-86; LYS-87; LYS-88;
RP   LYS-91; LYS-95; LYS-97 AND LYS-98.
RX   PubMed=30346270; DOI=10.7554/elife.40039;
RA   Li H., Wang H., Jing M., Zhu J., Guo B., Wang Y., Lin Y., Chen H., Kong L.,
RA   Ma Z., Wang Y., Ye W., Dong S., Tyler B., Wang Y.;
RT   "A Phytophthora effector recruits a host cytoplasmic transacetylase into
RT   nuclear speckles to enhance plant susceptibility.";
RL   Elife 7:0-0(2018).
CC   -!- FUNCTION: Effector that suppresses plant defense responses during the
CC       early stages of pathogen infection (PubMed:21653195, PubMed:26163574,
CC       PubMed:30346270). Suppresses cell death induced by effectors and PAMPs
CC       in plant hosts (PubMed:26163574, PubMed:30346270). Interacts with host
CC       acetyltransferase TAP1 and causes TAP1 relocation into the nucleus
CC       where it acetylates histones H2A and H3 during early infection, thereby
CC       promoting susceptibility of host plant to P.sojae (PubMed:30346270).
CC       {ECO:0000269|PubMed:21653195, ECO:0000269|PubMed:26163574,
CC       ECO:0000269|PubMed:30346270}.
CC   -!- SUBUNIT: Interacts with host acetyl transferase TAP1.
CC       {ECO:0000269|PubMed:30346270}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:30346270}. Host
CC       nucleus {ECO:0000269|PubMed:30346270}.
CC   -!- DOMAIN: The RxLR-dEER motif acts to carry the protein into the host
CC       cell cytoplasm through binding to cell surface phosphatidylinositol-3-
CC       phosphate. {ECO:0000305|PubMed:21653195}.
CC   -!- DOMAIN: Residues 69 to 86 are required for the interaction with host
CC       TAP1 and its re-localization into nuclear speckles.
CC       {ECO:0000269|PubMed:30346270}.
CC   -!- DOMAIN: The nuclear localization signal (NLS) is required for
CC       localization into nucleus. {ECO:0000269|PubMed:30346270}.
CC   -!- DISRUPTION PHENOTYPE: Leads to smaller lesions on soybean seedlings.
CC       {ECO:0000269|PubMed:30346270}.
CC   -!- SIMILARITY: Belongs to the RxLR effector family. {ECO:0000305}.
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DR   EMBL; JH159156; EGZ14040.1; -; Genomic_DNA.
DR   RefSeq; XP_009531469.1; XM_009533174.1.
DR   AlphaFoldDB; G4ZSG0; -.
DR   EnsemblProtists; EGZ14040; EGZ14040; PHYSODRAFT_355041.
DR   GeneID; 20649783; -.
DR   KEGG; psoj:PHYSODRAFT_355041; -.
DR   InParanoid; G4ZSG0; -.
DR   OMA; LAWAMKE; -.
DR   Proteomes; UP000002640; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   InterPro; IPR031825; RXLR.
DR   Pfam; PF16810; RXLR; 1.
PE   1: Evidence at protein level;
KW   Host nucleus; Reference proteome; Secreted; Signal; Virulence.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..122
FT                   /note="RxLR effector protein Avh52"
FT                   /id="PRO_5003472523"
FT   REGION          69..86
FT                   /note="TAP1-binding"
FT                   /evidence="ECO:0000269|PubMed:30346270"
FT   REGION          87..98
FT                   /note="Nuclear localization signal (NLS)"
FT                   /evidence="ECO:0000269|PubMed:30346270"
FT   MOTIF           50..68
FT                   /note="RxLR-dEER"
FT                   /evidence="ECO:0000305|PubMed:30346270"
FT   MUTAGEN         69..86
FT                   /note="Missing: Impairs the interaction with host TAP1 and
FT                   does not cause re-localization of TAP1 into nuclear
FT                   speckles."
FT                   /evidence="ECO:0000269|PubMed:30346270"
FT   MUTAGEN         87
FT                   /note="K->A: Impairs host nuclear localization; when
FT                   associated with A-88, A-91, A-95, A-97 and A-98."
FT                   /evidence="ECO:0000269|PubMed:30346270"
FT   MUTAGEN         88
FT                   /note="K->A: Impairs host nuclear localization; when
FT                   associated with A-87, A-91, A-95, A-97 and A-98."
FT                   /evidence="ECO:0000269|PubMed:30346270"
FT   MUTAGEN         91
FT                   /note="K->A: Impairs host nuclear localization; when
FT                   associated with A-87, A-88, A-95, A-97 and A-98."
FT                   /evidence="ECO:0000269|PubMed:30346270"
FT   MUTAGEN         95
FT                   /note="K->A: Impairs host nuclear localization; when
FT                   associated with A-87, A-88, A-91, A-97 and A-98."
FT                   /evidence="ECO:0000269|PubMed:30346270"
FT   MUTAGEN         97
FT                   /note="K->A: Impairs host nuclear localization; when
FT                   associated with A-87, A-88, A-91, A-95 and A-98."
FT                   /evidence="ECO:0000269|PubMed:30346270"
FT   MUTAGEN         98
FT                   /note="K->A: Impairs host nuclear localization; when
FT                   associated with A-87, A-88, A-91, A-95 and A-97."
FT                   /evidence="ECO:0000269|PubMed:30346270"
SQ   SEQUENCE   122 AA;  13484 MW;  C58D461962991D83 CRC64;
     MRLTSILVLV IAATFHTTGT ALTLTKDSKA GIANGDSPAS GDFIDANSAR LLRRVEKDKV
     DYEQDEQRSF GALKDAVKKL NPVTAVKKFF KQRAKRKKVI QTARDADNNL AWAMKEVYKA
     AN
 
 
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