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PAT1H_ARATH
ID   PAT1H_ARATH             Reviewed;         793 AA.
AC   Q0WPK4; O64542; Q56X08;
DT   31-JAN-2018, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   25-MAY-2022, entry version 111.
DE   RecName: Full=Protein PAT1 homolog {ECO:0000305};
DE            Short=AtPAT1 {ECO:0000303|PubMed:25603932};
GN   Name=PAT1 {ECO:0000303|PubMed:25603932};
GN   OrderedLocusNames=At1g79090 {ECO:0000312|Araport:AT1G79090};
GN   ORFNames=YUP8H12R.29 {ECO:0000312|EMBL:AAC17049.1};
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA   Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA   Shinozaki K.;
RT   "Analysis of multiple occurrences of alternative splicing events in
RT   Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL   DNA Res. 16:155-164(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=cv. Columbia;
RX   PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA   Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA   Rathjen J.P., Peck S.C.;
RT   "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT   thaliana.";
RL   J. Proteomics 72:439-451(2009).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-208, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19376835; DOI=10.1104/pp.109.138677;
RA   Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA   Grossmann J., Gruissem W., Baginsky S.;
RT   "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT   chloroplast kinase substrates and phosphorylation networks.";
RL   Plant Physiol. 150:889-903(2009).
RN   [7]
RP   FUNCTION, INTERACTION WITH MPK4 AND SUMM2, SUBCELLULAR LOCATION, INDUCTION
RP   BY FLAGELLIN, PHOSPHORYLATION AT SER-200; SER-208; SER-342 AND SER-343,
RP   MUTAGENESIS OF SER-208, AND DISRUPTION PHENOTYPE.
RX   PubMed=25603932; DOI=10.15252/embj.201488645;
RA   Roux M.E., Rasmussen M.W., Palma K., Lolle S., Regue A.M., Bethke G.,
RA   Glazebrook J., Zhang W., Sieburth L., Larsen M.R., Mundy J., Petersen M.;
RT   "The mRNA decay factor PAT1 functions in a pathway including MAP kinase 4
RT   and immune receptor SUMM2.";
RL   EMBO J. 34:593-608(2015).
CC   -!- FUNCTION: Activator of mRNA decapping. Involved in mRNA decay via
CC       decapping. Involved in disease resistance in response to biotrophic and
CC       necrotrophic pathogens. Is part of a signaling pathway including MPK4
CC       and the disease resistance protein SUMM2.
CC       {ECO:0000269|PubMed:25603932}.
CC   -!- SUBUNIT: Interacts with MPK4 and SUMM2. {ECO:0000269|PubMed:25603932}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000269|PubMed:25603932}.
CC   -!- INDUCTION: Accumulates in response to flg22 (at protein levels).
CC       {ECO:0000269|PubMed:25603932}.
CC   -!- PTM: Phosphorylated at Ser-208 by MPK4 upon flg22 elicitation.
CC       Phosphorylated at Ser-200, Ser-342 and Ser-343 upon flg22 elicitation.
CC       {ECO:0000269|PubMed:25603932}.
CC   -!- DISRUPTION PHENOTYPE: Serrated leaf and reduced plant size.
CC       Constitutive expression of the defense-related gene PR1 and enhanced
CC       resistance to the bacterial pathogen Pseudomonas syringae pv tomato
CC       strain DC3000. {ECO:0000269|PubMed:25603932}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC17049.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AC002986; AAC17049.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; AEE36202.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE36203.1; -; Genomic_DNA.
DR   EMBL; CP002684; ANM57835.1; -; Genomic_DNA.
DR   EMBL; AK318693; BAH56808.1; -; mRNA.
DR   EMBL; AK229063; BAF00945.1; -; mRNA.
DR   EMBL; AK221871; BAD94175.1; -; mRNA.
DR   PIR; T01046; T01046.
DR   RefSeq; NP_001320315.1; NM_001334869.1.
DR   RefSeq; NP_565199.1; NM_106560.4.
DR   RefSeq; NP_849904.1; NM_179573.4.
DR   AlphaFoldDB; Q0WPK4; -.
DR   ComplexPortal; CPX-1308; LSM1-7-PAT1 complex, variant LSM1A-LSM3A-LSM6A-PAT1.
DR   ComplexPortal; CPX-1345; LSM1-7-PAT1 complex, variant LSM1A-LSM3B-LSM6B-PAT1.
DR   ComplexPortal; CPX-1346; LSM1-7-PAT1 complex, variant LSM1A-LSM3B-LSM6A-PAT1.
DR   ComplexPortal; CPX-1347; LSM1-7-PAT1 complex, variant LSM1B-LSM3A-LSM6A-PAT1.
DR   ComplexPortal; CPX-1348; LSM1-7-PAT1 complex, variant LSM1B-LSM3B-LSM6A-PAT1.
DR   ComplexPortal; CPX-1349; LSM1-7-PAT1 complex, variant LSM1B-LSM3B-LSM6B-PAT1.
DR   ComplexPortal; CPX-1350; LSM1-7-PAT1 complex, variant LSM1B-LSM3A-LSM6B-PAT1.
DR   ComplexPortal; CPX-1351; LSM1-7-PAT1 complex, variant LSM1A-LSM3A-LSM6B-PAT1.
DR   STRING; 3702.AT1G79090.2; -.
DR   iPTMnet; Q0WPK4; -.
DR   PaxDb; Q0WPK4; -.
DR   PRIDE; Q0WPK4; -.
DR   ProteomicsDB; 236325; -.
DR   EnsemblPlants; AT1G79090.1; AT1G79090.1; AT1G79090.
DR   EnsemblPlants; AT1G79090.2; AT1G79090.2; AT1G79090.
DR   EnsemblPlants; AT1G79090.3; AT1G79090.3; AT1G79090.
DR   GeneID; 844250; -.
DR   Gramene; AT1G79090.1; AT1G79090.1; AT1G79090.
DR   Gramene; AT1G79090.2; AT1G79090.2; AT1G79090.
DR   Gramene; AT1G79090.3; AT1G79090.3; AT1G79090.
DR   KEGG; ath:AT1G79090; -.
DR   Araport; AT1G79090; -.
DR   TAIR; locus:2207400; AT1G79090.
DR   eggNOG; ENOG502QQ60; Eukaryota.
DR   HOGENOM; CLU_021130_0_0_1; -.
DR   InParanoid; Q0WPK4; -.
DR   OMA; QHSSQMM; -.
DR   OrthoDB; 369950at2759; -.
DR   PhylomeDB; Q0WPK4; -.
DR   PRO; PR:Q0WPK4; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q0WPK4; baseline and differential.
DR   GO; GO:1990726; C:Lsm1-7-Pat1 complex; IC:ComplexPortal.
DR   GO; GO:0000932; C:P-body; IDA:TAIR.
DR   GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0000290; P:deadenylation-dependent decapping of nuclear-transcribed mRNA; IMP:TAIR.
DR   GO; GO:0045087; P:innate immune response; IMP:TAIR.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0033962; P:P-body assembly; IBA:GO_Central.
DR   InterPro; IPR039900; Pat1-like.
DR   PANTHER; PTHR21551; PTHR21551; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; mRNA processing; Phosphoprotein; Plant defense;
KW   Reference proteome.
FT   CHAIN           1..793
FT                   /note="Protein PAT1 homolog"
FT                   /id="PRO_0000442788"
FT   REGION          203..256
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          291..312
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          476..501
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        222..256
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         200
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:25603932"
FT   MOD_RES         208
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:25603932,
FT                   ECO:0007744|PubMed:19376835"
FT   MOD_RES         342
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:25603932"
FT   MOD_RES         343
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:25603932"
FT   MUTAGEN         208
FT                   /note="S->A: Abolishes phosphorylation by MPK4."
FT                   /evidence="ECO:0000269|PubMed:25603932"
FT   CONFLICT        527
FT                   /note="D -> E (in Ref. 4; BAD94175)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        711
FT                   /note="N -> K (in Ref. 4; BAD94175)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   793 AA;  88840 MW;  8C70A4DFD7A9EA6E CRC64;
     MDAFGIGSSL NQAPVTQDLK KFGDNSTGNT MFDASQYAFF GNDVVEEVEL GGLEEEDEIL
     SFTGIAEDFS FDKEEVGDSR LLSDVDDLAS TFSKLNREPD VYSNTGPITD RRSSQNSLAA
     EWTHGEELPN WYGRQILDSD AIKDDKVWSA QPFSSLDRVE QRIPDRTKLY PEPQRQLHQD
     HNQQQFSSEP ILVPKSSFVS YPPPGSISPD QRLGHPNIPY QSGGPQMGSP NFSPFPNLQP
     QLPSMHHGSP QHTGNRPQFR PALPLNNLPP AQWMNRQNMH PGDSSGIMNN AMLQQPPHQN
     GLMPPQMQGS QNRLPHPMQP PLGHMPGMQP QLFNSHLSRS SSSGNYDGML GFGDLREVRP
     GSGHGNRQNV RFPQQGFDAG VQRRYPFRSK YMSAGEIENI LRMQLVATHS NDPYVDDYYH
     QACLAKKSAG AKLKHHFCPN HLRDLQQRAR SNNEPHAFLQ VEALGRVPFS SIRRPRPLLE
     VDPPNSAKFG NAEHKPTDKP LDQEPMLAAR VYIEDGLCLL LEVDDIDRFL EFNQLQDGGH
     QLKQRRQALL QSLAVSLQLG DPLAKNGQSQ SLDDFLFLRV ISLPKGRKLL IRYLQLIFPG
     SDLMRIVCMA IFRHLRSLFG VLSSDPDIIK TTNKLATVIN LCIQNMELGP VSTCLAAVSC
     SSEQAPLRPL GSPVGDGAST VLKSILDRAS ELIRANNFNN AGIALWRASF NEFFNMLMRY
     CISKYDSIMQ SLQLPPHFAT EISEEAAKAI VREMPIELLR SSFPHIDEQQ KRILMEFLKR
     SMLGSQKTEP VLS
 
 
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