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Universal stress protein PHOS32 (Phosphorylated protein of 32 kDa) (AtPHOS32)

 PHO32_ARATH             Reviewed;         242 AA.
Q8VYN9; Q9LSR2;
08-JUN-2016, integrated into UniProtKB/Swiss-Prot.
01-MAR-2002, sequence version 1.
23-MAY-2018, entry version 115.
RecName: Full=Universal stress protein PHOS32 {ECO:0000303|PubMed:12644671};
AltName: Full=Phosphorylated protein of 32 kDa {ECO:0000303|PubMed:18285339};
Short=AtPHOS32 {ECO:0000303|PubMed:18285339};
Flags: Precursor;
Name=PHOS32 {ECO:0000303|PubMed:18285339};
OrderedLocusNames=At5g54430 {ECO:0000312|Araport:AT5G54430};
ORFNames=F24B18.5 {ECO:0000312|EMBL:BAA97516.1};
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702 {ECO:0000312|EMBL:AAL49890.1};
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
Tabata S.;
"Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
[2]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=11910074; DOI=10.1126/science.1071006;
Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M.,
Hayashizaki Y., Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T.,
Shibata K., Shinagawa A., Shinozaki K.;
"Functional annotation of a full-length Arabidopsis cDNA collection.";
Science 296:141-145(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[6]
IDENTIFICATION.
PubMed=12644671; DOI=10.1104/pp.102.016006;
Kerk D., Bulgrien J., Smith D.W., Gribskov M.;
"Arabidopsis proteins containing similarity to the universal stress
protein domain of bacteria.";
Plant Physiol. 131:1209-1219(2003).
[7]
MUTAGENESIS OF SER-21, PHOSPHORYLATION UPON BACTERIAL ELICITATION,
PHOSPHORYLATION AT SER-21 BY MAPK3 AND MAPK6, AND NICKEL-BINDING.
STRAIN=cv. Columbia, and cv. Landsberg erecta;
PubMed=18285339; DOI=10.1074/jbc.M800735200;
Merkouropoulos G., Andreasson E., Hess D., Boller T., Peck S.C.;
"An Arabidopsis protein phosphorylated in response to microbial
elicitation, AtPHOS32, is a substrate of MAP kinases 3 and 6.";
J. Biol. Chem. 283:10493-10499(2008).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21 AND SER-219, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Root;
PubMed=18433157; DOI=10.1021/pr8000173;
de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,
Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C.,
Lorkovic Z.J., Barta A., Lecourieux D., Verhounig A., Jonak C.,
Hirt H.;
"Site-specific phosphorylation profiling of Arabidopsis proteins by
mass spectrometry and peptide chip analysis.";
J. Proteome Res. 7:2458-2470(2008).
[9]
PHOSPHORYLATION UPON INFECTION BY PHYTOPHTHORA INFESTANS ZOOSPORES AND
XYLANASE, AND PHOSPHORYLATION AT SER-21.
STRAIN=cv. Landsberg erecta;
PubMed=18785823; DOI=10.1094/MPMI-21-10-1275;
Lenman M., Soerensson C., Andreasson E.;
"Enrichment of phosphoproteins and phosphopeptide derivatization
identify universal stress proteins in elicitor-treated Arabidopsis.";
Mol. Plant Microbe Interact. 21:1275-1284(2008).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19376835; DOI=10.1104/pp.109.138677;
Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
Grossmann J., Gruissem W., Baginsky S.;
"Large-scale Arabidopsis phosphoproteome profiling reveals novel
chloroplast kinase substrates and phosphorylation networks.";
Plant Physiol. 150:889-903(2009).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
-!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
-!- PTM: Phosphorylated by MAPK3 and MAPK6 after pathogenic
elicitation (e.g. bacterial flg22, Phytophthora infestans
zoospores and xylanase). {ECO:0000269|PubMed:18285339,
ECO:0000269|PubMed:18785823}.
-!- MISCELLANEOUS: Can bind nickel. {ECO:0000269|PubMed:18285339}.
-!- SIMILARITY: Belongs to the universal stress protein A family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA97516.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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EMBL; AB026634; BAA97516.1; ALT_SEQ; Genomic_DNA.
EMBL; CP002688; AED96495.1; -; Genomic_DNA.
EMBL; CP002688; ANM70952.1; -; Genomic_DNA.
EMBL; AK118526; BAC43129.1; -; mRNA.
EMBL; AY070394; AAL49890.1; -; mRNA.
EMBL; AY123025; AAM67558.1; -; mRNA.
EMBL; AY087680; AAM65217.1; -; mRNA.
RefSeq; NP_001332519.1; NM_001345084.1.
RefSeq; NP_001332520.1; NM_001345085.1.
RefSeq; NP_001332521.1; NM_001345082.1.
RefSeq; NP_568808.1; NM_124823.4.
UniGene; At.28615; -.
ProteinModelPortal; Q8VYN9; -.
SMR; Q8VYN9; -.
STRING; 3702.AT5G54430.1; -.
iPTMnet; Q8VYN9; -.
PaxDb; Q8VYN9; -.
PRIDE; Q8VYN9; -.
EnsemblPlants; AT5G54430.1; AT5G54430.1; AT5G54430.
EnsemblPlants; AT5G54430.4; AT5G54430.4; AT5G54430.
GeneID; 835531; -.
Gramene; AT5G54430.1; AT5G54430.1; AT5G54430.
Gramene; AT5G54430.4; AT5G54430.4; AT5G54430.
KEGG; ath:AT5G54430; -.
Araport; AT5G54430; -.
TAIR; locus:2147319; AT5G54430.
eggNOG; ENOG410JB3G; Eukaryota.
eggNOG; ENOG411179Q; LUCA.
HOGENOM; HOG000241527; -.
OMA; HPQLPNI; -.
OrthoDB; EOG09360LIX; -.
PhylomeDB; Q8VYN9; -.
PRO; PR:Q8VYN9; -.
Proteomes; UP000006548; Chromosome 5.
ExpressionAtlas; Q8VYN9; baseline and differential.
GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; IDA:TAIR.
GO; GO:0005634; C:nucleus; IDA:TAIR.
GO; GO:0005886; C:plasma membrane; IDA:TAIR.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0002238; P:response to molecule of fungal origin; IDA:TAIR.
GO; GO:0006950; P:response to stress; IEA:InterPro.
Gene3D; 3.40.50.620; -; 1.
InterPro; IPR014729; Rossmann-like_a/b/a_fold.
InterPro; IPR006015; Universal_stress_UspA.
InterPro; IPR006016; UspA.
Pfam; PF00582; Usp; 1.
PRINTS; PR01438; UNVRSLSTRESS.
1: Evidence at protein level;
ATP-binding; Chloroplast; Complete proteome; Nucleotide-binding;
Phosphoprotein; Plastid; Reference proteome; Transit peptide.
TRANSIT 1 43 Chloroplast. {ECO:0000255}.
CHAIN 44 242 Universal stress protein PHOS32.
/FTId=PRO_0000436334.
NP_BIND 168 178 ATP. {ECO:0000250|UniProtKB:Q57997}.
NP_BIND 186 188 ATP. {ECO:0000250|UniProtKB:Q57997}.
BINDING 19 19 ATP; via carbonyl oxygen.
{ECO:0000250|UniProtKB:Q57997}.
BINDING 83 83 ATP; via amide nitrogen and carbonyl
oxygen. {ECO:0000250|UniProtKB:Q57997}.
MOD_RES 21 21 Phosphoserine; by MAPK3 and MAPK6.
{ECO:0000244|PubMed:18433157,
ECO:0000244|PubMed:19376835,
ECO:0000269|PubMed:18285339,
ECO:0000269|PubMed:18785823}.
MOD_RES 219 219 Phosphoserine.
{ECO:0000244|PubMed:18433157}.
MUTAGEN 21 21 S->A,D: Impaired phosphorylation by MAPK3
and MAPK6. {ECO:0000269|PubMed:18285339}.
SEQUENCE 242 AA; 26202 MW; AB31B159CDAF3EA9 CRC64;
MNPADSDHPQ LPNIKIHHPP SPRHSHHHHS SSTPSSAATP TPTAGARRKI GVAVDLSEES
SFAVRWAVDH YIRPGDAVVL LHVSPTSVLF GADWGPLPLK TQIEDPNAQP QPSQEDFDAF
TSTKVADLAK PLKELGFPYK IHIVKDHDMR ERLCLEIERL GLSAVIMGSR GFGAEKKRGS
DGKLGSVSDY CVHHCVCPVV VVRYPDDRDG PVPIVTVKSG GDDDGDVVAA SASAHHEHIK
DE


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