PHO34_ARATH
ID PHO34_ARATH Reviewed; 260 AA.
AC Q8L4N1; O81835; Q67XF9; Q67XK0; Q67YW3; Q680I4; Q682U9;
DT 08-JUN-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Universal stress protein PHOS34 {ECO:0000303|PubMed:12644671};
DE AltName: Full=Phosphorylated protein of 34 kDa {ECO:0000303|PubMed:18285339};
DE Short=AtPHOS34 {ECO:0000303|PubMed:18285339};
DE Flags: Precursor;
GN Name=PHOS34 {ECO:0000303|PubMed:18285339};
GN OrderedLocusNames=At4g27320 {ECO:0000312|Araport:AT4G27320};
GN ORFNames=M4I22.130 {ECO:0000312|EMBL:CAA19726.1};
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 {ECO:0000312|EMBL:AAM60894.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP IDENTIFICATION.
RX PubMed=12644671; DOI=10.1104/pp.102.016006;
RA Kerk D., Bulgrien J., Smith D.W., Gribskov M.;
RT "Arabidopsis proteins containing similarity to the universal stress protein
RT domain of bacteria.";
RL Plant Physiol. 131:1209-1219(2003).
RN [8]
RP PHOSPHORYLATION UPON BACTERIAL ELICITATION, AND NICKEL-BINDING.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=18285339; DOI=10.1074/jbc.m800735200;
RA Merkouropoulos G., Andreasson E., Hess D., Boller T., Peck S.C.;
RT "An Arabidopsis protein phosphorylated in response to microbial
RT elicitation, AtPHOS32, is a substrate of MAP kinases 3 and 6.";
RL J. Biol. Chem. 283:10493-10499(2008).
RN [9]
RP PHOSPHORYLATION UPON INFECTION BY PHYTOPHTHORA INFESTANS ZOOSPORES AND
RP XYLANASE, AND PHOSPHORYLATION AT SER-20.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=18785823; DOI=10.1094/mpmi-21-10-1275;
RA Lenman M., Soerensson C., Andreasson E.;
RT "Enrichment of phosphoproteins and phosphopeptide derivatization identify
RT universal stress proteins in elicitor-treated Arabidopsis.";
RL Mol. Plant Microbe Interact. 21:1275-1284(2008).
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8L4N1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8L4N1-2; Sequence=VSP_058350;
CC -!- PTM: Phosphorylated by MAPK3 and MAPK6 after pathogenic elicitation
CC (e.g. bacterial flg22, Phytophthora infestans zoospores and xylanase).
CC {ECO:0000269|PubMed:18285339, ECO:0000269|PubMed:18785823}.
CC -!- MISCELLANEOUS: Can bind nickel. {ECO:0000269|PubMed:18285339}.
CC -!- SIMILARITY: Belongs to the universal stress protein A family.
CC {ECO:0000305}.
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DR EMBL; AL030978; CAA19726.1; -; Genomic_DNA.
DR EMBL; AL161566; CAB79587.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85324.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM66181.1; -; Genomic_DNA.
DR EMBL; AY123998; AAM74507.1; -; mRNA.
DR EMBL; AY143840; AAN28779.1; -; mRNA.
DR EMBL; AK318875; BAH56990.1; -; mRNA.
DR EMBL; AK175197; BAD42960.1; -; mRNA.
DR EMBL; AK175268; BAD43031.1; -; mRNA.
DR EMBL; AK175342; BAD43105.1; -; mRNA.
DR EMBL; AK175411; BAD43174.1; -; mRNA.
DR EMBL; AK175423; BAD43186.1; -; mRNA.
DR EMBL; AK175883; BAD43646.1; -; mRNA.
DR EMBL; AK176355; BAD44118.1; -; mRNA.
DR EMBL; AK176431; BAD44194.1; -; mRNA.
DR EMBL; AK176530; BAD44293.1; -; mRNA.
DR EMBL; AK176789; BAD44552.1; -; mRNA.
DR EMBL; AK176819; BAD44582.1; -; mRNA.
DR EMBL; AK176860; BAD44623.1; -; mRNA.
DR EMBL; AK176877; BAD44640.1; -; mRNA.
DR EMBL; AY084304; AAM60894.1; -; mRNA.
DR PIR; T05756; T05756.
DR RefSeq; NP_001328092.1; NM_001341845.1. [Q8L4N1-2]
DR RefSeq; NP_567770.1; NM_118866.5. [Q8L4N1-1]
DR AlphaFoldDB; Q8L4N1; -.
DR SMR; Q8L4N1; -.
DR STRING; 3702.AT4G27320.1; -.
DR iPTMnet; Q8L4N1; -.
DR PaxDb; Q8L4N1; -.
DR PRIDE; Q8L4N1; -.
DR ProteomicsDB; 236677; -. [Q8L4N1-1]
DR EnsemblPlants; AT4G27320.1; AT4G27320.1; AT4G27320. [Q8L4N1-1]
DR EnsemblPlants; AT4G27320.2; AT4G27320.2; AT4G27320. [Q8L4N1-2]
DR GeneID; 828840; -.
DR Gramene; AT4G27320.1; AT4G27320.1; AT4G27320. [Q8L4N1-1]
DR Gramene; AT4G27320.2; AT4G27320.2; AT4G27320. [Q8L4N1-2]
DR KEGG; ath:AT4G27320; -.
DR Araport; AT4G27320; -.
DR TAIR; locus:2131719; AT4G27320.
DR eggNOG; ENOG502RXH2; Eukaryota.
DR HOGENOM; CLU_049301_0_0_1; -.
DR InParanoid; Q8L4N1; -.
DR OMA; QLPHIRI; -.
DR PRO; PR:Q8L4N1; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8L4N1; baseline and differential.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0002238; P:response to molecule of fungal origin; IDA:TAIR.
DR Gene3D; 3.40.50.620; -; 1.
DR InterPro; IPR044162; PHOS32/34.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR006015; Universal_stress_UspA.
DR InterPro; IPR006016; UspA.
DR PANTHER; PTHR31966; PTHR31966; 1.
DR Pfam; PF00582; Usp; 1.
DR PRINTS; PR01438; UNVRSLSTRESS.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Chloroplast; Nucleotide-binding;
KW Phosphoprotein; Plastid; Reference proteome; Transit peptide.
FT TRANSIT 1..33
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 34..260
FT /note="Universal stress protein PHOS34"
FT /id="PRO_0000436335"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 92..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 209..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..108
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..260
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 18
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q57997"
FT BINDING 80
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q57997"
FT BINDING 170..179
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q57997"
FT BINDING 187..189
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q57997"
FT MOD_RES 20
FT /note="Phosphoserine; by MAPK3 and MAPK6"
FT /evidence="ECO:0000269|PubMed:18785823"
FT MOD_RES 230
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VYN9"
FT VAR_SEQ 259..260
FT /note="DE -> G (in isoform 2)"
FT /id="VSP_058350"
FT CONFLICT 94
FT /note="L -> F (in Ref. 5; BAD44118)"
FT /evidence="ECO:0000305"
FT CONFLICT 96
FT /note="L -> I (in Ref. 5; BAD43646)"
FT /evidence="ECO:0000305"
FT CONFLICT 138
FT /note="G -> E (in Ref. 5; BAD43031)"
FT /evidence="ECO:0000305"
FT CONFLICT 182
FT /note="D -> G (in Ref. 5; BAD44582)"
FT /evidence="ECO:0000305"
FT CONFLICT 215
FT /note="P -> L (in Ref. 5; BAD44623)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 260 AA; 28106 MW; 6326F66E6B1CA87A CRC64;
MNPDSDYPHL PNIKIHHPSS PRHSHHHSSS TPSAATPTPT AGARRKIGVA VDLSEESAFA
VRWAVDHYIR PGDAVVILHV SPTSVLFGAD WGPLPLQTPP PPSAATDPGA QPKPSQEDFD
AFTSSKVADL AKPLKEAGFP HKIHIVKDHD MRERLCLETE RLNLSAVIMG SRGFGAEKRG
SDGKLGSVSD YCVHHCVCPV VVVRYPDDRD GPAPPGNVGA TREAIVTVKS RRDDDDDDDE
DHEAKIAAAA SDHHEHIKDE
