HSR4_ARATH
ID HSR4_ARATH Reviewed; 576 AA.
AC Q8VZG2; Q8LBK2; Q9SVK6;
DT 11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Protein HYPER-SENSITIVITY-RELATED 4 {ECO:0000303|PubMed:15181213};
DE Short=AtHSR4 {ECO:0000303|PubMed:15181213};
DE EC=3.6.1.- {ECO:0000250|UniProtKB:Q9FLD5};
DE AltName: Full=BCS1-like protein;
GN Name=HSR4 {ECO:0000303|PubMed:15181213}; Synonyms=BCS1;
GN OrderedLocusNames=At3g50930 {ECO:0000312|EMBL:AEE78728.1};
GN ORFNames=F18B3.210 {ECO:0000312|EMBL:CAB42922.1};
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:AAL57634.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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=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] OF 34-576.
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 [5]
RP INDUCTION BY XANTHOMONAS CAMPESTRIS.
RX PubMed=10518009; DOI=10.1016/s0014-5793(99)01233-8;
RA Lacomme C.J., Roby D.;
RT "Identification of new early markers of the hypersensitive response in
RT Arabidopsis thaliana.";
RL FEBS Lett. 459:149-153(1999).
RN [6]
RP INDUCTION BY FLG22.
RX PubMed=15181213; DOI=10.1104/pp.103.036749;
RA Navarro L., Zipfel C., Rowland O., Keller I., Robatzek S., Boller T.,
RA Jones J.D.;
RT "The transcriptional innate immune response to flg22. Interplay and overlap
RT with Avr gene-dependent defense responses and bacterial pathogenesis.";
RL Plant Physiol. 135:1113-1128(2004).
RN [7]
RP INDUCTION BY YARIV PHENYLGLYCOSIDES.
RX PubMed=15235117; DOI=10.1104/pp.104.039370;
RA Guan Y., Nothnagel E.A.;
RT "Binding of arabinogalactan proteins by Yariv phenylglycoside triggers
RT wound-like responses in Arabidopsis cell cultures.";
RL Plant Physiol. 135:1346-1366(2004).
RN [8]
RP INDUCTION BY ERWINIA CAROTOVORA.
RX PubMed=16270229; DOI=10.1007/s11103-005-1002-3;
RA Pandey A.-K., Ger M.-J., Huang H.-E., Yip M.-K., Zeng J., Feng T.-Y.;
RT "Expression of the hypersensitive response-assisting protein in Arabidopsis
RT results in harpin-dependent hypersensitive cell death in response to
RT Erwinia carotovora.";
RL Plant Mol. Biol. 59:771-780(2005).
RN [9]
RP INDUCTION BY BTH.
RX PubMed=16766691; DOI=10.1105/tpc.105.039677;
RA Mosher R.A., Durrant W.E., Wang D., Song J., Dong X.;
RT "A comprehensive structure-function analysis of Arabidopsis SNI1 defines
RT essential regions and transcriptional repressor activity.";
RL Plant Cell 18:1750-1765(2006).
RN [10]
RP INDUCTION BY TNT.
RX PubMed=18702669; DOI=10.1111/j.1365-313x.2008.03653.x;
RA Gandia-Herrero F., Lorenz A., Larson T., Graham I.A., Bowles D.J.,
RA Rylott E.L., Bruce N.C.;
RT "Detoxification of the explosive 2,4,6-trinitrotoluene in Arabidopsis:
RT discovery of bifunctional O- and C-glucosyltransferases.";
RL Plant J. 56:963-974(2008).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:Q9FLD5};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q9FLD5};
CC -!- SUBUNIT: Binds to the Yariv phenylglycoside (beta-D-Glc)(3).
CC {ECO:0000269|PubMed:15235117}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- INDUCTION: Accumulates in response to flg22, thus being a FLARE
CC (flagellin rapidly elicited gene) (PubMed:15181213). Up-regulated by
CC the Yariv phenylglycoside (beta-D-Glc)(3) (PubMed:15235117). Expressed
CC during hypersensitive response (HR) mediated by the bacterial pathogen
CC Xanthomonas campestris pv. campestris (PubMed:10518009). Slightly
CC induced by the virulent pathogen Erwinia carotovora subsp. carotovora
CC (PubMed:16270229). Triggered by benzothiadiazole S-methylester (BTH)
CC (PubMed:16766691). Accumulates in the presence of 2,4,6-trinitrotoluene
CC (TNT) (PubMed:18702669). {ECO:0000269|PubMed:10518009,
CC ECO:0000269|PubMed:15181213, ECO:0000269|PubMed:15235117,
CC ECO:0000269|PubMed:16270229, ECO:0000269|PubMed:16766691,
CC ECO:0000269|PubMed:18702669}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. BCS1 subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM26687.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAM64718.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAB42922.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL049862; CAB42922.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002686; AEE78728.1; -; Genomic_DNA.
DR EMBL; AF370607; AAK43926.1; -; mRNA.
DR EMBL; AY064981; AAL57634.1; -; mRNA.
DR EMBL; AY102119; AAM26687.1; ALT_INIT; mRNA.
DR EMBL; BT002611; AAO11527.1; -; mRNA.
DR EMBL; AY087160; AAM64718.1; ALT_INIT; mRNA.
DR PIR; T08414; T08414.
DR RefSeq; NP_190662.2; NM_114953.3.
DR AlphaFoldDB; Q8VZG2; -.
DR SMR; Q8VZG2; -.
DR STRING; 3702.AT3G50930.1; -.
DR PaxDb; Q8VZG2; -.
DR PRIDE; Q8VZG2; -.
DR ProteomicsDB; 232118; -.
DR EnsemblPlants; AT3G50930.1; AT3G50930.1; AT3G50930.
DR GeneID; 824257; -.
DR Gramene; AT3G50930.1; AT3G50930.1; AT3G50930.
DR KEGG; ath:AT3G50930; -.
DR Araport; AT3G50930; -.
DR TAIR; locus:2077997; AT3G50930.
DR eggNOG; KOG0743; Eukaryota.
DR HOGENOM; CLU_010189_0_2_1; -.
DR InParanoid; Q8VZG2; -.
DR OMA; SVENHAM; -.
DR OrthoDB; 532729at2759; -.
DR PhylomeDB; Q8VZG2; -.
DR PRO; PR:Q8VZG2; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8VZG2; baseline and differential.
DR Genevisible; Q8VZG2; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005740; C:mitochondrial envelope; IDA:TAIR.
DR GO; GO:0005741; C:mitochondrial outer membrane; IDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; IPI:TAIR.
DR GO; GO:0008219; P:cell death; IMP:TAIR.
DR GO; GO:0009626; P:plant-type hypersensitive response; IEP:UniProtKB.
DR GO; GO:0009617; P:response to bacterium; IEP:UniProtKB.
DR GO; GO:0002237; P:response to molecule of bacterial origin; IEP:UniProtKB.
DR GO; GO:0009411; P:response to UV; IEP:TAIR.
DR GO; GO:0009863; P:salicylic acid mediated signaling pathway; IMP:TAIR.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR025753; AAA_N_dom.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF14363; AAA_assoc; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00674; AAA; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Hydrolase; Hypersensitive response; Magnesium; Membrane;
KW Nucleotide-binding; Plant defense; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..576
FT /note="Protein HYPER-SENSITIVITY-RELATED 4"
FT /id="PRO_0000434702"
FT TRANSMEM 55..75
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 508..532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 306..313
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT CONFLICT 522
FT /note="K -> R (in Ref. 4; AAM64718)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 576 AA; 66136 MW; 90B8C6DC41A05C9C CRC64;
MEGSKLLPCV HKSPVPTSHQ LYINYEILGL TKLKKHKYTQ NKMSSSDSSS AESRLATAKT
VLTTAASVAA TAMLARSLVQ DYLPDEVHHY ISYGFRSIFG YFSSQMTIII EEFEGFAHNE
VFEAAEAYLA TKISPSNKRI KVSKHEKENN YNVTVERDEE VVDTYNGVKF QWILHCRHVE
SKHFHNPRDL NSTLRSEVRS FELNFHKKFK DVALESYLPF MVKRATLMKQ EKKTLKIFTL
SPENMYGNYS DAWTSVTLDH PSTFKTLAMD SDVKTSVMED LDKFVKRRDF YKRVGKAWKR
GYLLYGPPGT GKSSLIAAMA NHLNFDIYDL ELTAVNNNSE LRRLLIATAN RSILIVEDID
CSLELKDRTS DEPPRESDDI EDPRYKKVTL SGLLNFIDGL WSSCGDERII IFTTNYKEKL
DAALLRPGRM DMHIHMSYCT PSTFKALALN YLEIKEHRLF SKIEEGIEAT EVTPAEVAEQ
LMRNDSVDKV LEGLIEFLKV KKIENEQDKA KTEKQELENK KKTKEGTDSV VKKEVDEQLV
RNDRVDKVLE GLVELLKAKK IEDDQDKAKH EEVEQH
