POP3_ARATH
ID POP3_ARATH Reviewed; 109 AA.
AC Q9LUV2; Q0WKU8; Q8LCB1;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Stress-response A/B barrel domain-containing protein HS1 {ECO:0000305};
DE AltName: Full=Pop3 family protein At3g17210 {ECO:0000305};
DE AltName: Full=Protein HEAT STABLE 1 {ECO:0000303|PubMed:17720140};
DE Short=AtHS1 {ECO:0000303|PubMed:17720140};
GN Name=HS1 {ECO:0000303|PubMed:17720140}; OrderedLocusNames=At3g17210;
GN ORFNames=MGD8.2;
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=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(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].
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, AND INDUCTION.
RX PubMed=17720140; DOI=10.1016/j.bbrc.2007.07.188;
RA Park S.C., Lee J.R., Shin S.O., Park Y., Lee S.Y., Hahm K.S.;
RT "Characterization of a heat-stable protein with antimicrobial activity from
RT Arabidopsis thaliana.";
RL Biochem. Biophys. Res. Commun. 362:562-567(2007).
RN [7]
RP STRUCTURE BY NMR.
RX PubMed=14872131; DOI=10.1023/b:jnmr.0000015385.54050.19;
RA Lytle B.L., Peterson F.C., Kjer K.L., Frederick R.O., Zhao Q., Thao S.,
RA Bingman C., Johnson K.A., Phillips G.N. Jr., Volkman B.F.;
RT "Structure of the hypothetical protein At3g17210 from Arabidopsis
RT thaliana.";
RL J. Biomol. NMR 28:397-400(2004).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH MAGNESIUM, AND
RP SUBUNIT.
RX PubMed=15326607; DOI=10.1002/prot.20215;
RA Bingman C.A., Johnson K.A., Peterson F.C., Frederick R.O., Zhao Q.,
RA Thao S., Fox B.G., Volkman B.F., Jeon W.B., Smith D.W., Newman C.S.,
RA Ulrich E.L., Hegeman A., Sussman M.R., Markley J.L., Phillips G.N. Jr.;
RT "Crystal structure of the protein from gene At3g17210 of Arabidopsis
RT thaliana.";
RL Proteins 57:218-220(2004).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH MAGNESIUM.
RX PubMed=17850744; DOI=10.1016/j.str.2007.06.019;
RA Levin E.J., Kondrashov D.A., Wesenberg G.E., Phillips G.N. Jr.;
RT "Ensemble refinement of protein crystal structures: validation and
RT application.";
RL Structure 15:1040-1052(2007).
CC -!- FUNCTION: Heat stable protein involved in defense against fungal
CC pathogens. Possesses antifungal activity against diverse pathogenic
CC fungi. Possesses antimicrobial activity. Possesses ribonuclease
CC activity. {ECO:0000269|PubMed:17720140}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:15326607, ECO:0000269|PubMed:17850744};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15326607}.
CC -!- INDUCTION: By salicylic acid (SA) and jasmonic acid (JA).
CC {ECO:0000269|PubMed:17720140}.
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DR EMBL; AB022216; BAB02723.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75921.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM65995.1; -; Genomic_DNA.
DR EMBL; AF370462; AAK43839.1; -; mRNA.
DR EMBL; AY064673; AAL47379.1; -; mRNA.
DR EMBL; AK230465; BAF02259.1; -; mRNA.
DR EMBL; AY086696; AAM63750.1; -; mRNA.
DR RefSeq; NP_001319574.1; NM_001338278.1.
DR RefSeq; NP_566569.1; NM_112598.4.
DR PDB; 1Q4R; X-ray; 1.90 A; A=1-109.
DR PDB; 1Q53; NMR; -; A/B=1-109.
DR PDB; 2Q3P; X-ray; 1.90 A; A=1-109.
DR PDBsum; 1Q4R; -.
DR PDBsum; 1Q53; -.
DR PDBsum; 2Q3P; -.
DR AlphaFoldDB; Q9LUV2; -.
DR BMRB; Q9LUV2; -.
DR SMR; Q9LUV2; -.
DR BioGRID; 6313; 52.
DR IntAct; Q9LUV2; 52.
DR STRING; 3702.AT3G17210.1; -.
DR PaxDb; Q9LUV2; -.
DR PRIDE; Q9LUV2; -.
DR ProteomicsDB; 234891; -.
DR EnsemblPlants; AT3G17210.1; AT3G17210.1; AT3G17210.
DR EnsemblPlants; AT3G17210.2; AT3G17210.2; AT3G17210.
DR GeneID; 820980; -.
DR Gramene; AT3G17210.1; AT3G17210.1; AT3G17210.
DR Gramene; AT3G17210.2; AT3G17210.2; AT3G17210.
DR KEGG; ath:AT3G17210; -.
DR Araport; AT3G17210; -.
DR TAIR; locus:2089055; AT3G17210.
DR eggNOG; ENOG502S12K; Eukaryota.
DR HOGENOM; CLU_080664_4_1_1; -.
DR InParanoid; Q9LUV2; -.
DR OMA; YLPHPDH; -.
DR OrthoDB; 1579369at2759; -.
DR PhylomeDB; Q9LUV2; -.
DR EvolutionaryTrace; Q9LUV2; -.
DR PRO; PR:Q9LUV2; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LUV2; baseline and differential.
DR Genevisible; Q9LUV2; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042742; P:defense response to bacterium; IDA:TAIR.
DR GO; GO:0050832; P:defense response to fungus; IDA:TAIR.
DR GO; GO:0009865; P:pollen tube adhesion; IBA:GO_Central.
DR InterPro; IPR013097; Dabb.
DR InterPro; IPR011008; Dimeric_a/b-barrel.
DR InterPro; IPR044662; HS1/DABB1-like.
DR PANTHER; PTHR33178; PTHR33178; 1.
DR Pfam; PF07876; Dabb; 1.
DR SMART; SM00886; Dabb; 1.
DR SUPFAM; SSF54909; SSF54909; 1.
DR PROSITE; PS51502; S_R_A_B_BARREL; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Magnesium; Metal-binding; Plant defense; Reference proteome.
FT CHAIN 1..109
FT /note="Stress-response A/B barrel domain-containing protein
FT HS1"
FT /id="PRO_0000058515"
FT DOMAIN 8..102
FT /note="Stress-response A/B barrel"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00835"
FT BINDING 36
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:15326607,
FT ECO:0000269|PubMed:17850744, ECO:0007744|PDB:1Q4R,
FT ECO:0007744|PDB:2Q3P"
FT BINDING 39
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:15326607,
FT ECO:0000269|PubMed:17850744, ECO:0007744|PDB:1Q4R,
FT ECO:0007744|PDB:2Q3P"
FT BINDING 40
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:15326607,
FT ECO:0000269|PubMed:17850744, ECO:0007744|PDB:1Q4R,
FT ECO:0007744|PDB:2Q3P"
FT BINDING 42
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:15326607,
FT ECO:0000269|PubMed:17850744, ECO:0007744|PDB:1Q4R,
FT ECO:0007744|PDB:2Q3P"
FT CONFLICT 85
FT /note="E -> K (in Ref. 4; AAM63750)"
FT /evidence="ECO:0000305"
FT STRAND 8..16
FT /evidence="ECO:0007829|PDB:1Q4R"
FT HELIX 22..33
FT /evidence="ECO:0007829|PDB:1Q4R"
FT HELIX 35..38
FT /evidence="ECO:0007829|PDB:1Q4R"
FT STRAND 44..49
FT /evidence="ECO:0007829|PDB:1Q4R"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:1Q4R"
FT STRAND 62..69
FT /evidence="ECO:0007829|PDB:1Q4R"
FT HELIX 71..79
FT /evidence="ECO:0007829|PDB:1Q4R"
FT HELIX 81..92
FT /evidence="ECO:0007829|PDB:1Q4R"
FT STRAND 94..102
FT /evidence="ECO:0007829|PDB:1Q4R"
SQ SEQUENCE 109 AA; 12184 MW; B498426DDC5F9F37 CRC64;
MEEAKGPVKH VLLASFKDGV SPEKIEELIK GYANLVNLIE PMKAFHWGKD VSIENLHQGY
THIFESTFES KEAVAEYIAH PAHVEFATIF LGSLDKVLVI DYKPTSVSL
