HSPR2_ARATH
ID HSPR2_ARATH Reviewed; 435 AA.
AC O04203; Q8GUL9; Q8LB61;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 25-MAY-2022, entry version 120.
DE RecName: Full=Nematode resistance protein-like HSPRO2;
DE AltName: Full=AKINbetagamma-interacting protein 2;
DE AltName: Full=Ortholog of sugar beet HS1 PRO-1 protein 2;
DE AltName: Full=Protein Hs1pro-2;
GN Name=HSPRO2; OrderedLocusNames=At2g40000; ORFNames=T28M21.16;
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 [MRNA], INTERACTION WITH SNF4, AND SUBCELLULAR
RP LOCATION.
RX PubMed=17028154; DOI=10.1104/pp.106.087718;
RA Gissot L., Polge C., Jossier M., Girin T., Bouly J.-P., Kreis M.,
RA Thomas M.;
RT "AKINbetagamma contributes to SnRK1 heterotrimeric complexes and interacts
RT with two proteins implicated in plant pathogen resistance through its
RT KIS/GBD sequence.";
RL Plant Physiol. 142:931-944(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [3]
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 [4]
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 [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 INDUCTION BY FLG22.
RX PubMed=15085136; DOI=10.1038/nature02485;
RA Zipfel C., Robatzek S., Navarro L., Oakeley E.J., Jones J.D.G., Felix G.,
RA Boller T.;
RT "Bacterial disease resistance in Arabidopsis through flagellin
RT perception.";
RL Nature 428:764-767(2004).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION.
RX PubMed=17977154; DOI=10.1094/mpmi-20-11-1431;
RA Murray S.L., Ingle R.A., Petersen L.N., Denby K.J.;
RT "Basal resistance against Pseudomonas syringae in Arabidopsis involves
RT WRKY53 and a protein with homology to a nematode resistance protein.";
RL Mol. Plant Microbe Interact. 20:1431-1438(2007).
CC -!- FUNCTION: Positive regulator of basal resistance.
CC {ECO:0000269|PubMed:17977154}.
CC -!- SUBUNIT: Interacts with SNF4. {ECO:0000269|PubMed:17028154}.
CC -!- INTERACTION:
CC O04203; Q944A6: SNF4; NbExp=3; IntAct=EBI-1153953, EBI-2360649;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17028154}.
CC -!- INDUCTION: By bacterial pathogen P.syringae pv. tomato. By Salycilic
CC acid (SA). By the bacterial elicitor flg22.
CC {ECO:0000269|PubMed:15085136, ECO:0000269|PubMed:17977154}.
CC -!- DISRUPTION PHENOTYPE: Shows high sensibility to P.syringae pv. tomato
CC infection. {ECO:0000269|PubMed:17977154}.
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DR EMBL; DQ132635; ABA12453.1; -; mRNA.
DR EMBL; AF002109; AAB95285.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09761.1; -; Genomic_DNA.
DR EMBL; AY080778; AAL87262.1; -; mRNA.
DR EMBL; AY117156; AAM51231.1; -; mRNA.
DR EMBL; BT002396; AAO00756.1; -; mRNA.
DR EMBL; AY087407; AAM64956.1; -; mRNA.
DR PIR; A84824; A84824.
DR RefSeq; NP_181529.1; NM_129558.3.
DR AlphaFoldDB; O04203; -.
DR BioGRID; 3926; 7.
DR IntAct; O04203; 5.
DR STRING; 3702.AT2G40000.1; -.
DR iPTMnet; O04203; -.
DR PaxDb; O04203; -.
DR PRIDE; O04203; -.
DR ProteomicsDB; 230252; -.
DR EnsemblPlants; AT2G40000.1; AT2G40000.1; AT2G40000.
DR GeneID; 818588; -.
DR Gramene; AT2G40000.1; AT2G40000.1; AT2G40000.
DR KEGG; ath:AT2G40000; -.
DR Araport; AT2G40000; -.
DR TAIR; locus:2061221; AT2G40000.
DR eggNOG; ENOG502S740; Eukaryota.
DR HOGENOM; CLU_036144_0_0_1; -.
DR InParanoid; O04203; -.
DR OMA; ESFCFRS; -.
DR OrthoDB; 533789at2759; -.
DR PhylomeDB; O04203; -.
DR PRO; PR:O04203; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O04203; baseline and differential.
DR Genevisible; O04203; AT.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0071456; P:cellular response to hypoxia; HEP:TAIR.
DR GO; GO:0042742; P:defense response to bacterium; IMP:TAIR.
DR GO; GO:0006979; P:response to oxidative stress; IMP:TAIR.
DR GO; GO:0009751; P:response to salicylic acid; IEP:TAIR.
DR GO; GO:0019441; P:tryptophan catabolic process to kynurenine; IEA:InterPro.
DR InterPro; IPR009743; Hs1pro-1_C.
DR InterPro; IPR038759; HSPRO1/HSPRO2.
DR InterPro; IPR009869; HSPRO1_N.
DR InterPro; IPR037217; Trp/Indoleamine_2_3_dOase-like.
DR PANTHER; PTHR34795; PTHR34795; 1.
DR Pfam; PF07014; Hs1pro-1_C; 1.
DR Pfam; PF07231; Hs1pro-1_N; 2.
DR SUPFAM; SSF140959; SSF140959; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Plant defense; Reference proteome.
FT CHAIN 1..435
FT /note="Nematode resistance protein-like HSPRO2"
FT /id="PRO_0000412197"
FT CONFLICT 44
FT /note="C -> S (in Ref. 4; AAO00756)"
FT /evidence="ECO:0000305"
FT CONFLICT 259
FT /note="G -> E (in Ref. 5; AAM64956)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 435 AA; 49244 MW; A0121598C4C751B1 CRC64;
MVDMDWKRKM VSSDLPNSPK LSSKLHVTIP SPFKIVPVSS PISCSAPALC SAYELYLRLP
ELRKLWSSRD FPQWTSEPIL KPALQALEIS FRLVFAVCSD TRPYINHREW NRRLDSLITK
QIQLVAAICE DEEEEGISAE APVGGGRSSL SLLPQLATWR RSEALGKKIL YTIDNEMSRC
KYTLGLGEQN IAGKPNLRYD AICRPNEIYS LKDNPYADHI DNHENQTLYI IHQILESWIY
ASGNLLNRIV SSIEEEKFGK ASNDVYLLEK IWKILAEIED LHMLMDPEDF LKLKKQLQIK
STGKNDAFCF RSKGLVEMMK MSKDLRQKVP AVLAVEVDPT GGPRLQEAAM KLYARKTECD
KIHLLQGMQA VEAAAKSFFF GYRQLVAAMM GSAEMNATAS QESCDSLSQI FMEPTYFPSL
DAAKTFLGEF WSHLG
