HIR1_ARATH
ID HIR1_ARATH Reviewed; 286 AA.
AC Q9FM19;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 114.
DE RecName: Full=Hypersensitive-induced response protein 1 {ECO:0000303|PubMed:15060130};
DE Short=AtHIR1 {ECO:0000303|PubMed:15060130};
GN Name=HIR1 {ECO:0000303|PubMed:15060130};
GN Synonyms=P31 {ECO:0000303|PubMed:15319477};
GN OrderedLocusNames=At5g62740 {ECO:0000312|Araport:AT5G62740};
GN ORFNames=MQB2.6 {ECO:0000312|EMBL:BAB10843.1};
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9628582; DOI=10.1093/dnares/5.1.41;
RA Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence
RT features of the regions of 1,456,315 bp covered by nineteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:41-54(1998).
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].
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 IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=15060130; DOI=10.1074/mcp.m400001-mcp200;
RA Marmagne A., Rouet M.-A., Ferro M., Rolland N., Alcon C., Joyard J.,
RA Garin J., Barbier-Brygoo H., Ephritikhine G.;
RT "Identification of new intrinsic proteins in Arabidopsis plasma membrane
RT proteome.";
RL Mol. Cell. Proteomics 3:675-691(2004).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=15319477; DOI=10.1105/tpc.104.024372;
RA Favery B., Chelysheva L.A., Lebris M., Jammes F., Marmagne A.,
RA De Almeida-Engler J., Lecomte P., Vaury C., Arkowitz R.A., Abad P.;
RT "Arabidopsis formin AtFH6 is a plasma membrane-associated protein
RT upregulated in giant cells induced by parasitic nematodes.";
RL Plant Cell 16:2529-2540(2004).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=17644812; DOI=10.1074/mcp.m700099-mcp200;
RA Marmagne A., Ferro M., Meinnel T., Bruley C., Kuhn L., Garin J.,
RA Barbier-Brygoo H., Ephritikhine G.;
RT "A high content in lipid-modified peripheral proteins and integral receptor
RT kinases features in the arabidopsis plasma membrane proteome.";
RL Mol. Cell. Proteomics 6:1980-1996(2007).
RN [8]
RP INTERACTION WITH RESISTANCE PROTEINS, SUBUNIT, AND SUBCELLULAR LOCATION.
RA Qi Y., Katagiri F.;
RT "New classes of proteins forming complexes with resistance proteins.";
RL (In) Proceedings of the 20th international conference on Arabidopsis
RL research, abstract#501734213, Edinburgh (2009).
RN [9]
RP INTERACTION WITH LRR1.
RX PubMed=19712067; DOI=10.1111/j.1365-3040.2009.02039.x;
RA Zhou L., Cheung M.Y., Zhang Q., Lei C.L., Zhang S.H., Sun S.S., Lam H.M.;
RT "A novel simple extracellular leucine-rich repeat (eLRR) domain protein
RT from rice (OsLRR1) enters the endosomal pathway and interacts with the
RT hypersensitive-induced reaction protein 1 (OsHIR1).";
RL Plant Cell Environ. 32:1804-1820(2009).
CC -!- FUNCTION: Positive regulator of hypersensitive response (HR)-like cell
CC death. May be involved in potassium ion channel regulation.
CC {ECO:0000250|UniProtKB:Q5GI04}.
CC -!- SUBUNIT: Self-interacts and forms heteromers (Ref.8). Interacts with
CC NB-LRR class of R proteins before R proteins (e.g. RPS2 or RPM1) are
CC activated by the effectors (Ref.8). Interacts with LRR1
CC (PubMed:19712067). {ECO:0000269|PubMed:19712067, ECO:0000269|Ref.8}.
CC -!- INTERACTION:
CC Q9FM19; Q9C5U2: AHK2; NbExp=2; IntAct=EBI-1807466, EBI-1100634;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15060130,
CC ECO:0000305|PubMed:15319477, ECO:0000305|PubMed:17644812,
CC ECO:0000305|Ref.8}; Lipid-anchor {ECO:0000305}; Cytoplasmic side
CC {ECO:0000305|PubMed:15319477, ECO:0000305|PubMed:17644812,
CC ECO:0000305|Ref.8}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY062850; AAL32928.1; -; mRNA.
DR EMBL; AY114572; AAM47891.1; -; mRNA.
DR EMBL; AY086631; AAM63689.1; -; mRNA.
DR EMBL; AB009053; BAB10843.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97649.1; -; Genomic_DNA.
DR RefSeq; NP_201080.1; NM_125669.3.
DR AlphaFoldDB; Q9FM19; -.
DR SMR; Q9FM19; -.
DR BioGRID; 21638; 4.
DR IntAct; Q9FM19; 1.
DR STRING; 3702.AT5G62740.1; -.
DR iPTMnet; Q9FM19; -.
DR SwissPalm; Q9FM19; -.
DR PaxDb; Q9FM19; -.
DR PRIDE; Q9FM19; -.
DR ProteomicsDB; 228742; -.
DR EnsemblPlants; AT5G62740.1; AT5G62740.1; AT5G62740.
DR GeneID; 836395; -.
DR Gramene; AT5G62740.1; AT5G62740.1; AT5G62740.
DR KEGG; ath:AT5G62740; -.
DR Araport; AT5G62740; -.
DR TAIR; locus:2170698; AT5G62740.
DR eggNOG; KOG2620; Eukaryota.
DR HOGENOM; CLU_024949_5_1_1; -.
DR InParanoid; Q9FM19; -.
DR OMA; CHTETAK; -.
DR OrthoDB; 1237942at2759; -.
DR PhylomeDB; Q9FM19; -.
DR PRO; PR:Q9FM19; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FM19; baseline and differential.
DR Genevisible; Q9FM19; AT.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0043424; F:protein histidine kinase binding; IPI:UniProtKB.
DR Gene3D; 3.30.479.30; -; 1.
DR InterPro; IPR001107; Band_7.
DR InterPro; IPR036013; Band_7/SPFH_dom_sf.
DR Pfam; PF01145; Band_7; 1.
DR SMART; SM00244; PHB; 1.
DR SUPFAM; SSF117892; SSF117892; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Coiled coil; Lipoprotein; Membrane; Myristate;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255"
FT CHAIN 2..286
FT /note="Hypersensitive-induced response protein 1"
FT /id="PRO_0000398596"
FT COILED 114..190
FT /evidence="ECO:0000255"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 286 AA; 31431 MW; D8C80F2E30949B57 CRC64;
MGNLFCCVQV DQSTVAIKET FGKFEDVLEP GCHFLPWCLG SQVAGYLSLR VQQLDVRCET
KTKDNVFVNV VASIQYRALA NKANDAYYKL SNTRGQIQAY VFDVIRASVP KLLLDDVFEQ
KNDIAKAVEE ELEKAMSAYG YEIVQTLIVD IEPDEHVKRA MNEINAAARM RLAANEKAEA
EKILQIKRAE GEAESKYLSG LGIARQRQAI VDGLRDSVLG FAVNVPGTTA KDVMDMVLVT
QYFDTMKEIG ASSKSSAVFI PHGPGAVRDV ASQIRDGLLQ GSSANL
