HIR2_ARATH
ID HIR2_ARATH Reviewed; 286 AA.
AC Q9CAR7; B9DGQ2;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Hypersensitive-induced response protein 2;
DE Short=AtHIR2;
GN Name=HIR2; OrderedLocusNames=At1g69840; ORFNames=T17F3.13;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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; TISSUE=Rosette leaf;
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 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 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 [7]
RP INTERACTION WITH AHK2.
RX PubMed=18642946; DOI=10.1021/pr0703831;
RA Dortay H., Gruhn N., Pfeifer A., Schwerdtner M., Schmuelling T., Heyl A.;
RT "Toward an interaction map of the two-component signaling pathway of
RT Arabidopsis thaliana.";
RL J. Proteome Res. 7:3649-3660(2008).
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).
CC -!- SUBUNIT: Self-interacts and forms heteromers. Interacts with AHK2.
CC Interacts with NB-LRR class of R proteins (e.g. RPS2 or RPM1) before R
CC proteins are activated by the effectors. {ECO:0000269|PubMed:18642946,
CC ECO:0000269|Ref.8}.
CC -!- INTERACTION:
CC Q9CAR7; Q9C5U2: AHK2; NbExp=2; IntAct=EBI-1807580, EBI-1100634;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:15060130,
CC ECO:0000305|PubMed:17644812, ECO:0000305|Ref.8}; Lipid-anchor
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305|Ref.8}.
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DR EMBL; AC010675; AAG52556.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34984.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34985.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34986.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34987.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34988.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34989.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34990.1; -; Genomic_DNA.
DR EMBL; AY099840; AAM20691.1; -; mRNA.
DR EMBL; BT000336; AAN15655.1; -; mRNA.
DR EMBL; AK317238; BAH19919.1; -; mRNA.
DR PIR; F96720; F96720.
DR RefSeq; NP_001077802.1; NM_001084333.2.
DR RefSeq; NP_001077803.1; NM_001084334.2.
DR RefSeq; NP_001185358.1; NM_001198429.1.
DR RefSeq; NP_177142.1; NM_105652.6.
DR RefSeq; NP_849870.1; NM_179539.4.
DR RefSeq; NP_974116.1; NM_202387.4.
DR RefSeq; NP_974117.1; NM_202388.4.
DR AlphaFoldDB; Q9CAR7; -.
DR SMR; Q9CAR7; -.
DR BioGRID; 28541; 5.
DR IntAct; Q9CAR7; 3.
DR STRING; 3702.AT1G69840.3; -.
DR iPTMnet; Q9CAR7; -.
DR SwissPalm; Q9CAR7; -.
DR PaxDb; Q9CAR7; -.
DR PRIDE; Q9CAR7; -.
DR ProteomicsDB; 230222; -.
DR DNASU; 843320; -.
DR EnsemblPlants; AT1G69840.1; AT1G69840.1; AT1G69840.
DR EnsemblPlants; AT1G69840.2; AT1G69840.2; AT1G69840.
DR EnsemblPlants; AT1G69840.3; AT1G69840.3; AT1G69840.
DR EnsemblPlants; AT1G69840.4; AT1G69840.4; AT1G69840.
DR EnsemblPlants; AT1G69840.5; AT1G69840.5; AT1G69840.
DR EnsemblPlants; AT1G69840.6; AT1G69840.6; AT1G69840.
DR EnsemblPlants; AT1G69840.7; AT1G69840.7; AT1G69840.
DR GeneID; 843320; -.
DR Gramene; AT1G69840.1; AT1G69840.1; AT1G69840.
DR Gramene; AT1G69840.2; AT1G69840.2; AT1G69840.
DR Gramene; AT1G69840.3; AT1G69840.3; AT1G69840.
DR Gramene; AT1G69840.4; AT1G69840.4; AT1G69840.
DR Gramene; AT1G69840.5; AT1G69840.5; AT1G69840.
DR Gramene; AT1G69840.6; AT1G69840.6; AT1G69840.
DR Gramene; AT1G69840.7; AT1G69840.7; AT1G69840.
DR KEGG; ath:AT1G69840; -.
DR Araport; AT1G69840; -.
DR TAIR; locus:2196749; AT1G69840.
DR eggNOG; KOG2620; Eukaryota.
DR HOGENOM; CLU_024949_5_1_1; -.
DR InParanoid; Q9CAR7; -.
DR OMA; EMMMMTQ; -.
DR OrthoDB; 1237942at2759; -.
DR PhylomeDB; Q9CAR7; -.
DR PRO; PR:Q9CAR7; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9CAR7; baseline and differential.
DR Genevisible; Q9CAR7; AT.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0009705; C:plant-type vacuole membrane; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; 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 2"
FT /id="PRO_0000398597"
FT COILED 156..190
FT /evidence="ECO:0000255"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000255"
FT CONFLICT 258
FT /note="V -> E (in Ref. 4; BAH19919)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 286 AA; 31406 MW; 970254272F65D211 CRC64;
MGQALGCIQV DQSNVAIKET FGKFDEVLEP GCHCLPWCLG SQVAGHLSLR VQQLDVRCET
KTKDNVFVTV VASIQYRALA ESAQDAFYKL SNTRNQIQAY VFDVIRASVP KLDLDSTFEQ
KNDIAKTVET ELEKAMSHYG YEIVQTLIVD IEPDVHVKRA MNEINAASRM REAASEKAEA
EKILQIKRAE GEAESKYLSG MGIARQRQAI VDGLRNSVLA FSESVPGTSS KDVMDMVLVT
QYFDTLKEIG ASSKSNSVFI PHGPGAVRDI ASQIRDGLLQ GNSAAE
