HSPR1_ARATH
ID HSPR1_ARATH Reviewed; 428 AA.
AC Q9LY61; Q2QCL4; Q8LEJ2;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Nematode resistance protein-like HSPRO1;
DE AltName: Full=AKINbetagamma-interacting protein 1;
DE AltName: Full=Ortholog of sugar beet HS1 PRO-1 protein 1;
DE AltName: Full=Protein Hs1pro-1;
GN Name=HSPRO1; OrderedLocusNames=At3g55840; ORFNames=F27K19.20;
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=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 [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.
CC -!- FUNCTION: Positive regulator of basal resistance. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with SNF4. {ECO:0000269|PubMed:17028154}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17028154}.
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DR EMBL; DQ132634; ABA12452.1; -; mRNA.
DR EMBL; AL163832; CAB87838.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79447.1; -; Genomic_DNA.
DR EMBL; AY034950; AAK59456.1; -; mRNA.
DR EMBL; AY070026; AAL47497.1; -; mRNA.
DR EMBL; AY085394; AAM62622.1; -; mRNA.
DR PIR; T49196; T49196.
DR RefSeq; NP_191143.1; NM_115442.2.
DR AlphaFoldDB; Q9LY61; -.
DR BioGRID; 10066; 2.
DR IntAct; Q9LY61; 3.
DR STRING; 3702.AT3G55840.1; -.
DR PaxDb; Q9LY61; -.
DR PRIDE; Q9LY61; -.
DR ProteomicsDB; 232152; -.
DR DNASU; 824750; -.
DR EnsemblPlants; AT3G55840.1; AT3G55840.1; AT3G55840.
DR GeneID; 824750; -.
DR Gramene; AT3G55840.1; AT3G55840.1; AT3G55840.
DR KEGG; ath:AT3G55840; -.
DR Araport; AT3G55840; -.
DR TAIR; locus:2081988; AT3G55840.
DR eggNOG; ENOG502QVKI; Eukaryota.
DR HOGENOM; CLU_036144_0_0_1; -.
DR InParanoid; Q9LY61; -.
DR OMA; ESWIYVS; -.
DR OrthoDB; 533789at2759; -.
DR PhylomeDB; Q9LY61; -.
DR PRO; PR:Q9LY61; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LY61; baseline and differential.
DR Genevisible; Q9LY61; 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:0006952; P:defense response; IEA:UniProtKB-KW.
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; 1.
DR SUPFAM; SSF140959; SSF140959; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Plant defense; Reference proteome.
FT CHAIN 1..428
FT /note="Nematode resistance protein-like HSPRO1"
FT /id="PRO_0000412196"
FT CONFLICT 126
FT /note="E -> D (in Ref. 5; AAM62622)"
FT /evidence="ECO:0000305"
FT CONFLICT 131
FT /note="A -> S (in Ref. 5; AAM62622)"
FT /evidence="ECO:0000305"
FT CONFLICT 142
FT /note="S -> C (in Ref. 5; AAM62622)"
FT /evidence="ECO:0000305"
FT CONFLICT 156
FT /note="V -> I (in Ref. 5; AAM62622)"
FT /evidence="ECO:0000305"
FT CONFLICT 222
FT /note="S -> I (in Ref. 5; AAM62622)"
FT /evidence="ECO:0000305"
FT CONFLICT 364
FT /note="S -> T (in Ref. 1; ABA12452)"
FT /evidence="ECO:0000305"
FT CONFLICT 382
FT /note="G -> E (in Ref. 5; AAM62622)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 428 AA; 48788 MW; 278D0A023953D07A CRC64;
MADLDLQRKM VSPKLHVTIP EPCKLSSVSS PISSSSSAAC SAYELYLRLP ELRNLWSSLY
FPHWISEPVL KPALQALEIT FRLILTVASD TRPYINRREW IRRLDSLTTS QIKIVAAICG
DEDNYEENVS AAPVSNGWSS LSLLSEIATC RTSESVGQKI LSTIENEMRW CKYTLGLGEP
NLAGKPYLQY DAVCLPEELH SLKNNPYADH IENQENQMLY TSHQILESWI YVSVNLLYRI
ESRIEEGKFE KASSDVYLLE RIWKLLSEIE DLHILMDPED FLKVKKQLQI KSTFPNDAFC
FRSKGLVEMA KMSKELRQKV PAVLEVEVDP TGGPRLQEAA MKLYSRKTEY EKIHLLQGMQ
AVESAAKRFF FGYQKLVAAM IGNAEANANR TVANHESYDS LTQVFMEPPY YPSLDAAKTF
LGEFWSQL
