PRNL2_ARATH
ID PRNL2_ARATH Reviewed; 321 AA.
AC Q9ZW82; Q0WQ94;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 3.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Pirin-like protein 2 {ECO:0000305};
DE AltName: Full=PIRIN2 {ECO:0000303|PubMed:24947605};
DE AltName: Full=Pirin-like protein At2g43120 {ECO:0000305};
GN Name=PRN2 {ECO:0000303|PubMed:24947605}; OrderedLocusNames=At2g43120;
GN ORFNames=F14B2.6;
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=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 [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;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Bautista V.R., Kim C.J., Chen H., Quinitio C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, INTERACTION WITH RD21A; RD21B AND XCP2, SUBCELLULAR LOCATION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=24947605; DOI=10.1111/tpj.12602;
RA Zhang B., Tremousaygue D., Denance N., van Esse H.P., Hoerger A.C.,
RA Dabos P., Goffner D., Thomma B.P., van der Hoorn R.A., Tuominen H.;
RT "PIRIN2 stabilizes cysteine protease XCP2 and increases susceptibility to
RT the vascular pathogen Ralstonia solanacearum in Arabidopsis.";
RL Plant J. 79:1009-1019(2014).
CC -!- FUNCTION: Involved in susceptibility to the bacterial plant pathogen
CC Ralstonia solanacearum. Stabilizes the xylem cysteine protease XCP2 by
CC blocking its autolysis. {ECO:0000269|PubMed:24947605}.
CC -!- SUBUNIT: Interacts with RD21A, RD21B and XCP2.
CC {ECO:0000269|PubMed:24947605}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:24947605}.
CC Nucleus {ECO:0000269|PubMed:24947605}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but mutant plants show increased resistance to infection by
CC the bacterial wilt pathogen Ralstonia solanacearum.
CC {ECO:0000269|PubMed:24947605}.
CC -!- SIMILARITY: Belongs to the pirin family. {ECO:0000305}.
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DR EMBL; AC004450; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002685; AEC10211.1; -; Genomic_DNA.
DR EMBL; AK228809; BAF00705.1; -; mRNA.
DR EMBL; BT029512; ABL66768.1; -; mRNA.
DR PIR; C84862; C84862.
DR RefSeq; NP_850385.1; NM_180054.2.
DR AlphaFoldDB; Q9ZW82; -.
DR SMR; Q9ZW82; -.
DR BioGRID; 4251; 2.
DR STRING; 3702.AT2G43120.1; -.
DR PaxDb; Q9ZW82; -.
DR PRIDE; Q9ZW82; -.
DR ProteomicsDB; 234849; -.
DR EnsemblPlants; AT2G43120.1; AT2G43120.1; AT2G43120.
DR GeneID; 818914; -.
DR Gramene; AT2G43120.1; AT2G43120.1; AT2G43120.
DR KEGG; ath:AT2G43120; -.
DR Araport; AT2G43120; -.
DR TAIR; locus:2041026; AT2G43120.
DR eggNOG; ENOG502QQ5A; Eukaryota.
DR HOGENOM; CLU_045717_5_2_1; -.
DR InParanoid; Q9ZW82; -.
DR PhylomeDB; Q9ZW82; -.
DR PRO; PR:Q9ZW82; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZW82; baseline and differential.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030414; F:peptidase inhibitor activity; IDA:TAIR.
DR GO; GO:0042742; P:defense response to bacterium; IGI:TAIR.
DR Gene3D; 2.60.120.10; -; 2.
DR InterPro; IPR012093; Pirin.
DR InterPro; IPR008778; Pirin_C_dom.
DR InterPro; IPR003829; Pirin_N_dom.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR011051; RmlC_Cupin_sf.
DR PANTHER; PTHR13903; PTHR13903; 1.
DR Pfam; PF02678; Pirin; 1.
DR Pfam; PF05726; Pirin_C; 1.
DR PIRSF; PIRSF006232; Pirin; 1.
DR SUPFAM; SSF51182; SSF51182; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Iron; Metal-binding; Nucleus; Plant defense; Reference proteome.
FT CHAIN 1..321
FT /note="Pirin-like protein 2"
FT /id="PRO_0000214056"
FT BINDING 88
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:O00625"
FT BINDING 90
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:O00625"
FT BINDING 132
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:O00625"
FT BINDING 134
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:O00625"
SQ SEQUENCE 321 AA; 35538 MW; D164410400832893 CRC64;
MRAAINRANS LGGLFSFRFI RNIKSMSSST SQDFVSRPVI KKVFAKLQKE GDGAVVRRGI
SRSEQKLLDP FLMLDEFSVS PPAGFPDHPH RGFETVTYVL EGGITHQDFK GHKGTIYAGD
VQWMTAGRGI IHSEMPEEEV NKGLQLWINL SSNEKMIEPN YQELSHSDIP KAEQNGVEVK
VIAGESMGIQ SPVYTRTPTM FLDFTLQPGA QIHQNVPESW NAFAYILESG EGGGVFSSSN
SSPIPAHSVV VFGPGNDGVS VWNKSSSKQL RFVLIAGEPI GEPVVQYGPF VMNTQAEIDM
TIEDYHYGKN GFEMAKYWRS Q
