PRN1_ARATH
ID PRN1_ARATH Reviewed; 287 AA.
AC Q9LX49;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Pirin-1;
DE AltName: Full=AtPirin1;
GN Name=PRN1; OrderedLocusNames=At3g59220; ORFNames=F25L23_80;
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].
RC STRAIN=cv. Columbia;
RA Zilberman D., Jacobsen S.E.;
RT "Pirin, a highly conserved protein essential for Arabidopsis development,
RT interacts with the MET1/DNMT1 class of DNA methyltransferases.";
RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
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 CHARACTERIZATION, AND INTERACTION WITH GPA1.
RC STRAIN=cv. Wassilewskija;
RX PubMed=12837948; DOI=10.1105/tpc.011890;
RA Lapik Y.R., Kaufman L.S.;
RT "The Arabidopsis cupin domain protein AtPirin1 interacts with the G protein
RT alpha-subunit GPA1 and regulates seed germination and early seedling
RT development.";
RL Plant Cell 15:1578-1590(2003).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH NFYB6 AND NFYB9.
RC STRAIN=cv. Columbia, and cv. Wassilewskija;
RX PubMed=17322342; DOI=10.1104/pp.106.089904;
RA Warpeha K.M., Upadhyay S., Yeh J., Adamiak J., Hawkins S.I., Lapik Y.R.,
RA Anderson M.B., Kaufman L.S.;
RT "The GCR1, GPA1, PRN1, NF-Y signal chain mediates both blue light and
RT abscisic acid responses in Arabidopsis.";
RL Plant Physiol. 143:1590-1600(2007).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: Involved in abscisic acid signal transduction. Plays a role
CC in seed germination and early seedling development. Involved in the
CC blue light (BL) signaling. {ECO:0000269|PubMed:17322342}.
CC -!- SUBUNIT: Interacts with the G protein alpha-1 subunit GPA1. Interacts
CC with NFYB6 and NFYB9. {ECO:0000269|PubMed:12837948,
CC ECO:0000269|PubMed:17322342}.
CC -!- INTERACTION:
CC Q9LX49; P18064: GPA1; NbExp=3; IntAct=EBI-1606661, EBI-443890;
CC Q9LX49; O04027: NFYB4; NbExp=2; IntAct=EBI-1606661, EBI-1751677;
CC Q9LX49; Q84W66: NFYB6; NbExp=2; IntAct=EBI-1606661, EBI-1751693;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: Present at similar levels in seedlings and mature
CC plants.
CC -!- INDUCTION: Up-regulated by abscisic acid (ABA) and low-fluence red
CC light, but not by low-fluence blue light.
CC -!- DOMAIN: Contains one cupin domain that is not required for interaction
CC with the G protein alpha subunit.
CC -!- DISRUPTION PHENOTYPE: Altered response to blue light (BL) and abscisic
CC acid (ABA). {ECO:0000269|PubMed:17322342}.
CC -!- SIMILARITY: Belongs to the pirin family. {ECO:0000305}.
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DR EMBL; AF353716; AAL83949.1; -; mRNA.
DR EMBL; AL356014; CAB91592.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79893.1; -; Genomic_DNA.
DR PIR; T48990; T48990.
DR RefSeq; NP_191481.1; NM_115784.3.
DR AlphaFoldDB; Q9LX49; -.
DR SMR; Q9LX49; -.
DR BioGRID; 10406; 22.
DR IntAct; Q9LX49; 4.
DR STRING; 3702.AT3G59220.1; -.
DR iPTMnet; Q9LX49; -.
DR PaxDb; Q9LX49; -.
DR PRIDE; Q9LX49; -.
DR ProteomicsDB; 234707; -.
DR DNASU; 825091; -.
DR EnsemblPlants; AT3G59220.1; AT3G59220.1; AT3G59220.
DR GeneID; 825091; -.
DR Gramene; AT3G59220.1; AT3G59220.1; AT3G59220.
DR KEGG; ath:AT3G59220; -.
DR Araport; AT3G59220; -.
DR TAIR; locus:2081187; AT3G59220.
DR eggNOG; ENOG502QQ5A; Eukaryota.
DR HOGENOM; CLU_045717_5_2_1; -.
DR InParanoid; Q9LX49; -.
DR OMA; AIQAHHV; -.
DR OrthoDB; 1328043at2759; -.
DR PhylomeDB; Q9LX49; -.
DR PRO; PR:Q9LX49; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LX49; baseline and differential.
DR Genevisible; Q9LX49; AT.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IMP:UniProtKB.
DR GO; GO:0009785; P:blue light signaling pathway; IMP:UniProtKB.
DR GO; GO:0009737; P:response to abscisic acid; IMP: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 Abscisic acid signaling pathway; Acetylation; Nucleus; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..287
FT /note="Pirin-1"
FT /id="PRO_0000214054"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0007744|PubMed:22223895"
SQ SEQUENCE 287 AA; 31603 MW; F44ACE2F98208B1E CRC64;
MTYENNSVPR IVIKKVLAKL EKEGEGAVVR NGITKIDQKL LDPFVLLVEF SFSLSAGFPD
HPHRGFESVT YMLQGGIIHK DPKGHKGTIQ AGDVQWMTAG RGIIHSEFPE EEVNNGLQLW
INLPSTEKMT EPKYKELSSL DIPRAEENGV EVKVIAGDSM GIKSPVYTRT PTMFLDFTLK
PGSQTHQTVP ESWTAFAYII EGDEGVFGSL NSSAISAHHV VVFGPGDLVS VWNKSTSRSL
RFLLIAGEPI GEPVVQCGPF VMNSQAEIDM AFDDYQNAKN GFEMAKC
