PIA2_ARATH
ID PIA2_ARATH Reviewed; 174 AA.
AC Q9FNP4;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Phytochrome-interacting ankyrin-repeat protein 2 {ECO:0000303|PubMed:21395597};
DE Contains:
DE RecName: Full=Protein ANKYRIN REPEAT 6, mitochondrial {ECO:0000303|PubMed:21123745};
GN Name=PIA2 {ECO:0000303|PubMed:21395597};
GN Synonyms=ANK6 {ECO:0000303|PubMed:21123745};
GN OrderedLocusNames=At5g61230 {ECO:0000312|Araport:AT5G61230};
GN ORFNames=MAF19.22 {ECO:0000312|EMBL:BAB10384.1};
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=9405937; DOI=10.1093/dnares/4.4.291;
RA Kotani H., Nakamura Y., Sato S., Kaneko T., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. II. Sequence
RT features of the regions of 1,044,062 bp covered by thirteen physically
RT assigned P1 clones.";
RL DNA Res. 4:291-300(1997).
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 FUNCTION, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION,
RP INTERACTION WITH SIGE/SIG5, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=21123745; DOI=10.1073/pnas.1015911107;
RA Yu F., Shi J., Zhou J., Gu J., Chen Q., Li J., Cheng W., Mao D., Tian L.,
RA Buchanan B.B., Li L., Chen L., Li D., Luan S.;
RT "ANK6, a mitochondrial ankyrin repeat protein, is required for male-female
RT gamete recognition in Arabidopsis thaliana.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:22332-22337(2010).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, PHOSPHORYLATION BY PHYA, INTERACTION WITH
RP PHYA, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Columbia;
RX PubMed=21395597; DOI=10.1111/j.1399-3054.2011.01468.x;
RA Yoo J., Shin D.H., Cho M.-H., Kim T.-L., Bhoo S.H., Hahn T.-R.;
RT "An ankyrin repeat protein is involved in anthocyanin biosynthesis in
RT Arabidopsis.";
RL Physiol. Plantarum 142:314-325(2011).
RN [6]
RP FUNCTION, MUTAGENESIS OF SER-10; ARG-13; SER-15 AND PHE-16, INTERACTION
RP WITH PIF3 AND PHYA, AND PHOSPHORYLATION AT SER-15 BY PHYA.
RC STRAIN=cv. Columbia;
RX PubMed=27143545; DOI=10.1093/jb/mvw031;
RA Yoo J., Cho M.-H., Lee S.-W., Bhoo S.H.;
RT "Phytochrome-interacting ankyrin repeat protein 2 modulates phytochrome A-
RT mediated PIF3 phosphorylation in light signal transduction.";
RL J. Biochem. 160:243-249(2016).
RN [7]
RP INTERACTION WITH RPS9M, AND SUBCELLULAR LOCATION.
RX PubMed=29312411; DOI=10.3389/fpls.2017.02171;
RA Lu C., Yu F., Tian L., Huang X., Tan H., Xie Z., Hao X., Li D., Luan S.,
RA Chen L.;
RT "RPS9M, a mitochondrial ribosomal protein, is essential for central cell
RT maturation and endosperm development in Arabidopsis.";
RL Front. Plant Sci. 8:2171-2171(2017).
CC -!- FUNCTION: Promotes anthocyanin accumulation through interaction with
CC PHYA, especially in response to far-red light, high light and sucrose
CC treatment, probably by triggering A3G2XYLT/UF3GT expression
CC (PubMed:21395597, PubMed:27143545). Required for gametophytes
CC development as well as male-female gamete recognition during
CC fertilization, possibly by regulating mitochondrial gene expression
CC (PubMed:21123745). Represses PHYA-mediated PIF3 phosphorylation
CC (PubMed:27143545). {ECO:0000269|PubMed:21123745,
CC ECO:0000269|PubMed:21395597, ECO:0000269|PubMed:27143545}.
CC -!- SUBUNIT: Interacts with phytochrome A (PHYA), both in Pr and Pfr forms
CC (PubMed:21395597, PubMed:27143545). Binds to PIF3, a repressor of
CC photomorphogenesis in response to phytochrome-mediated light signaling;
CC this interaction may trigger the repression of PHYA-mediated PIF3
CC phosphorylation (PubMed:27143545). Interacts with SIGE/SIG5 in
CC mitochondrion (PubMed:21123745). Interacts with RPS9M (via C terminus)
CC (PubMed:29312411). {ECO:0000269|PubMed:21123745,
CC ECO:0000269|PubMed:21395597, ECO:0000269|PubMed:27143545,
CC ECO:0000269|PubMed:29312411}.
CC -!- INTERACTION:
CC Q9FNP4; O81313: IND; NbExp=3; IntAct=EBI-4435148, EBI-4446992;
CC Q9FNP4; O23160: MYB73; NbExp=3; IntAct=EBI-4435148, EBI-25506855;
CC Q9FNP4; Q9ZNX9: SIGE; NbExp=4; IntAct=EBI-4435148, EBI-15343551;
CC -!- SUBCELLULAR LOCATION: [Phytochrome-interacting ankyrin-repeat protein
CC 2]: Cytoplasm {ECO:0000269|PubMed:21395597}. Nucleus
CC {ECO:0000269|PubMed:21123745, ECO:0000269|PubMed:21395597}.
CC -!- SUBCELLULAR LOCATION: [Protein ANKYRIN REPEAT 6, mitochondrial]:
CC Mitochondrion {ECO:0000269|PubMed:21123745,
CC ECO:0000269|PubMed:29312411}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in flowers, cotyledons, leaves and
CC siliques, and, to a lower extent, in roots and stems (PubMed:21123745,
CC PubMed:21395597). Also detected at low levels in seedlings grown in
CC continuous dark or light conditions (PubMed:21395597). Expressed in
CC male and female gametophytes (PubMed:21123745).
CC {ECO:0000269|PubMed:21123745, ECO:0000269|PubMed:21395597}.
CC -!- DEVELOPMENTAL STAGE: Levels in leaves diminishes after transition from
CC the vegetative to the reproductive phase. Accumulates strongly in
CC developmental tissues (PubMed:21395597). Highly expressed in the male
CC (e.g. pollen grains and pollen tubes) and female (e.g. synergids, egg
CC cell and central cell) gametophytes before and during, but not after
CC fertilization. In fertilized ovules, levels decrease rapidely to become
CC undetectable at the stage before the first division of the endosperm
CC (PubMed:21123745). {ECO:0000269|PubMed:21123745,
CC ECO:0000269|PubMed:21395597}.
CC -!- PTM: Phosphorylated by PHYA. {ECO:0000269|PubMed:21395597,
CC ECO:0000269|PubMed:27143545}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethality in homozygous mutant. In
CC heterozygous plants, impaired male-female gamete recognition when
CC pollen of ank6 mutant is placed on ank6 female gamete. Defects in
CC female gametophyte development at the one-nucleate stage
CC (PubMed:21123745). Abnormal hypocotyls length. Reduced accumulation of
CC anthocyanin in seedlings grown under far-red light, in response to high
CC light and after sucrose treatment, associated with lower levels of the
CC UDP-flavonoid-3'-glucosyl-transferase (A3G2XYLT/UF3GT), a major enzyme
CC in the anthocyanin biosynthesis processes (PubMed:21395597).
CC {ECO:0000269|PubMed:21123745, ECO:0000269|PubMed:21395597}.
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DR EMBL; AB006696; BAB10384.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97439.1; -; Genomic_DNA.
DR EMBL; AY039615; AAK62670.1; -; mRNA.
DR EMBL; AY078023; AAL77724.1; -; mRNA.
DR RefSeq; NP_200931.1; NM_125516.4.
DR AlphaFoldDB; Q9FNP4; -.
DR SMR; Q9FNP4; -.
DR DIP; DIP-60439N; -.
DR IntAct; Q9FNP4; 14.
DR STRING; 3702.AT5G61230.1; -.
DR iPTMnet; Q9FNP4; -.
DR PaxDb; Q9FNP4; -.
DR PRIDE; Q9FNP4; -.
DR EnsemblPlants; AT5G61230.1; AT5G61230.1; AT5G61230.
DR GeneID; 836244; -.
DR Gramene; AT5G61230.1; AT5G61230.1; AT5G61230.
DR KEGG; ath:AT5G61230; -.
DR Araport; AT5G61230; -.
DR TAIR; locus:2159456; AT5G61230.
DR eggNOG; KOG0504; Eukaryota.
DR HOGENOM; CLU_000134_45_8_1; -.
DR InParanoid; Q9FNP4; -.
DR OMA; LPDDMYD; -.
DR OrthoDB; 1514637at2759; -.
DR PhylomeDB; Q9FNP4; -.
DR PRO; PR:Q9FNP4; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FNP4; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0010313; F:phytochrome binding; IDA:UniProtKB.
DR GO; GO:0009567; P:double fertilization forming a zygote and endosperm; IMP:TAIR.
DR GO; GO:0009553; P:embryo sac development; IMP:TAIR.
DR GO; GO:0080173; P:male-female gamete recognition during double fertilization forming a zygote and endosperm; IMP:TAIR.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; IMP:UniProtKB.
DR GO; GO:0031542; P:positive regulation of anthocyanin biosynthetic process; IMP:UniProtKB.
DR GO; GO:0010218; P:response to far red light; IMP:UniProtKB.
DR GO; GO:0009644; P:response to high light intensity; IMP:UniProtKB.
DR GO; GO:0009744; P:response to sucrose; IMP:UniProtKB.
DR Gene3D; 1.25.40.20; -; 2.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR Pfam; PF12796; Ank_2; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 3.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 3.
PE 1: Evidence at protein level;
KW ANK repeat; Cytoplasm; Mitochondrion; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..174
FT /note="Phytochrome-interacting ankyrin-repeat protein 2"
FT /id="PRO_0000439866"
FT CHAIN 23..174
FT /note="Protein ANKYRIN REPEAT 6, mitochondrial"
FT /id="PRO_0000439867"
FT REPEAT 28..57
FT /note="ANK 1"
FT /evidence="ECO:0000255"
FT REPEAT 65..94
FT /note="ANK 2"
FT /evidence="ECO:0000255"
FT REPEAT 100..129
FT /note="ANK 3"
FT /evidence="ECO:0000255"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:27143545"
FT MUTAGEN 10
FT /note="S->A: Normal phosphorylation by PHYA, normal
FT repression of PHYA-mediated PIF3 phosphorylation, and
FT normal interaction with PHYA."
FT /evidence="ECO:0000269|PubMed:27143545"
FT MUTAGEN 13
FT /note="R->P: Abolished phosphorylation by PHYA. Impaired
FT repression of PHYA-mediated PIF3 phosphorylation. Normal
FT interaction with PHYA, but decreased interaction with PIF3.
FT In plants lacking PIF3, reduced anthocyanin accumulation in
FT seedlings grown under far-red light."
FT /evidence="ECO:0000269|PubMed:27143545"
FT MUTAGEN 15
FT /note="S->A: Impaired phosphorylation by PHYA. Normal
FT repression of PHYA-mediated PIF3 phosphorylation, and
FT normal interaction with PHYA."
FT /evidence="ECO:0000269|PubMed:27143545"
FT MUTAGEN 16
FT /note="F->P: Abolished phosphorylation by PHYA. Impaired
FT repression of PHYA-mediated PIF3 phosphorylation. Normal
FT interaction with PHYA, but decreased interaction with PIF3.
FT In plants lacking PIF3, reduced anthocyanin accumulation in
FT seedlings grown under far-red light."
FT /evidence="ECO:0000269|PubMed:27143545"
SQ SEQUENCE 174 AA; 19207 MW; 22970E70A40A2966 CRC64;
MLQEPSAAFS LRRNSFRRRS PRSNVDDRGW NPLHIKARKG DLKSVKQLLD QGMDVNALAW
GPKSKGVSAL HLAAEGGHIE VMDLLLERGA NIDAKTWGSC GWTPLHAAAK ERKREAVKFL
VENGAFLADD ITDTRFNPPV HYCHGLEWAY EEMKKLNSES SSSSGGDTSS SSDN
