ID D7MJY1_ARALL Unreviewed; 258 AA.
AC D7MJY1;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 13-SEP-2023, entry version 63.
DE RecName: Full=14-3-3 domain-containing protein {ECO:0000259|SMART:SM00101};
GN ORFNames=ARALYDRAFT_494127 {ECO:0000313|EMBL:EFH47097.1};
OS Arabidopsis lyrata subsp. lyrata (Lyre-leaved rock-cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=81972 {ECO:0000313|Proteomes:UP000008694};
RN [1] {ECO:0000313|Proteomes:UP000008694}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. MN47 {ECO:0000313|Proteomes:UP000008694};
RX PubMed=21478890; DOI=10.1038/ng.807;
RA Hu T.T., Pattyn P., Bakker E.G., Cao J., Cheng J.-F., Clark R.M.,
RA Fahlgren N., Fawcett J.A., Grimwood J., Gundlach H., Haberer G.,
RA Hollister J.D., Ossowski S., Ottilar R.P., Salamov A.A., Schneeberger K.,
RA Spannagl M., Wang X., Yang L., Nasrallah M.E., Bergelson J.,
RA Carrington J.C., Gaut B.S., Schmutz J., Mayer K.F.X., Van de Peer Y.,
RA Grigoriev I.V., Nordborg M., Weigel D., Guo Y.-L.;
RT "The Arabidopsis lyrata genome sequence and the basis of rapid genome size
RT change.";
RL Nat. Genet. 43:476-481(2011).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the 14-3-3 family.
CC {ECO:0000256|ARBA:ARBA00006141, ECO:0000256|RuleBase:RU003466}.
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DR EMBL; GL348719; EFH47097.1; -; Genomic_DNA.
DR RefSeq; XP_002870838.1; XM_002870792.1.
DR AlphaFoldDB; D7MJY1; -.
DR STRING; 81972.D7MJY1; -.
DR EnsemblPlants; fgenesh2_kg.7__3560__AT5G38480.1; fgenesh2_kg.7__3560__AT5G38480.1; fgenesh2_kg.7__3560__AT5G38480.1.
DR Gramene; fgenesh2_kg.7__3560__AT5G38480.1; fgenesh2_kg.7__3560__AT5G38480.1; fgenesh2_kg.7__3560__AT5G38480.1.
DR eggNOG; KOG0841; Eukaryota.
DR HOGENOM; CLU_058290_0_0_1; -.
DR OrthoDB; 920089at2759; -.
DR Proteomes; UP000008694; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:EnsemblPlants.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0006995; P:cellular response to nitrogen starvation; IEA:EnsemblPlants.
DR GO; GO:0016036; P:cellular response to phosphate starvation; IEA:EnsemblPlants.
DR GO; GO:0051365; P:cellular response to potassium ion starvation; IEA:EnsemblPlants.
DR GO; GO:0009631; P:cold acclimation; IEA:EnsemblPlants.
DR GO; GO:0019222; P:regulation of metabolic process; IEA:EnsemblPlants.
DR GO; GO:0050826; P:response to freezing; IEA:EnsemblPlants.
DR Gene3D; 1.20.190.20; 14-3-3 domain; 1.
DR InterPro; IPR000308; 14-3-3.
DR InterPro; IPR023409; 14-3-3_CS.
DR InterPro; IPR036815; 14-3-3_dom_sf.
DR InterPro; IPR023410; 14-3-3_domain.
DR PANTHER; PTHR18860; 14-3-3 PROTEIN; 1.
DR PANTHER; PTHR18860:SF95; 14-3-3-LIKE PROTEIN GF14 PSI; 1.
DR Pfam; PF00244; 14-3-3; 1.
DR PIRSF; PIRSF000868; 14-3-3; 1.
DR PRINTS; PR00305; 1433ZETA.
DR SMART; SM00101; 14_3_3; 1.
DR SUPFAM; SSF48445; 14-3-3 protein; 1.
DR PROSITE; PS00796; 1433_1; 1.
DR PROSITE; PS00797; 1433_2; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000008694}.
FT DOMAIN 7..250
FT /note="14-3-3"
FT /evidence="ECO:0000259|SMART:SM00101"
FT COILED 13..40
FT /evidence="ECO:0000256|SAM:Coils"
FT SITE 62
FT /note="Interaction with phosphoserine on interacting
FT protein"
FT /evidence="ECO:0000256|PIRSR:PIRSR000868-1"
FT SITE 135
FT /note="Interaction with phosphoserine on interacting
FT protein"
FT /evidence="ECO:0000256|PIRSR:PIRSR000868-1"
SQ SEQUENCE 258 AA; 28893 MW; 0222762DF3CE8642 CRC64;
MSTEASREEN VYMAKLAEQA ERYEEMVEFM EKVAKTVDAE ELSVEERNLL SVAYKNVIGA
RRASWRIISS IEQKEESKGN EDHVAIIKDY RGKIETELSK ICDGILNVLE AHLIPSASPA
ESKVFYLKMK GDYHRYLAEF KAGAERKEAA ESTLVAYKSA SDIATAELAP THPIRLGLAL
NFSVFYYEIL NSPDRACSLA KQAFDDAIAE LDTLGEESYK DSTLIMQLLR DNLTLWTSDM
TDEAGDEIKE ASKPEGAE
//