SOK3_ARATH
ID SOK3_ARATH Reviewed; 540 AA.
AC Q8GYT8; Q9ZUV7;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 121.
DE RecName: Full=Protein SOSEKI 3 {ECO:0000303|PubMed:30737509};
DE Short=AtSOK3 {ECO:0000303|PubMed:32004461};
GN Name=SOK3 {ECO:0000303|PubMed:30737509};
GN OrderedLocusNames=At2g28150 {ECO:0000312|Araport:AT2G28150};
GN ORFNames=F24D13.6 {ECO:0000312|EMBL:AEC08085.1};
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=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;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND TISSUE
RP SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=30737509; DOI=10.1038/s41477-019-0363-6;
RA Yoshida S., van der Schuren A., van Dop M., van Galen L., Saiga S.,
RA Adibi M., Moeller B., Ten Hove C.A., Marhavy P., Smith R., Friml J.,
RA Weijers D.;
RT "A SOSEKI-based coordinate system interprets global polarity cues in
RT Arabidopsis.";
RL Nat. Plants 5:160-166(2019).
RN [7]
RP FUNCTION, INTERACTION WITH ANGUSTIFOLIA, SUBUNIT, AND GENE FAMILY.
RX PubMed=32004461; DOI=10.1016/j.cell.2020.01.011;
RA van Dop M., Fiedler M., Mutte S., de Keijzer J., Olijslager L.,
RA Albrecht C., Liao C.Y., Janson M.E., Bienz M., Weijers D.;
RT "DIX domain polymerization drives assembly of plant cell polarity
RT complexes.";
RL Cell 180:427.e12-439.e12(2020).
CC -!- FUNCTION: SOSEKI proteins (SOK1-5) locally interpret global polarity
CC cues and can influence cell division orientation to coordinate cell
CC polarization relative to body axes, probably by guiding ANGUSTIFOLIA
CC (AN) polarized localization. {ECO:0000269|PubMed:30737509}.
CC -!- SUBUNIT: Homodimer (By similarity). Forms long polymer filaments with
CC other SOKs proteins polymers (e.g. SOK1, SOK2, SOK3 and SOK4) crucial
CC for polar localization and biological activity (PubMed:32004461). Binds
CC to ANGUSTIFOLIA (AN) (PubMed:32004461). {ECO:0000250|UniProtKB:Q9SYJ8,
CC ECO:0000269|PubMed:32004461}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:30737509};
CC Peripheral membrane protein {ECO:0000269|PubMed:30737509}; Cytoplasmic
CC side {ECO:0000269|PubMed:30737509}. Note=SOSEKI proteins integrate
CC apical-basal and radial organismal axes to localize to polar cell
CC edges. {ECO:0000269|PubMed:30737509}.
CC -!- TISSUE SPECIFICITY: Expressed during embryogenesis and in roots.
CC {ECO:0000269|PubMed:30737509}.
CC -!- DEVELOPMENTAL STAGE: Accumulates at the basal side and all corners of
CC most cells in the primary root, lateral roots and embryos.
CC {ECO:0000269|PubMed:30737509}.
CC -!- DOMAIN: The DIX-like oligomerization domain is required for
CC polymerization, edge localization and biological activity.
CC {ECO:0000250|UniProtKB:Q9SYJ8}.
CC -!- MISCELLANEOUS: 'Soseki' means cornerstone in Japanese.
CC {ECO:0000303|PubMed:30737509}.
CC -!- SIMILARITY: Belongs to the SOSEKI family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC98451.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC005851; AAC98451.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC08085.1; -; Genomic_DNA.
DR EMBL; AK117392; BAC42061.1; -; mRNA.
DR EMBL; BT006130; AAP04115.1; -; mRNA.
DR PIR; D84681; D84681.
DR RefSeq; NP_180382.2; NM_128375.4.
DR AlphaFoldDB; Q8GYT8; -.
DR SMR; Q8GYT8; -.
DR STRING; 3702.AT2G28150.1; -.
DR PaxDb; Q8GYT8; -.
DR PRIDE; Q8GYT8; -.
DR ProteomicsDB; 187545; -.
DR EnsemblPlants; AT2G28150.1; AT2G28150.1; AT2G28150.
DR GeneID; 817361; -.
DR Gramene; AT2G28150.1; AT2G28150.1; AT2G28150.
DR KEGG; ath:AT2G28150; -.
DR Araport; AT2G28150; -.
DR TAIR; locus:2046213; AT2G28150.
DR eggNOG; ENOG502QTBW; Eukaryota.
DR HOGENOM; CLU_025038_1_0_1; -.
DR InParanoid; Q8GYT8; -.
DR OrthoDB; 543876at2759; -.
DR PhylomeDB; Q8GYT8; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q8GYT8; baseline and differential.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:1905392; P:plant organ morphogenesis; IMP:UniProtKB.
DR GO; GO:0051258; P:protein polymerization; IDA:UniProtKB.
DR GO; GO:0051302; P:regulation of cell division; IMP:UniProtKB.
DR GO; GO:2000067; P:regulation of root morphogenesis; IMP:UniProtKB.
DR GO; GO:0090708; P:specification of plant organ axis polarity; IMP:UniProtKB.
DR InterPro; IPR010369; SOK.
DR InterPro; IPR021182; SOK_magnoliopsida.
DR PANTHER; PTHR31083; PTHR31083; 1.
DR Pfam; PF06136; SOK2_plant; 1.
DR PIRSF; PIRSF031043; UCP031043; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Cell membrane; Developmental protein; Membrane;
KW Reference proteome.
FT CHAIN 1..540
FT /note="Protein SOSEKI 3"
FT /id="PRO_0000452142"
FT REGION 32..123
FT /note="DIX-like oligomerization domain"
FT /evidence="ECO:0000250|UniProtKB:Q9SYJ8"
FT REGION 147..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 219..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 412..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 342..343
FT /note="Association to cell membranes"
FT /evidence="ECO:0000250|UniProtKB:Q9SYJ8"
FT COMPBIAS 147..168
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..201
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..247
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 278..294
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..467
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 540 AA; 60084 MW; E8AEA04669C745BD CRC64;
MEARMKKYSR EVSPERAKVW TEKSPKYHQK IKKVQIVYYL SKNRQLEHPH FMEVLISSPN
GLYLRDVIER LNVLRGRGMA SMYSWSSKRS YRNGFVWHDL SEDDLILPAN GNEYVLKGSE
LFDESNSDHF SPIVNLATQN MKQIVVEPPS SRSMDDSSSS SSMNNGKGTN KHSHEDDELS
PPALRSVSSS GVSPDSRDAK NSSSWCLAEY KVYKSEGLAD ASTQTDETVS GRSKTPIETF
SRGVSTDEDV SSEPETSENN LVSEASCAGK ERESAEISRN SVSPPFSNSA SSLGGKTDTL
ESLIRADVSK MNSFRILEQE DVRMPAIPRL RASNMLMQLI SCGSISVKDN NFGLVPTYKP
KFGHSKFPSP FFSSSFMMGD LDRLSETPSL MGLRMEEKEY FSGSLVETKL QKKDAADSNA
SLKRSSSYNG DRASNQMGVA ENGDSKPDSS KNNPSSRKAS SILGKQQPLV SEKRRDSSED
TTKNIPCTTK THDACSKRIT ESLRKPDSFR EDEERVIKID ERLASGARVR IESKVPSEEP
