SOK1_ARATH
ID SOK1_ARATH Reviewed; 372 AA.
AC Q9SYJ8;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Protein SOSEKI 1 {ECO:0000303|PubMed:30737509};
DE Short=AtSOK1 {ECO:0000303|PubMed:32004461};
GN Name=SOK1 {ECO:0000303|PubMed:30737509};
GN OrderedLocusNames=At1g05577 {ECO:0000312|Araport:AT1G05577};
GN ORFNames=F3F20.2 {ECO:0000312|EMBL:AAD30611.1};
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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=16244158; DOI=10.1104/pp.105.063479;
RA Xiao Y.-L., Smith S.R., Ishmael N., Redman J.C., Kumar N., Monaghan E.L.,
RA Ayele M., Haas B.J., Wu H.C., Town C.D.;
RT "Analysis of the cDNAs of hypothetical genes on Arabidopsis chromosome 2
RT reveals numerous transcript variants.";
RL Plant Physiol. 139:1323-1337(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Underwood B.A., Xiao Y.-L., Moskal W.A. Jr., Monaghan E.L., Wang W.,
RA Redman J.C., Wu H.C., Utterback T., Town C.D.;
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY,
RP INDUCTION, DOMAIN, AND SUBUNIT.
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 [6]
RP FUNCTION, MUTAGENESIS OF HIS-29; ASP-78; CYS-233; GLY-234 AND
RP 307-CYS--CYS-310, SUBUNIT, INTERACTION WITH ANGUSTIFOLIA, 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 ECO:0000269|PubMed:32004461}.
CC -!- SUBUNIT: Homodimer (PubMed:30737509). 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:0000269|PubMed:30737509,
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 (SOK1-5)
CC integrate apical-basal and radial organismal axes to localize to polar
CC cell edges in roots, pointing towards the endodermis, mainly to inner
CC apical edges. {ECO:0000269|PubMed:30737509,
CC ECO:0000269|PubMed:32004461}.
CC -!- TISSUE SPECIFICITY: Expressed during embryogenesis and in roots.
CC {ECO:0000269|PubMed:30737509}.
CC -!- DEVELOPMENTAL STAGE: During embryogenesis, first observed in the apical
CC side of lower tier inner cells at the early globular stage
CC (PubMed:30737509). At transition to heart stage and later in the post-
CC embryonic root and lateral roots, accumulates at the outer apical
CC corner or outer lateral side of young vascular cells, including the
CC pericycle, and outer corners of the hypophysis (PubMed:30737509). Also
CC present in the columella root cap of the primary root
CC (PubMed:30737509). {ECO:0000269|PubMed:30737509}.
CC -!- INDUCTION: Highly unstable; disappears during cell division but is
CC afterwards quickly re-established in lateral root primordia and primary
CC root (at the protein level). {ECO:0000269|PubMed:30737509}.
CC -!- DOMAIN: The DIX-like oligomerization domain is required for
CC polymerization, edge localization and biological activity.
CC {ECO:0000269|PubMed:30737509}.
CC -!- MISCELLANEOUS: 'Soseki' means cornerstone in Japanese.
CC {ECO:0000303|PubMed:30737509}.
CC -!- SIMILARITY: Belongs to the SOSEKI family. {ECO:0000305}.
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DR EMBL; AC007153; AAD30611.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27858.1; -; Genomic_DNA.
DR EMBL; AY800564; AAV68800.1; -; mRNA.
DR EMBL; AY924654; AAX23729.1; -; mRNA.
DR PIR; F86189; F86189.
DR RefSeq; NP_683277.1; NM_148436.4.
DR AlphaFoldDB; Q9SYJ8; -.
DR SMR; Q9SYJ8; -.
DR STRING; 3702.AT1G05577.1; -.
DR PaxDb; Q9SYJ8; -.
DR PRIDE; Q9SYJ8; -.
DR ProteomicsDB; 191502; -.
DR EnsemblPlants; AT1G05577.1; AT1G05577.1; AT1G05577.
DR GeneID; 837062; -.
DR Gramene; AT1G05577.1; AT1G05577.1; AT1G05577.
DR KEGG; ath:AT1G05577; -.
DR Araport; AT1G05577; -.
DR TAIR; locus:504956226; AT1G05577.
DR eggNOG; KOG1650; Eukaryota.
DR HOGENOM; CLU_037903_1_0_1; -.
DR OMA; WEDERRY; -.
DR OrthoDB; 1242361at2759; -.
DR PhylomeDB; Q9SYJ8; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SYJ8; baseline and differential.
DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA: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..372
FT /note="Protein SOSEKI 1"
FT /id="PRO_0000452141"
FT REGION 11..102
FT /note="DIX-like oligomerization domain"
FT /evidence="ECO:0000303|PubMed:30737509"
FT REGION 146..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 330..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 233..234
FT /note="Association to cell membranes"
FT /evidence="ECO:0000269|PubMed:32004461"
FT COMPBIAS 146..166
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..211
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 330..351
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 29
FT /note="H->D: Impaired polymerization leading to an altered
FT polar localization and abnormal cell division planes in the
FT root; when associated with A-78 or R-78."
FT /evidence="ECO:0000269|PubMed:32004461"
FT MUTAGEN 78
FT /note="D->A,R: Impaired polymerization leading to an
FT altered polar localization and abnormal cell division
FT planes in the root; when associated with D-29."
FT /evidence="ECO:0000269|PubMed:32004461"
FT MUTAGEN 233
FT /note="C->A: Altered association to cell membranes.
FT Delocalization from cell membranes and impaired ability to
FT alter cell division planes; when associated with A-234."
FT /evidence="ECO:0000269|PubMed:32004461"
FT MUTAGEN 234
FT /note="G->A: Delocalization from cell membranes and
FT impaired ability to alter cell division planes; when
FT associated with A-233."
FT /evidence="ECO:0000269|PubMed:32004461"
FT MUTAGEN 307..310
FT /note="CSQC->ASQA: No detectable changes in localization or
FT biological activity."
FT /evidence="ECO:0000269|PubMed:32004461"
SQ SEQUENCE 372 AA; 41639 MW; 5DAC04B3E5E6F4C9 CRC64;
MESNGGGGEV RRVNLVYFLS RSGHVDHPHL LRVHHLSRNG VFLRDVKKWL ADARGDAMPD
AFSWSCKRRY KNGYVWQDLL DDDLITPISD NEYVLKGSEI LLSSPKEDYP NVEKKAWVTR
NGGIDAEEKL QKLKLTSEKI QKESPVFCSQ RSTATTSTVT EESTTNEEGF VLKKQDPKTV
SGQRDGSTEN GSGNDVESGR PSVSSTTSSS SYIKNKSYSS VRASHVLRNL MKCGGLDTND
AVLVPLNKSR SGAFGPAWED ERRYQYHQQH NARKSFEGAW SGIKMKETIE FCKPKVAPSK
PSMAPLCSQC GKLFKPEKMH SHMKLCRGMK NSSANNDLMT SNNTVKPRQQ RCRNIPGNPL
GHQRVLTTTL KE
