SOK4_ARATH
ID SOK4_ARATH Reviewed; 343 AA.
AC Q8GY65; F4J7X6; Q9LX84;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Protein SOSEKI 4 {ECO:0000303|PubMed:30737509};
DE Short=AtSOK4 {ECO:0000303|PubMed:32004461};
DE AltName: Full=Auxin-regulated protein 3 {ECO:0000303|PubMed:31207460};
DE Short=AtAuxRP3 {ECO:0000303|PubMed:31207460};
GN Name=SOK4 {ECO:0000303|PubMed:30737509};
GN Synonyms=AUXRP3 {ECO:0000303|PubMed:31207460};
GN OrderedLocusNames=At3g46110 {ECO:0000312|Araport:AT3G46110};
GN ORFNames=F12M12.80 {ECO:0000312|EMBL:CAB90938.1};
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=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 [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] (ISOFORM 1).
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] (ISOFORM 1).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX PubMed=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
RN [6]
RP FUNCTION.
RC STRAIN=cv. Columbia;
RX PubMed=31207460; DOI=10.1016/j.jplph.2019.152990;
RA Shen L., Zhong T., Wang L., Zhang Q., Jin H., Xu M., Ye J.;
RT "Characterization the role of a UFC homolog, AtAuxRP3, in the regulation of
RT Arabidopsis seedling growth and stress response.";
RL J. Plant Physiol. 240:152990-152990(2019).
RN [7]
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 [8]
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 15-109, FUNCTION, INTERACTION
RP WITH ANGUSTIFOLIA, MUTAGENESIS OF ASP-85, DOMAIN, 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 (PubMed:30737509). Positive regulator of
CC auxin (indole-3-acetic acid, IAA) biosynthesis and signaling pathway
CC leading to the modulation of seedling growth, plant and inflorescence
CC development (PubMed:31207460). Negative regulator of stress responses
CC (e.g. salinity and osmotic stress) (PubMed:31207460).
CC {ECO:0000269|PubMed:30737509, ECO:0000269|PubMed:31207460}.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8GY65-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8GY65-2; Sequence=VSP_060913;
CC -!- TISSUE SPECIFICITY: Expressed during embryogenesis and in roots.
CC {ECO:0000269|PubMed:30737509}.
CC -!- DEVELOPMENTAL STAGE: During embryogenesis, first observed at the
CC globular stage and accumulates in cells next to the suspensor,
CC including lens-shaped cells (PubMed:30737509). Observed at low levels
CC in few vascular cells of the primary root (PubMed:30737509). Also
CC expressed in lateral root (PubMed:30737509).
CC {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:32004461}.
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=CAB90938.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL355775; CAB90938.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE78114.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78115.1; -; Genomic_DNA.
DR EMBL; BT005317; AAO63381.1; -; mRNA.
DR EMBL; AK117838; BAC42479.1; -; mRNA.
DR EMBL; BX823834; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; T49252; T49252.
DR RefSeq; NP_190197.2; NM_114480.4. [Q8GY65-1]
DR RefSeq; NP_974389.1; NM_202660.2. [Q8GY65-2]
DR PDB; 6RSN; X-ray; 1.70 A; A=15-109.
DR PDBsum; 6RSN; -.
DR AlphaFoldDB; Q8GY65; -.
DR SMR; Q8GY65; -.
DR STRING; 3702.AT3G46110.1; -.
DR PaxDb; Q8GY65; -.
DR PRIDE; Q8GY65; -.
DR ProteomicsDB; 180937; -.
DR ProteomicsDB; 199671; -.
DR EnsemblPlants; AT3G46110.1; AT3G46110.1; AT3G46110. [Q8GY65-1]
DR EnsemblPlants; AT3G46110.2; AT3G46110.2; AT3G46110. [Q8GY65-2]
DR GeneID; 823754; -.
DR Gramene; AT3G46110.1; AT3G46110.1; AT3G46110. [Q8GY65-1]
DR Gramene; AT3G46110.2; AT3G46110.2; AT3G46110. [Q8GY65-2]
DR KEGG; ath:AT3G46110; -.
DR Araport; AT3G46110; -.
DR TAIR; locus:2075331; AT3G46110.
DR eggNOG; ENOG502QTBW; Eukaryota.
DR HOGENOM; CLU_025038_0_0_1; -.
DR InParanoid; Q8GY65; -.
DR OMA; PVMPRAH; -.
DR OrthoDB; 543876at2759; -.
DR PhylomeDB; Q8GY65; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8GY65; 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:0009734; P:auxin-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0010229; P:inflorescence development; IMP:UniProtKB.
DR GO; GO:1905392; P:plant organ morphogenesis; IMP:UniProtKB.
DR GO; GO:0051258; P:protein polymerization; IDA:UniProtKB.
DR GO; GO:0010600; P:regulation of auxin biosynthetic process; IMP:UniProtKB.
DR GO; GO:0010928; P:regulation of auxin mediated signaling pathway; IMP:UniProtKB.
DR GO; GO:0051302; P:regulation of cell division; IMP:UniProtKB.
DR GO; GO:2000024; P:regulation of leaf development; IMP:UniProtKB.
DR GO; GO:2000067; P:regulation of root morphogenesis; IMP:UniProtKB.
DR GO; GO:0006970; P:response to osmotic stress; IMP:UniProtKB.
DR GO; GO:1902074; P:response to salt; 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; 2.
DR Pfam; PF06136; SOK2_plant; 2.
DR PIRSF; PIRSF031043; UCP031043; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Auxin signaling pathway; Cell cycle;
KW Cell division; Cell membrane; Developmental protein; Membrane;
KW Reference proteome; Stress response.
FT CHAIN 1..343
FT /note="Protein SOSEKI 4"
FT /id="PRO_0000452143"
FT REGION 18..109
FT /note="DIX-like oligomerization domain"
FT /evidence="ECO:0000303|PubMed:32004461"
FT REGION 148..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 233..234
FT /note="Association to cell membranes"
FT /evidence="ECO:0000250|UniProtKB:Q9SYJ8"
FT COMPBIAS 154..177
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..194
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 312..343
FT /note="Missing (in isoform 2)"
FT /id="VSP_060913"
FT MUTAGEN 85
FT /note="D->A: Severely attenuated polymerization."
FT /evidence="ECO:0000269|PubMed:32004461"
FT CONFLICT 58
FT /note="N -> S (in Ref. 5; BX823834)"
FT /evidence="ECO:0000305"
FT CONFLICT 284
FT /note="F -> L (in Ref. 5; BX823834)"
FT /evidence="ECO:0000305"
FT STRAND 19..30
FT /evidence="ECO:0007829|PDB:6RSN"
FT STRAND 36..41
FT /evidence="ECO:0007829|PDB:6RSN"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:6RSN"
FT HELIX 50..61
FT /evidence="ECO:0007829|PDB:6RSN"
FT TURN 63..65
FT /evidence="ECO:0007829|PDB:6RSN"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:6RSN"
FT STRAND 69..77
FT /evidence="ECO:0007829|PDB:6RSN"
FT STRAND 80..85
FT /evidence="ECO:0007829|PDB:6RSN"
FT TURN 96..98
FT /evidence="ECO:0007829|PDB:6RSN"
FT STRAND 99..106
FT /evidence="ECO:0007829|PDB:6RSN"
SQ SEQUENCE 343 AA; 38927 MW; 36FFCFC4C4D28535 CRC64;
MALVSSRATQ DSKPSRERIV PVVYYLSRNG RLDHPHFIEV PLSSHNGLYL KDVINRLNDL
RGNGMACLYS WSSKRTYKNG FVWYDLSDED FIFPVHGQEY VLKGSQILDL DNNSGNFSAV
THRRNQSWSS VDHYKVYKAS ELNAEATRKL SMDASTQTDD RRRRKSPVDE VNEVTELSRE
EITSPPQSDS SPETLESLMR ADGRLILLQE DQELNRTVEK MRPSAVLMQL ISCGAMSFKK
CGPTLMNGNT RSTAVRGTGN YRLERAEKEL KSFGRVKLEE KEYFSGSLID ESSKKELVPA
LKRSSSYNID RSSRMGLTKE KEGEELARAN FIPRNPNSVV GQP
