SOK2_ARATH
ID SOK2_ARATH Reviewed; 414 AA.
AC Q9LX14;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 110.
DE RecName: Full=Protein SOSEKI 2 {ECO:0000303|PubMed:30737509};
DE Short=AtSOK2 {ECO:0000303|PubMed:32004461};
DE AltName: Full=Protein UPSTREAM OF FLC {ECO:0000303|PubMed:15186749};
GN Name=SOK2 {ECO:0000303|PubMed:30737509};
GN Synonyms=UFC {ECO:0000303|PubMed:15186749};
GN OrderedLocusNames=At5g10150 {ECO:0000312|Araport:AT5G10150};
GN ORFNames=T31P16.140 {ECO:0000312|EMBL:CAB92056.1};
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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].
RA Shinn P., Chen H., Cheuk R., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, AND INDUCTION BY VERNALIZATION.
RX PubMed=15186749; DOI=10.1016/j.cub.2004.04.045;
RA Finnegan E.J., Sheldon C.C., Jardinaud F., Peacock W.J., Dennis E.S.;
RT "A cluster of Arabidopsis genes with a coordinate response to an
RT environmental stimulus.";
RL Curr. Biol. 14:911-916(2004).
RN [5]
RP INDUCTION BY SUF4.
RX PubMed=17138694; DOI=10.1105/tpc.106.045179;
RA Kim S., Choi K., Park C., Hwang H.J., Lee I.;
RT "SUPPRESSOR OF FRIGIDA4, encoding a C2H2-Type zinc finger protein,
RT represses flowering by transcriptional activation of Arabidopsis FLOWERING
RT LOCUS C.";
RL Plant Cell 18:2985-2998(2006).
RN [6]
RP FUNCTION, AND INDUCTION BY VERNALIZATION.
RC STRAIN=cv. C24;
RX PubMed=18156133; DOI=10.1093/pcp/pcm176;
RA Andersson C.R., Helliwell C.A., Bagnall D.J., Hughes T.P., Finnegan E.J.,
RA Peacock W.J., Dennis E.S.;
RT "The FLX gene of Arabidopsis is required for FRI-dependent activation of
RT FLC expression.";
RL Plant Cell Physiol. 49:191-200(2008).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY,
RP 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 [8]
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: Part of a three-gene cluster containing FLC, UFC and DFC,
CC which is coordinately regulated in response to vernalization
CC (PubMed:15186749, PubMed:18156133). Also regulated by FLX
CC (PubMed:15186749). SOSEKI proteins (SOK1-5) locally interpret global
CC polarity cues and can influence cell division orientation to coordinate
CC cell polarization relative to body axes, probably by guiding
CC ANGUSTIFOLIA (AN) polarized localization (PubMed:30737509,
CC PubMed:32004461). {ECO:0000269|PubMed:15186749,
CC ECO:0000269|PubMed:18156133, 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 integrate
CC apical-basal and radial organismal axes to localize to polar cell
CC edges, pointing towards the epidermis, mainly to inner basal edges.
CC {ECO:0000269|PubMed:30737509}.
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 forming cotyledons at the heart stage
CC (PubMed:30737509). Expressed in the inner basal edge of endodermal
CC cells in the primary and lateral roots (PubMed:30737509).
CC {ECO:0000269|PubMed:30737509}.
CC -!- INDUCTION: Epigenetically down-regulated by vernalization
CC (PubMed:15186749, PubMed:18156133). Not regulated by SUF4
CC (PubMed:17138694). {ECO:0000269|PubMed:15186749,
CC ECO:0000269|PubMed:17138694, ECO:0000269|PubMed:18156133}.
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; AL356332; CAB92056.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91502.1; -; Genomic_DNA.
DR EMBL; BT014891; AAT44967.1; -; mRNA.
DR EMBL; BT015021; AAT70472.1; -; mRNA.
DR PIR; T50019; T50019.
DR RefSeq; NP_196577.1; NM_121053.5.
DR AlphaFoldDB; Q9LX14; -.
DR SMR; Q9LX14; -.
DR STRING; 3702.AT5G10150.1; -.
DR iPTMnet; Q9LX14; -.
DR PaxDb; Q9LX14; -.
DR PRIDE; Q9LX14; -.
DR EnsemblPlants; AT5G10150.1; AT5G10150.1; AT5G10150.
DR GeneID; 830879; -.
DR Gramene; AT5G10150.1; AT5G10150.1; AT5G10150.
DR KEGG; ath:AT5G10150; -.
DR Araport; AT5G10150; -.
DR TAIR; locus:2184133; AT5G10150.
DR eggNOG; ENOG502QVHU; Eukaryota.
DR HOGENOM; CLU_025038_1_0_1; -.
DR InParanoid; Q9LX14; -.
DR OrthoDB; 543876at2759; -.
DR PhylomeDB; Q9LX14; -.
DR PRO; PR:Q9LX14; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LX14; baseline and differential.
DR GO; GO:0009925; C:basal plasma membrane; IDA:TAIR.
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..414
FT /note="Protein SOSEKI 2"
FT /id="PRO_0000423724"
FT REGION 44..135
FT /note="DIX-like oligomerization domain"
FT /evidence="ECO:0000269|PubMed:30737509"
FT REGION 171..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 283..284
FT /note="Association to cell membranes"
FT /evidence="ECO:0000250|UniProtKB:Q9SYJ8"
FT COMPBIAS 176..192
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..247
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..267
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 414 AA; 47953 MW; F18F3AFE696EE114 CRC64;
MEAVRCRRGR ENNKSPERII RSLNHHQHDE ELEEEVKTKK PIFRRVQVVY YLTRNGHLEH
PHFIEVISPV NQPLRLRDVM NRLTILRGKC MTSQYAWSCK RSYRNGFVWN DLAENDVIYP
SDCAEYVLKG SEITDKFQEV HVNRPLSGSI QEAPKSRLLR SKLKPQNRTA SFDDAELYVG
EEEEEEDGEY ELYEEKTSYT SSTTPQSRCS RGVSTETMES TEQKPNLTKT EQDLQVRSDS
SDLTRSNPVV KPRRHEVSTR VEDGDPVEPG SGRGSMWLQM ISCGHIATKY YAPSVMNPRQ
KEENLRKGVL CKNIVKKTVV DDEREMIRFM SENPRFGNPQ AEEKEYFSGS IVESVSQERV
TAEPSLRRSN SFNEERSKIV EMAKETKKKE ERSMAKVKCI PRTCLMSSSK QIKK
