SOK5_ARATH
ID SOK5_ARATH Reviewed; 423 AA.
AC Q9FJF5;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Protein SOSEKI 5 {ECO:0000303|PubMed:30737509};
DE Short=AtSOK5 {ECO:0000303|PubMed:32004461};
GN Name=SOK5 {ECO:0000303|PubMed:30737509};
GN OrderedLocusNames=At5g59790 {ECO:0000312|Araport:AT5G59790};
GN ORFNames=MMN10.1 {ECO:0000312|EMBL:BAB08346.1};
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=9872454; DOI=10.1093/dnares/5.5.297;
RA Nakamura Y., Sato S., Asamizu E., Kaneko T., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VII. Sequence
RT features of the regions of 1,013,767 bp covered by sixteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:297-308(1998).
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=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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
RP MUTAGENESIS OF CYS-303 AND 356-GLU--GLU-359, 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. {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) (Probable). {ECO:0000250|UniProtKB:Q9SYJ8,
CC ECO:0000269|PubMed:32004461, ECO:0000305|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: During embryogenesis, first observed at the
CC globular stage and accumulates in cells next to the suspensor,
CC including lens-shaped cells (PubMed:30737509). Expressed in the inner
CC basal edge of endodermal cells in the primary and lateral roots
CC (PubMed:30737509). {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}.
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DR EMBL; AB015475; BAB08346.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97234.1; -; Genomic_DNA.
DR EMBL; AY093139; AAM13138.1; -; mRNA.
DR EMBL; BT008516; AAP37875.1; -; mRNA.
DR EMBL; AK226458; BAE98600.1; -; mRNA.
DR RefSeq; NP_200787.1; NM_125371.6.
DR AlphaFoldDB; Q9FJF5; -.
DR SMR; Q9FJF5; -.
DR IntAct; Q9FJF5; 2.
DR STRING; 3702.AT5G59790.1; -.
DR PaxDb; Q9FJF5; -.
DR PRIDE; Q9FJF5; -.
DR ProteomicsDB; 190006; -.
DR EnsemblPlants; AT5G59790.1; AT5G59790.1; AT5G59790.
DR GeneID; 836100; -.
DR Gramene; AT5G59790.1; AT5G59790.1; AT5G59790.
DR KEGG; ath:AT5G59790; -.
DR Araport; AT5G59790; -.
DR TAIR; locus:2168042; AT5G59790.
DR eggNOG; ENOG502QUB8; Eukaryota.
DR HOGENOM; CLU_025038_0_0_1; -.
DR InParanoid; Q9FJF5; -.
DR OMA; FKDCGPS; -.
DR OrthoDB; 543876at2759; -.
DR PhylomeDB; Q9FJF5; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FJF5; 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..423
FT /note="Protein SOSEKI 5"
FT /id="PRO_0000452144"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 45..136
FT /note="DIX-like oligomerization domain"
FT /evidence="ECO:0000250|UniProtKB:Q9SYJ8"
FT REGION 150..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 196..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 379..423
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 MOTIF 303..304
FT /note="Association to cell membranes"
FT /evidence="ECO:0000250|UniProtKB:Q9SYJ8"
FT COMPBIAS 209..231
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..258
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..407
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 303
FT /note="C->A: Delocalization from cell membranes."
FT /evidence="ECO:0000269|PubMed:32004461"
FT MUTAGEN 356..359
FT /note="EDKE->QDKQ: No detectable changes in localization or
FT biological activity."
FT /evidence="ECO:0000269|PubMed:32004461"
SQ SEQUENCE 423 AA; 47784 MW; 29AAE60D10753C50 CRC64;
MSSRVFRATP DNNYLVPRRS KDQQDTSPDR NRIWSEPRLK PVVNRKVPVV YYLCRNGQLD
HPHFIEVTLS SHDGLYLKDV INRLNDLRGK GMASLYSWSS KRSYKNGFVW HDLSEDDFIF
PVQGQEYVLK GSEVLDSCLI SNPRSLLETS SFRDPRSLNP DKNSGDDIPA VINRRRNQSW
SSIDLSEYKV YKATESSAES TQRLAADAST QTDDRRRRRR PAKEEIEEVK SPASYENQST
ELSRDEISPP PSDSSPETLE NLIKADGRLI LRPSESSTDH RTVESLSSGR MRASAVLMQL
ISCGTMSFKE CGPVLLKDQG LALNGRSGCT ITRGAEDNGE ERVDKELKSF GRVQLEDKEY
FSGSLIETKK ELVPALKRSS SYNADRCSRM GPTTEKDEEE AVRAKCIPRK PKPVAKRNNG
GQQ
