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SOK4_PHYPA
ID   SOK4_PHYPA              Reviewed;         390 AA.
AC   A9RNY0;
DT   07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 54.
DE   RecName: Full=Protein SOSEKI 4 {ECO:0000303|PubMed:32004461};
DE            Short=PpSOK4 {ECO:0000303|PubMed:32004461};
GN   Name=SOK4 {ECO:0000303|PubMed:32004461};
GN   ORFNames=PHYPA_022993 {ECO:0000312|EMBL:PNR35094.1},
GN   PHYPADRAFT_160198 {ECO:0000312|EMBL:EDQ79421.1};
OS   Physcomitrium patens (Spreading-leaved earth moss) (Physcomitrella patens).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Bryophyta;
OC   Bryophytina; Bryopsida; Funariidae; Funariales; Funariaceae; Physcomitrium.
OX   NCBI_TaxID=3218;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Gransden 2004;
RX   PubMed=18079367; DOI=10.1126/science.1150646;
RA   Rensing S.A., Lang D., Zimmer A.D., Terry A., Salamov A., Shapiro H.,
RA   Nishiyama T., Perroud P.-F., Lindquist E.A., Kamisugi Y., Tanahashi T.,
RA   Sakakibara K., Fujita T., Oishi K., Shin-I T., Kuroki Y., Toyoda A.,
RA   Suzuki Y., Hashimoto S.-I., Yamaguchi K., Sugano S., Kohara Y.,
RA   Fujiyama A., Anterola A., Aoki S., Ashton N., Barbazuk W.B., Barker E.,
RA   Bennetzen J.L., Blankenship R., Cho S.H., Dutcher S.K., Estelle M.,
RA   Fawcett J.A., Gundlach H., Hanada K., Heyl A., Hicks K.A., Hughes J.,
RA   Lohr M., Mayer K., Melkozernov A., Murata T., Nelson D.R., Pils B.,
RA   Prigge M., Reiss B., Renner T., Rombauts S., Rushton P.J., Sanderfoot A.,
RA   Schween G., Shiu S.-H., Stueber K., Theodoulou F.L., Tu H., Van de Peer Y.,
RA   Verrier P.J., Waters E., Wood A., Yang L., Cove D., Cuming A.C., Hasebe M.,
RA   Lucas S., Mishler B.D., Reski R., Grigoriev I.V., Quatrano R.S.,
RA   Boore J.L.;
RT   "The Physcomitrella genome reveals evolutionary insights into the conquest
RT   of land by plants.";
RL   Science 319:64-69(2008).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Gransden 2004;
RX   PubMed=29237241; DOI=10.1111/tpj.13801;
RA   Lang D., Ullrich K.K., Murat F., Fuchs J., Jenkins J., Haas F.B.,
RA   Piednoel M., Gundlach H., Van Bel M., Meyberg R., Vives C., Morata J.,
RA   Symeonidi A., Hiss M., Muchero W., Kamisugi Y., Saleh O., Blanc G.,
RA   Decker E.L., van Gessel N., Grimwood J., Hayes R.D., Graham S.W.,
RA   Gunter L.E., McDaniel S.F., Hoernstein S.N.W., Larsson A., Li F.W.,
RA   Perroud P.F., Phillips J., Ranjan P., Rokshar D.S., Rothfels C.J.,
RA   Schneider L., Shu S., Stevenson D.W., Thummler F., Tillich M.,
RA   Villarreal Aguilar J.C., Widiez T., Wong G.K., Wymore A., Zhang Y.,
RA   Zimmer A.D., Quatrano R.S., Mayer K.F.X., Goodstein D., Casacuberta J.M.,
RA   Vandepoele K., Reski R., Cuming A.C., Tuskan G.A., Maumus F., Salse J.,
RA   Schmutz J., Rensing S.A.;
RT   "The Physcomitrella patens chromosome-scale assembly reveals moss genome
RT   structure and evolution.";
RL   Plant J. 93:515-533(2018).
RN   [3]
RP   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 locally interpret global polarity cues and
CC       can influence cell division orientation to coordinate cell polarization
CC       relative to body axes. {ECO:0000250|UniProtKB:Q9SYJ8}.
CC   -!- SUBUNIT: Homodimer (By similarity). Forms long polymer filaments with
CC       other SOKs proteins polymers crucial for polar localization and
CC       biological activity (PubMed:32004461). {ECO:0000250|UniProtKB:Q9SYJ8,
CC       ECO:0000269|PubMed:32004461}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9SYJ8};
CC       Peripheral membrane protein {ECO:0000250|UniProtKB:Q9SYJ8}; Cytoplasmic
CC       side {ECO:0000250|UniProtKB:Q9SYJ8}.
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. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the SOSEKI family. {ECO:0000305}.
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DR   EMBL; DS544908; EDQ79421.1; -; Genomic_DNA.
DR   EMBL; ABEU02000018; PNR35094.1; -; Genomic_DNA.
DR   RefSeq; XP_001755748.1; XM_001755696.1.
DR   AlphaFoldDB; A9RNY0; -.
DR   SMR; A9RNY0; -.
DR   STRING; 3218.PP1S19_321V6.1; -.
DR   EnsemblPlants; Pp3c18_11140V3.1; Pp3c18_11140V3.1; Pp3c18_11140.
DR   EnsemblPlants; Pp3c18_11140V3.2; Pp3c18_11140V3.2; Pp3c18_11140.
DR   EnsemblPlants; Pp3c18_11140V3.3; Pp3c18_11140V3.3; Pp3c18_11140.
DR   Gramene; Pp3c18_11140V3.1; Pp3c18_11140V3.1; Pp3c18_11140.
DR   Gramene; Pp3c18_11140V3.2; Pp3c18_11140V3.2; Pp3c18_11140.
DR   Gramene; Pp3c18_11140V3.3; Pp3c18_11140V3.3; Pp3c18_11140.
DR   eggNOG; ENOG502QVHU; Eukaryota.
DR   HOGENOM; CLU_708616_0_0_1; -.
DR   InParanoid; A9RNY0; -.
DR   Proteomes; UP000006727; Chromosome 18.
DR   GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; ISS: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; ISS:UniProtKB.
DR   GO; GO:0051258; P:protein polymerization; IDA:UniProtKB.
DR   GO; GO:0051302; P:regulation of cell division; ISS:UniProtKB.
DR   GO; GO:0090708; P:specification of plant organ axis polarity; ISS:UniProtKB.
DR   InterPro; IPR010369; SOK.
DR   PANTHER; PTHR31083; PTHR31083; 1.
DR   Pfam; PF06136; SOK2_plant; 1.
PE   1: Evidence at protein level;
KW   Cell cycle; Cell division; Cell membrane; Developmental protein; Membrane;
KW   Reference proteome.
FT   CHAIN           1..390
FT                   /note="Protein SOSEKI 4"
FT                   /id="PRO_0000452148"
FT   REGION          22..115
FT                   /note="DIX-like oligomerization domain"
FT                   /evidence="ECO:0000250|UniProtKB:Q9SYJ8"
FT   REGION          210..247
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          291..321
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        215..229
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        299..320
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   390 AA;  44293 MW;  B1308A0387DA82D6 CRC64;
     MPSLRTERRS FGMETPRHSS FRMAEVLYVL SCGGQLEHPH MINVQYPVHQ PGPTLRDVKT
     RLIALRGRGM PDSFSWSYKR NYKDTFIWCD LFDDNFILPL SESGEYALKA TKRFDASQVK
     YLRPPRRSEN LEAEGDVSMV VKKGLVLISD TGSVTSNRTM ELNKQLMNSL SHSRSAAAVR
     NNEHSDVSSS DTHYSYEDVI ERKDYPARCK SNSGATKRGK ASVTPKQCHP SSRPAYWEFS
     PQGNRTGRED SLMTIGLTKH VVEENEGPTT PRAPARRRTW KKEIDKITIF RESNNSESSD
     DEQPSVQAET HVSKLSKSGG SYSAAPEDLF LYILRKATRL GSFKPRVCTE VDVVDSTQSK
     TKMLFRSKTK DEVNRLLYHS PLKQDQSIKK
 
 
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