SOK2_PHYPA
ID SOK2_PHYPA Reviewed; 636 AA.
AC A0A2K1L2D9;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 28-MAR-2018, sequence version 1.
DT 03-AUG-2022, entry version 16.
DE RecName: Full=Protein SOSEKI 2 {ECO:0000303|PubMed:32004461};
DE Short=PpSOK2 {ECO:0000303|PubMed:32004461};
GN Name=SOK2 {ECO:0000303|PubMed:32004461};
GN ORFNames=PHYPA_002987 {ECO:0000312|EMBL:PNR60194.1};
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; ABEU02000002; PNR60194.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K1L2D9; -.
DR SMR; A0A2K1L2D9; -.
DR STRING; 3218.PP1S165_20V6.1; -.
DR EnsemblPlants; Pp3c2_20380V3.1; Pp3c2_20380V3.1; Pp3c2_20380.
DR EnsemblPlants; Pp3c2_20380V3.2; Pp3c2_20380V3.2; Pp3c2_20380.
DR Gramene; Pp3c2_20380V3.1; Pp3c2_20380V3.1; Pp3c2_20380.
DR Gramene; Pp3c2_20380V3.2; Pp3c2_20380V3.2; Pp3c2_20380.
DR Proteomes; UP000006727; Chromosome 2.
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..636
FT /note="Protein SOSEKI 2"
FT /id="PRO_0000452146"
FT REGION 9..103
FT /note="DIX-like oligomerization domain"
FT /evidence="ECO:0000250|UniProtKB:Q9SYJ8"
FT REGION 164..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 281..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 340..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 499..524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..182
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..389
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 636 AA; 69848 MW; 6D945828527F5BAC CRC64;
MDSSSESYHK IEVIYLLSKG AEQDDHPHMI QVQYPSHQHA PTLRDVKFRL TALRGRGMPD
SYSWSYKRSY KGTFIWCDVF DGDDILPLSE SGEYVLKALE VMDSSEDACD RGVEHLGQEV
ARVLPTNRNG TSANFNEVHS IDDVRRVAPN KCVEVKRQFM GGSVHNNMTG KANRNEQGDA
YGTTSRVPDP ENCIENKRCL ESMTGSDSSR SNISTDESYG LSFERDLKMD MKEMPACPAT
RSTDHGGMSS LAPRSSRLSR REYVKCKTWA VKEDENAALN HGRLSRRSSD TLRDSNSVGN
TVDIPSSPVT RPCFPGDPLI FMLKKATKFH RSQLCRKAEV EGSPCATVGK PSSSRHTSKI
RHGSGPLKAY HGPHSSKSAT QNSRPVTYET SAKESERDIR SLCQFLGASN VGSVSQTINK
EGTKKTGSAR HIQAGSNDDF DFARHKEVAV DISEKLLLPE QVTGRYEKPS RMSKQLINKL
DSKSLNMVTR PAVRLSSKLG SGQASESFSP ASPHAPQRPI VSRPQEKAVN QLSLVAGFED
PQITSSDTSN AGLSCTSKAS GLKAVKLPRN ASNNCYFSLT IPDLEKRAAD TKVYPWRENS
AFNSIELYSG TLQKVDLAIN TSFNGATLGE LASGGC
