SOK3_PHYPA
ID SOK3_PHYPA Reviewed; 709 AA.
AC A0A2K1J5A5;
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 3 {ECO:0000303|PubMed:32004461};
DE Short=PpSOK3 {ECO:0000303|PubMed:32004461};
GN Name=SOK3 {ECO:0000303|PubMed:32004461};
GN ORFNames=PHYPA_022558 {ECO:0000312|EMBL:PNR36707.1};
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; ABEU02000017; PNR36707.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K1J5A5; -.
DR SMR; A0A2K1J5A5; -.
DR STRING; 3218.PP1S68_283V6.1; -.
DR EnsemblPlants; Pp3c17_23930V3.1; Pp3c17_23930V3.1; Pp3c17_23930.
DR EnsemblPlants; Pp3c17_23930V3.2; Pp3c17_23930V3.2; Pp3c17_23930.
DR Gramene; Pp3c17_23930V3.1; Pp3c17_23930V3.1; Pp3c17_23930.
DR Gramene; Pp3c17_23930V3.2; Pp3c17_23930V3.2; Pp3c17_23930.
DR Proteomes; UP000006727; Chromosome 17.
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..709
FT /note="Protein SOSEKI 3"
FT /id="PRO_0000452147"
FT REGION 8..101
FT /note="DIX-like oligomerization domain"
FT /evidence="ECO:0000250|UniProtKB:Q9SYJ8"
FT REGION 242..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 315..344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 358..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 411..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 506..560
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 315..330
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 526..541
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 709 AA; 78642 MW; 39DCEEE312E3823D CRC64;
MARGEDSSSV QVLYQLSWDG KLEHPHMIEV HYPPNQGGLR LRDVKKRLTT LRGHGINDSF
SWSSKRNYKN EFIWNDLCDD DVIQPLRGSG EYVLRASELF DTFTNKPWEH PSKHSNERMQ
SSRTMSVDNV TLQQGLINVK LHSGALARED DQPSGEKLCC SGRRSCINLE DCSSKGVAID
IPKNLQNLSV DQETIDVEKS DFCLSSSDNE VSPRLKTAAD CITPVKDVGL VVMTRSTTVH
GLHTPAPRSL TSPTEPPFSP GSAKRMWKKE IRKSLFRTSR NSSNVNPVLS GENAALDVDV
PPITLSTQED VSFWRDGRSK SASPSSLNEL REVQNEKEKE AEQSTSQLIR LLWARWTGGS
SKGKRTPQST CEDPLPKSPE AKQMPRSRTK TPCKEIRSTN HIAGSLPVTC PSPAVDNKAH
SSLDRQEIPP QEECKNRPSP MTLQSCEEIT SPVTEIEQDV EIGDIKAIVE EQASNKFPEP
EFQQNLRTEQ IVLSVQIPDL HIDALDSPTS DTQGSPAEAD IPKSATARVK TSNSLPRVKT
TTSPKPLPPG FHKGTNDTKP VQIITPRRTP RTSIPLASPP PLVRTFNRVS VRSLSSIAAI
TLSPENDSAA SNLSPENPIV KKRINFRERD EMPLIPGLTT LDWEKALQEA VTDCLPPPNF
REILQECSTC GRTFKPDSLQ VHMRGCHPPQ YARAFSARAS PHVVRSRAS
