SOK_MARPO
ID SOK_MARPO Reviewed; 911 AA.
AC A0A2R6X6S3;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2018, sequence version 1.
DT 25-MAY-2022, entry version 17.
DE RecName: Full=Protein SOSEKI {ECO:0000303|PubMed:32004461};
DE Short=MpSOK {ECO:0000303|PubMed:32004461};
GN Name=SOK {ECO:0000303|PubMed:32004461};
GN ORFNames=MARPO_0032s0007 {ECO:0000312|EMBL:PTQ41796.1};
OS Marchantia polymorpha (Liverwort) (Marchantia aquatica).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX NCBI_TaxID=3197;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tak-1;
RX PubMed=28985561; DOI=10.1016/j.cell.2017.09.030;
RA Bowman J.L., Kohchi T., Yamato K.T., Jenkins J., Shu S., Ishizaki K.,
RA Yamaoka S., Nishihama R., Nakamura Y., Berger F., Adam C., Aki S.S.,
RA Althoff F., Araki T., Arteaga-Vazquez M.A., Balasubrmanian S., Barry K.,
RA Bauer D., Boehm C.R., Briginshaw L., Caballero-Perez J., Catarino B.,
RA Chen F., Chiyoda S., Chovatia M., Davies K.M., Delmans M., Demura T.,
RA Dierschke T., Dolan L., Dorantes-Acosta A.E., Eklund D.M., Florent S.N.,
RA Flores-Sandoval E., Fujiyama A., Fukuzawa H., Galik B., Grimanelli D.,
RA Grimwood J., Grossniklaus U., Hamada T., Haseloff J., Hetherington A.J.,
RA Higo A., Hirakawa Y., Hundley H.N., Ikeda Y., Inoue K., Inoue S.I.,
RA Ishida S., Jia Q., Kakita M., Kanazawa T., Kawai Y., Kawashima T.,
RA Kennedy M., Kinose K., Kinoshita T., Kohara Y., Koide E., Komatsu K.,
RA Kopischke S., Kubo M., Kyozuka J., Lagercrantz U., Lin S.S., Lindquist E.,
RA Lipzen A.M., Lu C.W., De Luna E., Martienssen R.A., Minamino N.,
RA Mizutani M., Mizutani M., Mochizuki N., Monte I., Mosher R., Nagasaki H.,
RA Nakagami H., Naramoto S., Nishitani K., Ohtani M., Okamoto T., Okumura M.,
RA Phillips J., Pollak B., Reinders A., Rovekamp M., Sano R., Sawa S.,
RA Schmid M.W., Shirakawa M., Solano R., Spunde A., Suetsugu N., Sugano S.,
RA Sugiyama A., Sun R., Suzuki Y., Takenaka M., Takezawa D., Tomogane H.,
RA Tsuzuki M., Ueda T., Umeda M., Ward J.M., Watanabe Y., Yazaki K.,
RA Yokoyama R., Yoshitake Y., Yotsui I., Zachgo S., Schmutz J.;
RT "Insights into land plant evolution garnered from the Marchantia polymorpha
RT genome.";
RL Cell 171:287-304.e15(2017).
RN [2]
RP SUBCELLULAR LOCATION, 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:0000269|PubMed:32004461};
CC Peripheral membrane protein {ECO:0000269|PubMed:32004461}; Cytoplasmic
CC side {ECO:0000269|PubMed:32004461}. Note=Localize to polar cell edges
CC in roots. {ECO:0000269|PubMed:32004461}.
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; KZ772704; PTQ41796.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2R6X6S3; -.
DR SMR; A0A2R6X6S3; -.
DR EnsemblPlants; PTQ41796; PTQ41796; MARPO_0032s0007.
DR Gramene; PTQ41796; PTQ41796; MARPO_0032s0007.
DR OMA; PRINSIM; -.
DR Proteomes; UP000244005; Unassembled WGS sequence.
DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
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; 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..911
FT /note="Protein SOSEKI"
FT /id="PRO_0000452149"
FT REGION 15..107
FT /note="DIX-like oligomerization domain"
FT /evidence="ECO:0000250|UniProtKB:Q9SYJ8"
FT REGION 219..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 492..810
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 493..494
FT /note="Association to cell membranes"
FT /evidence="ECO:0000250|UniProtKB:Q9SYJ8"
FT COMPBIAS 219..256
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 257..409
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 411..425
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 451..470
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..573
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 588..690
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 721..735
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 736..772
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 773..809
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 911 AA; 100289 MW; D4063B0F060DEC2D CRC64;
MVLVGQGMEP EEAFTKVQVV YYLSRGGQLQ QPHLIDVPVS THSNGLYLRD VKRRLTSIRG
KGMGDSFSWS CKRNYKNNFI WQDLADDDKI LPLSDGELVL KGSELYTGFQ EKAEFMDGQF
DPENASQLPN KIKKLASKKF DFEAVKRSLD MESDKLQEQS DLAAALSLSL QLMSDPHMKR
FSKDKSMDLN QQVMNSLSQA KSNAAEECML DHSVTDISSE TLHSEESTVQ KFSFNETIRE
RSKSTASASS SGTDREHSYG PPRKTESMGR ERSLPRDLPR SREVSRELPP QVPREAPREK
SREMSRELPR EAPRELQLPR EAPRELPREV PRETSRELPR EAPREISREL PREGPREVAR
EQPREVVVPR EVVREVSREL PRDVSRDSSK AVKDTAKTRQ EKPEELPTIK TKKSPTCSES
GDSTPFMLSP RRLMAALSSP SPEKKFGKLV HSSSTRSSTP STSAASTQCE DSLPNINIRL
AKQATCLSNF RLCGNANPHA TDSRPDSPEH PLAAAAQPAS GAVPQSPNTR GHQGGPYWPR
WRSGRKPRTS SEGKEGPEPP TPPRGPMTKP VTVAKPDPPL KKSFEFDMNV SGVNSAMATP
FLQTENNSPS SSESSSAAVS SGKKPASISL SGTSDASDGG NGASSTASSS SEVQNNVSVK
EVITQQLPSP SSSEGRPSLN IDTASLPRVS ISEAISDVRE TVKTTRPDSP ESPMKPNPPS
SPVRTQLSSS PSFNKRIEDA RARARSLVSK EIRSGESRSS KDLLKENDRV KTSSGSMRSG
STRTPNNKNG TTGAGSKTLS GTFNRSPPRI NSIMWEDAPL TPTKKEFVNR DDRPLTAGRT
NLDWEKTLQE AASLSLPPPD FGQILQECGQ CGRTFKPDSL KVHMRGCHAL RRSKDFQPFN
GTSVAIRTRL Q
