ID   KEULE_ARATH             Reviewed;         666 AA.
AC   Q9C5X3; Q0WTH1; Q9LNB0;
DT   01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 2.
DT   25-MAY-2022, entry version 127.
DE   RecName: Full=SNARE-interacting protein KEULE;
GN   Name=KEU; OrderedLocusNames=At1g12360; ORFNames=F5O11.8;
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 [MRNA].
RC   TISSUE=Flower;
RX   PubMed=11157980; DOI=10.1083/jcb.152.3.531;
RA   Assaad F.F., Huet Y., Mayer U., Juergens G.;
RT   "The cytokinesis gene KEULE encodes a Sec1 protein that binds the syntaxin
RT   KNOLLE.";
RL   J. Cell Biol. 152:531-544(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
RN   [3]
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   [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   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19376835; DOI=10.1104/pp.109.138677;
RA   Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA   Grossmann J., Gruissem W., Baginsky S.;
RT   "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT   chloroplast kinase substrates and phosphorylation networks.";
RL   Plant Physiol. 150:889-903(2009).
RN   [6]
RP   FUNCTION, INTERACTION WITH SEC6, AND SUBCELLULAR LOCATION.
RX   PubMed=23702595; DOI=10.1093/mp/sst082;
RA   Wu J., Tan X., Wu C., Cao K., Li Y., Bao Y.;
RT   "Regulation of cytokinesis by exocyst subunit SEC6 and KEULE in Arabidopsis
RT   thaliana.";
RL   Mol. Plant 6:1863-1876(2013).
CC   -!- FUNCTION: Regulator of vesicle trafficking involved in cytokinesis and
CC       root hair development, but not required for cell elongation.
CC       {ECO:0000269|PubMed:23702595}.
CC   -!- SUBUNIT: Binds the syntaxin KNOLLE. Interacts with SEC6.
CC       {ECO:0000269|PubMed:23702595}.
CC   -!- INTERACTION:
CC       Q9C5X3; Q9S7P9: SNAP33; NbExp=5; IntAct=EBI-603005, EBI-603017;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23702595}. Membrane
CC       {ECO:0000269|PubMed:23702595}; Peripheral membrane protein
CC       {ECO:0000269|PubMed:23702595}. Cytoplasm, cytoskeleton, phragmoplast
CC       {ECO:0000269|PubMed:23702595}. Note=Localized with its membrane
CC       receptor. During cytokinesis, localizes to the cell plate from a very
CC       early stage of cell plate formation and until the cell plate reaches
CC       the parental cell wall.
CC   -!- TISSUE SPECIFICITY: Expressed throughout the plant, both in mitotically
CC       active and quiescent cells. Enriched in dividing tissues.
CC   -!- SIMILARITY: Belongs to the STXBP/unc-18/SEC1 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF79632.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AF331066; AAK01291.1; -; mRNA.
DR   EMBL; AC025416; AAF79632.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; AEE28870.1; -; Genomic_DNA.
DR   EMBL; AK227584; BAE99577.1; -; mRNA.
DR   PIR; C86258; C86258.
DR   RefSeq; NP_563905.1; NM_101108.4.
DR   AlphaFoldDB; Q9C5X3; -.
DR   SMR; Q9C5X3; -.
DR   BioGRID; 23031; 9.
DR   IntAct; Q9C5X3; 5.
DR   STRING; 3702.AT1G12360.1; -.
DR   iPTMnet; Q9C5X3; -.
DR   PaxDb; Q9C5X3; -.
DR   PRIDE; Q9C5X3; -.
DR   ProteomicsDB; 250624; -.
DR   EnsemblPlants; AT1G12360.1; AT1G12360.1; AT1G12360.
DR   GeneID; 837791; -.
DR   Gramene; AT1G12360.1; AT1G12360.1; AT1G12360.
DR   KEGG; ath:AT1G12360; -.
DR   Araport; AT1G12360; -.
DR   TAIR; locus:2034670; AT1G12360.
DR   eggNOG; KOG1300; Eukaryota.
DR   HOGENOM; CLU_009210_3_0_1; -.
DR   InParanoid; Q9C5X3; -.
DR   OMA; ITDRTMD; -.
DR   OrthoDB; 725424at2759; -.
DR   PhylomeDB; Q9C5X3; -.
DR   PRO; PR:Q9C5X3; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9C5X3; baseline and differential.
DR   Genevisible; Q9C5X3; AT.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
DR   GO; GO:0005829; C:cytosol; IDA:TAIR.
DR   GO; GO:0019898; C:extrinsic component of membrane; IDA:TAIR.
DR   GO; GO:0009524; C:phragmoplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0030141; C:secretory granule; IBA:GO_Central.
DR   GO; GO:0019905; F:syntaxin binding; IBA:GO_Central.
DR   GO; GO:0000911; P:cytokinesis by cell plate formation; IMP:TAIR.
DR   GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR   GO; GO:0006904; P:vesicle docking involved in exocytosis; IBA:GO_Central.
DR   GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR   Gene3D; 3.40.50.1910; -; 1.
DR   Gene3D; 3.40.50.2060; -; 1.
DR   Gene3D; 3.90.830.10; -; 1.
DR   InterPro; IPR043154; Sec-1-like_dom1.
DR   InterPro; IPR043127; Sec-1-like_dom3a.
DR   InterPro; IPR001619; Sec1-like.
DR   InterPro; IPR027482; Sec1-like_dom2.
DR   InterPro; IPR036045; Sec1-like_sf.
DR   PANTHER; PTHR11679; PTHR11679; 1.
DR   Pfam; PF00995; Sec1; 1.
DR   PIRSF; PIRSF005715; VPS45_Sec1; 1.
DR   SUPFAM; SSF56815; SSF56815; 1.
PE   1: Evidence at protein level;
KW   Cell cycle; Cell division; Coiled coil; Cytoplasm; Cytoskeleton; Membrane;
KW   Protein transport; Reference proteome; Transport.
FT   CHAIN           1..666
FT                   /note="SNARE-interacting protein KEULE"
FT                   /id="PRO_0000206294"
FT   REGION          534..589
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          340..377
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        544..573
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        452
FT                   /note="Q -> E (in Ref. 1; AAK01291)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   666 AA;  75083 MW;  731AFDD00E234CEF CRC64;
     MSYSDSDSSS HGGEYKNFRQ ITRERLLYEM LRSAKTGSSK STWKVLIMDK LTVKIMSYAC
     KMADITQEGV SLVEDIFRRR QPLPSMDAIY FIQPTKENVI MFLSDMSGKS PLYKKAFVFF
     SSPVSKELVG HIKKDSSVLP RIGALREMNL EFFAIDSQGF ITDHERALED LFGDEETSRK
     GDACLNVMAS RIATVFASLR EFPAVRYRAA KSLDASTMTT LRDLIPTKLA AGIWNCLAKH
     KQSIENFPQT ETCELLILDR SIDQIAPVIH EWTYDAMCHD LLNMEGNKYV HVIPSKSGGQ
     PEKKDVLLEE HDPIWLELRH AHIADASERL HDKMTNFLSK NKAAQLQGKR DGAELSTRDL
     QKMVQALPQY SEQIDKLSLH VEIARKLNDL IREQGLRELG QLEQDLVFGD AGMKDVIKYL
     STQEEASREG KLRLLMILAT IYPEKFEGEK GQNLMKLAKL SSDDMTAVNN MSLLGSAVDA
     KKNTPGGFTL KFDLHKKKRA VRKERQEEAA WQLSRFYPMI EELIEKLSKG ELPKEDFPCM
     NDPSPSFHGS TSLSSAASSS QGQAAQSMRS RRTPTWAKPR GSDDGYSSDS VLRHASSDFR
     KMGQRIFVFI VGGATRSELK VCHKLSTKLK REVILGSTSL DDPPQFITKL KLLTANDDLS
     LDDLQI