SY111_ARATH
ID SY111_ARATH Reviewed; 310 AA.
AC Q42374; Q8VXY8; Q9FRS8;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Syntaxin-related protein KNOLLE;
DE AltName: Full=Syntaxin-111;
DE Short=AtSYP111;
GN Name=KN; Synonyms=SYP111; OrderedLocusNames=At1g08560; ORFNames=F22O13.4;
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 [GENOMIC DNA / MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=8548827; DOI=10.1016/s0092-8674(00)80993-9;
RA Lukowitz W., Mayer U., Juergens G.;
RT "Cytokinesis in the Arabidopsis embryo involves the syntaxin-related KNOLLE
RT gene product.";
RL Cell 84:61-71(1996).
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;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP CHARACTERIZATION.
RX PubMed=9396754; DOI=10.1083/jcb.139.6.1485;
RA Lauber M.H., Waizenegger I., Steinmann T., Schwarz H., Mayer U., Hwang I.,
RA Lukowitz W., Juergens G.;
RT "The Arabidopsis KNOLLE protein is a cytokinesis-specific syntaxin.";
RL J. Cell Biol. 139:1485-1493(1997).
RN [6]
RP INTERACTION WITH SNAP33.
RX PubMed=11591731; DOI=10.1083/jcb.200107126;
RA Heese M., Gansel X., Sticher L., Wick P., Grebe M., Granier F.,
RA Juergens G.;
RT "Functional characterization of the KNOLLE-interacting t-SNARE AtSNAP33 and
RT its role in plant cytokinesis.";
RL J. Cell Biol. 155:239-249(2001).
RN [7]
RP INTERACTION WITH KEULE.
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 [8]
RP INTERACTION WITH NPSN11.
RX PubMed=12068098; DOI=10.1104/pp.003970;
RA Zheng H., Bednarek S.Y., Sanderfoot A.A., Alonso J., Ecker J.R.,
RA Raikhel N.V.;
RT "NPSN11 is a cell plate-associated SNARE protein that interacts with the
RT syntaxin KNOLLE.";
RL Plant Physiol. 129:530-539(2002).
CC -!- FUNCTION: Involved in cytokinesis. Acts as a cell plate-specific
CC syntaxin, required for the fusion of vesicles at the plane of cell
CC division.
CC -!- SUBUNIT: Interacts with SNAP33 and/or NPSN11 to form a t-SNARE complex
CC and with KEULE. {ECO:0000269|PubMed:11157980,
CC ECO:0000269|PubMed:11591731, ECO:0000269|PubMed:12068098}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type IV membrane protein.
CC -!- TISSUE SPECIFICITY: Abundant in flowers and developing siliques. A low
CC level expression is seen in the seedlings, roots, and leaves.
CC -!- DEVELOPMENTAL STAGE: It is detected throughout embryogenesis until
CC expression declines in mature embryo. During embryogenesis it is
CC detected in patches of single cells or small cell groups.
CC -!- INDUCTION: At or soon after the onset of mitosis.
CC -!- SIMILARITY: Belongs to the syntaxin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF99783.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U39452; AAC49163.1; -; Genomic_DNA.
DR EMBL; U39451; AAC49162.1; -; mRNA.
DR EMBL; AC003981; AAF99783.1; ALT_FRAME; Genomic_DNA.
DR EMBL; CP002684; AEE28306.1; -; Genomic_DNA.
DR EMBL; BT000970; AAN41370.1; -; mRNA.
DR PIR; D86218; D86218.
DR PIR; T00709; T00709.
DR RefSeq; NP_172332.1; NM_100729.4.
DR AlphaFoldDB; Q42374; -.
DR SMR; Q42374; -.
DR BioGRID; 22619; 27.
DR IntAct; Q42374; 22.
DR MINT; Q42374; -.
DR STRING; 3702.AT1G08560.1; -.
DR TCDB; 8.A.91.1.1; the syntaxin (syntaxin) family.
DR iPTMnet; Q42374; -.
DR PaxDb; Q42374; -.
DR PRIDE; Q42374; -.
DR ProteomicsDB; 226770; -.
DR EnsemblPlants; AT1G08560.1; AT1G08560.1; AT1G08560.
DR GeneID; 837378; -.
DR Gramene; AT1G08560.1; AT1G08560.1; AT1G08560.
DR KEGG; ath:AT1G08560; -.
DR Araport; AT1G08560; -.
DR TAIR; locus:2025620; AT1G08560.
DR eggNOG; KOG0810; Eukaryota.
DR HOGENOM; CLU_042423_1_1_1; -.
DR InParanoid; Q42374; -.
DR OMA; FMESYFR; -.
DR OrthoDB; 1033833at2759; -.
DR PhylomeDB; Q42374; -.
DR PRO; PR:Q42374; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q42374; baseline and differential.
DR Genevisible; Q42374; AT.
DR GO; GO:0009504; C:cell plate; IDA:TAIR.
DR GO; GO:0012505; C:endomembrane system; IDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0009524; C:phragmoplast; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0031201; C:SNARE complex; IBA:GO_Central.
DR GO; GO:0005484; F:SNAP receptor activity; IBA:GO_Central.
DR GO; GO:0000149; F:SNARE binding; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0048278; P:vesicle docking; IBA:GO_Central.
DR GO; GO:0006906; P:vesicle fusion; IBA:GO_Central.
DR CDD; cd00179; SynN; 1.
DR InterPro; IPR010989; SNARE.
DR InterPro; IPR045242; Syntaxin.
DR InterPro; IPR006012; Syntaxin/epimorphin_CS.
DR InterPro; IPR006011; Syntaxin_N.
DR InterPro; IPR000727; T_SNARE_dom.
DR PANTHER; PTHR19957; PTHR19957; 1.
DR Pfam; PF05739; SNARE; 1.
DR Pfam; PF00804; Syntaxin; 1.
DR SMART; SM00503; SynN; 1.
DR SMART; SM00397; t_SNARE; 1.
DR SUPFAM; SSF47661; SSF47661; 1.
DR PROSITE; PS00914; SYNTAXIN; 1.
DR PROSITE; PS50192; T_SNARE; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell cycle; Cell division; Coiled coil; Membrane;
KW Protein transport; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..310
FT /note="Syntaxin-related protein KNOLLE"
FT /id="PRO_0000210244"
FT TOPO_DOM 1..283
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 284..304
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 305..310
FT /note="Vesicular"
FT /evidence="ECO:0000255"
FT DOMAIN 212..274
FT /note="t-SNARE coiled-coil homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
FT COILED 94..159
FT /evidence="ECO:0000255"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9ZSD4"
SQ SEQUENCE 310 AA; 35275 MW; F97909E27835DD87 CRC64;
MNDLMTKSFM SYVDLKKAAM KDMEAGPDFD LEMASTKADK MDENLSSFLE EAEYVKAEMG
LISETLARIE QYHEESKGVH KAESVKSLRN KISNEIVSGL RKAKSIKSKL EEMDKANKEI
KRLSGTPVYR SRTAVTNGLR KKLKEVMMEF QGLRQKMMSE YKETVERRYF TVTGEHANDE
MIEKIITDNA GGEEFLTRAI QEHGKGKVLE TVVEIQDRYD AAKEIEKSLL ELHQVFLDMA
VMVESQGEQM DEIEHHVINA SHYVADGANE LKTAKSHQRN SRKWMCIGII VLLLIILIVV
IPIITSFSSS
