CSLC6_ARATH
ID CSLC6_ARATH Reviewed; 682 AA.
AC Q9SRT3;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Probable xyloglucan glycosyltransferase 6 {ECO:0000303|PubMed:11027699};
DE EC=2.4.1.- {ECO:0000250|UniProtKB:Q9LJP4};
DE AltName: Full=Cellulose synthase-like protein C6 {ECO:0000303|PubMed:11027699};
DE Short=AtCslC6 {ECO:0000303|PubMed:11027699};
GN Name=CSLC6 {ECO:0000303|PubMed:11027699};
GN OrderedLocusNames=At3g07330 {ECO:0000312|Araport:AT3G07330};
GN ORFNames=F21O3.4 {ECO:0000312|EMBL:AAF02144.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [2]
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 [3]
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 [4]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=11027699; DOI=10.1104/pp.124.2.495;
RA Richmond T.A., Somerville C.R.;
RT "The cellulose synthase superfamily.";
RL Plant Physiol. 124:495-498(2000).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [6]
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 [7]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=32737163; DOI=10.1073/pnas.2007245117;
RA Kim S.-J., Chandrasekar B., Rea A.C., Danhof L., Zemelis-Durfee S.,
RA Thrower N., Shepard Z.S., Pauly M., Brandizzi F., Keegstra K.;
RT "The synthesis of xyloglucan, an abundant plant cell wall polysaccharide,
RT requires CSLC function.";
RL Proc. Natl. Acad. Sci. U.S.A. 117:20316-20324(2020).
CC -!- FUNCTION: Probable beta-1,4-glucan synthase rather involved in the
CC synthesis of the xyloglucan backbone than cellulose. Seems to work
CC simultaneously with xyloglucan 6-xylosyltransferase. Xyloglucan is a
CC noncellulosic polysaccharides of plant cell wall and consists of a
CC glucan backbone substituted by xylose, galactose and fucose.
CC {ECO:0000269|PubMed:32737163}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q9LJP4}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q9LJP4}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Mainly expressed in flowers and seeds, and, to a
CC lower extent, in seedlings, roots, leaves and stems.
CC {ECO:0000269|PubMed:32737163}.
CC -!- DISRUPTION PHENOTYPE: Normal xyloglucan (XyG) levels (PubMed:32737163).
CC Plants missing several xyloglucan synthases (e.g. CSLC4, CSLC5, CSLC6,
CC CSLC8 and CSLC12) have no detectable XyG levels and several associated
CC phenotypes including reduced stems height and leaves area, as well as
CC shorter root hairs and reduced pollen tube formation ability
CC (PubMed:32737163). {ECO:0000269|PubMed:32737163}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. Plant
CC cellulose synthase-like C subfamily. {ECO:0000305}.
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DR EMBL; AC009853; AAF02144.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74529.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM64747.1; -; Genomic_DNA.
DR EMBL; AY070454; AAL49857.1; -; mRNA.
DR EMBL; AY142677; AAN13215.1; -; mRNA.
DR RefSeq; NP_001326755.1; NM_001337702.1.
DR RefSeq; NP_187389.1; NM_111612.4.
DR AlphaFoldDB; Q9SRT3; -.
DR SMR; Q9SRT3; -.
DR BioGRID; 5256; 2.
DR IntAct; Q9SRT3; 2.
DR STRING; 3702.AT3G07330.1; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR iPTMnet; Q9SRT3; -.
DR PaxDb; Q9SRT3; -.
DR PRIDE; Q9SRT3; -.
DR ProteomicsDB; 224537; -.
DR EnsemblPlants; AT3G07330.1; AT3G07330.1; AT3G07330.
DR EnsemblPlants; AT3G07330.2; AT3G07330.2; AT3G07330.
DR GeneID; 819921; -.
DR Gramene; AT3G07330.1; AT3G07330.1; AT3G07330.
DR Gramene; AT3G07330.2; AT3G07330.2; AT3G07330.
DR KEGG; ath:AT3G07330; -.
DR Araport; AT3G07330; -.
DR TAIR; locus:2079661; AT3G07330.
DR eggNOG; ENOG502QTBF; Eukaryota.
DR HOGENOM; CLU_012856_1_0_1; -.
DR InParanoid; Q9SRT3; -.
DR OMA; VEVVYAW; -.
DR OrthoDB; 559375at2759; -.
DR PhylomeDB; Q9SRT3; -.
DR BioCyc; ARA:AT3G07330-MON; -.
DR PRO; PR:Q9SRT3; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SRT3; baseline and differential.
DR Genevisible; Q9SRT3; AT.
DR GO; GO:0005768; C:endosome; HDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000138; C:Golgi trans cisterna; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005802; C:trans-Golgi network; HDA:TAIR.
DR GO; GO:0016757; F:glycosyltransferase activity; IMP:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0071555; P:cell wall organization; IMP:UniProtKB.
DR GO; GO:0099402; P:plant organ development; IMP:UniProtKB.
DR GO; GO:0048868; P:pollen tube development; IMP:UniProtKB.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR001173; Glyco_trans_2-like.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR Pfam; PF13632; Glyco_trans_2_3; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW Cell wall biogenesis/degradation; Glycosyltransferase; Golgi apparatus;
KW Membrane; Phosphoprotein; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..682
FT /note="Probable xyloglucan glycosyltransferase 6"
FT /id="PRO_0000319343"
FT TRANSMEM 109..129
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 173..193
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 491..511
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 516..536
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 632..651
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 657..677
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 260
FT /evidence="ECO:0000255"
FT ACT_SITE 413
FT /evidence="ECO:0000255"
FT BINDING 319
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 321
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT MOD_RES 608
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LJP4"
SQ SEQUENCE 682 AA; 78371 MW; F6D0494C506E57B9 CRC64;
MSRSQNEEFQ QWWNKQRDRN NHDVLYAGDD EAFLTVEIRT PATVDPDKDR IRTRTVRQLS
RLYLLKFKQL ASSFLWIGNS FLYLVRTANR RIANDNPPSV SSSARLYRLI KGFLVVVVLL
LCFELAAYFK GWHFTPPSVA SAEVAVEVVY AWWLEIRASY LAPPLQSLTN VCIVLFLIQS
VDRLVLVLGC FWIKLRRIKP VASMEYPTKL VGEGVRLEDY PMVIVQIPMC NEKEVYQQSI
GAVCMLDWPR ERMLVQVLDD SSELDVQQLI KAEVQKWQQR GVRIVYRHRL IRTGYKAGNL
KAAMNCEYVK DYEFVAIFDA DFQPPADFLK KTVPHFKGNE ELALVQTRWA FVNKDENLLT
RLQNINLSFH FEVEQQVNGV FINFFGFNGT AGVWRIKALE DCGGWLERTT VEDMDIAVRA
HLCGWKFIYL NDVKCLCELP ESYEAYKKQQ YRWHSGPMQL FRLCFFDILR SKVSAAKKAN
MIFLFFLLRK LILPFYSFTL FCVILPLTMF FPEANLPSWV VCYIPGIMSI LNIIPAPRSF
PFIVPYLLFE NTMSVTKFGA MISGLFKFDS SYEWVVTKKL GRSSEADLVA YAESGSLVES
TTIQRSSSDS GLTELSKLGA AKKAGKTKRN RLYRTEIALA FILLAASVRS LLSAQGIHFY
FLLFQGITFV IVGLDLIGEQ VS
