CSLC4_ARATH
ID CSLC4_ARATH Reviewed; 673 AA.
AC Q9LJP4;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Xyloglucan glycosyltransferase 4 {ECO:0000303|PubMed:11027699};
DE EC=2.4.1.- {ECO:0000269|PubMed:17488821};
DE AltName: Full=Cellulose synthase-like protein C4 {ECO:0000303|PubMed:11027699};
DE Short=AtCslC4 {ECO:0000303|PubMed:11027699};
DE AltName: Full=Xyloglucan synthase 4 {ECO:0000303|PubMed:11027699};
GN Name=CSLC4 {ECO:0000303|PubMed:11027699};
GN OrderedLocusNames=At3g28180 {ECO:0000312|Araport:AT3G28180};
GN ORFNames=MIG10.8 {ECO:0000312|EMBL:BAB01433.1};
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=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(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 FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17488821; DOI=10.1073/pnas.0703133104;
RA Cocuron J.-C., Lerouxel O., Drakakaki G., Alonso A.P., Liepman A.H.,
RA Keegstra K., Raikhel N., Wilkerson C.G.;
RT "A gene from the cellulose synthase-like C family encodes a beta-1,4 glucan
RT synthase.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:8550-8555(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-581, AND IDENTIFICATION BY
RP 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 INTERACTION WITH CSLC4 AND XXT5, AND SUBCELLULAR LOCATION.
RX PubMed=22665445; DOI=10.1104/pp.112.199356;
RA Chou Y.H., Pogorelko G., Zabotina O.A.;
RT "Xyloglucan xylosyltransferases XXT1, XXT2, and XXT5 and the glucan
RT synthase CSLC4 form Golgi-localized multiprotein complexes.";
RL Plant Physiol. 159:1355-1366(2012).
RN [8]
RP FUNCTION, INTERACTION WITH FUT1; MUR3 AND XLT2, AND SUBCELLULAR LOCATION.
RX PubMed=25392066; DOI=10.1093/pcp/pcu161;
RA Chou Y.H., Pogorelko G., Young Z.T., Zabotina O.A.;
RT "Protein-protein interactions among xyloglucan-synthesizing enzymes and
RT formation of Golgi-localized multiprotein complexes.";
RL Plant Cell Physiol. 56:255-267(2015).
RN [9]
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: Beta-1,4-glucan synthase rather involved in the synthesis of
CC the xyloglucan backbone than cellulose. Seems to work simultaneously
CC with xyloglucan 6-xylosyltransferase. Xyloglucan is a noncellulosic
CC polysaccharides of plant cell wall and consists of a glucan backbone
CC substituted by xylose, galactose and fucose (PubMed:17488821,
CC PubMed:32737163). Associates with other xyloglucan-synthesizing enzymes
CC to form multiprotein complexes for xyloglucan synthesis in the Golgi
CC (PubMed:25392066). {ECO:0000269|PubMed:17488821,
CC ECO:0000269|PubMed:25392066, ECO:0000269|PubMed:32737163}.
CC -!- SUBUNIT: Homodimer (PubMed:22665445). Interacts with XXT5
CC (PubMed:22665445). Interacts with FUT1, MUR3 and XLT2
CC (PubMed:25392066). {ECO:0000269|PubMed:22665445,
CC ECO:0000269|PubMed:25392066}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:22665445, ECO:0000269|PubMed:25392066,
CC ECO:0000305|PubMed:17488821}; Multi-pass membrane protein
CC {ECO:0000305|PubMed:17488821}.
CC -!- TISSUE SPECIFICITY: Expressed in seedlings, roots, leaves, stems,
CC flowers and seeds. {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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP000415; BAB01433.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77412.1; -; Genomic_DNA.
DR EMBL; AY056286; AAL07135.1; -; mRNA.
DR EMBL; AY091433; AAM14372.1; -; mRNA.
DR RefSeq; NP_566835.1; NM_113737.3.
DR AlphaFoldDB; Q9LJP4; -.
DR SMR; Q9LJP4; -.
DR BioGRID; 7773; 6.
DR IntAct; Q9LJP4; 2.
DR STRING; 3702.AT3G28180.1; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR iPTMnet; Q9LJP4; -.
DR PaxDb; Q9LJP4; -.
DR PRIDE; Q9LJP4; -.
DR ProteomicsDB; 220364; -.
DR EnsemblPlants; AT3G28180.1; AT3G28180.1; AT3G28180.
DR GeneID; 822444; -.
DR Gramene; AT3G28180.1; AT3G28180.1; AT3G28180.
DR KEGG; ath:AT3G28180; -.
DR Araport; AT3G28180; -.
DR TAIR; locus:2089730; AT3G28180.
DR eggNOG; ENOG502QTBF; Eukaryota.
DR HOGENOM; CLU_012856_1_0_1; -.
DR InParanoid; Q9LJP4; -.
DR OMA; STKQFTW; -.
DR OrthoDB; 286400at2759; -.
DR PhylomeDB; Q9LJP4; -.
DR BioCyc; ARA:AT3G28180-MON; -.
DR BioCyc; MetaCyc:AT3G28180-MON; -.
DR BRENDA; 2.4.2.39; 399.
DR PRO; PR:Q9LJP4; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LJP4; baseline and differential.
DR Genevisible; Q9LJP4; 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; IPI: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..673
FT /note="Xyloglucan glycosyltransferase 4"
FT /id="PRO_0000319341"
FT TRANSMEM 90..110
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 144..164
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 469..489
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 494..514
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 623..643
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 648..668
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 238
FT /evidence="ECO:0000255"
FT ACT_SITE 391
FT /evidence="ECO:0000255"
FT BINDING 297
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 299
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT MOD_RES 581
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
SQ SEQUENCE 673 AA; 77516 MW; 1BC9A7E77D45D4A7 CRC64;
MAPNSVAVTM EKPDNFSLLE INGSDPSSFP DKRKSISPKQ FSWFLLLKAH RLISCLSWLV
SSVKKRIAFS AKNINEEEDP KSRGKQMYRF IKACLVISII ALSIEIVAHF KKWNLDLINR
PSWEVYGLVE WSYMAWLSFR SDYIAPLVIS LSRFCTVLFL IQSLDRLVLC LGCFWIKFKK
IEPKLTEESI DLEDPSSFPM VLIQIPMCNE REVYEQSIGA ASQLDWPKDR ILIQVLDDSD
DPNLQLLIKE EVSVWAEKGV NIIYRHRLIR TGYKAGNLKS AMTCDYVKDY EFVTIFDADF
TPNPDFLKKT VPHFKGNPEL GLVQARWSFV NKDENLLTRL QNINLCFHFE VEQQVNGVFL
NFFGFNGTAG VWRIKALEES GGWLERTTVE DMDIAVRAHL NGWKFIYLND VEVTCELPES
YEAYKKQQHR WHSGPMQLFR LCLPSIIKSK ISVWKKANLI FLFFLLRKLI LPFYSFTLFC
IILPLTMFIP EAELPLWIIC YVPIFISLLN ILPSPKSFPF LVPYLLFENT MSITKFNAMI
SGLFQFGSAY EWVVTKKTGR SSESDLLAFA EKEEKLHRRN SESGLELLSK LKEQETNLVG
QETVKKSLGG LMRPKNKKKT NMVFKKELGL AFLLLTAAAR SFLSAHGLHF YFLLFQGLSF
LVVGLDLIGE QIS
