CSLC5_ARATH
ID CSLC5_ARATH Reviewed; 692 AA.
AC Q9SB75; A0A178UYZ0; Q56Z56; W8PV45;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Probable xyloglucan glycosyltransferase 5 {ECO:0000303|PubMed:11027699};
DE EC=2.4.1.- {ECO:0000250|UniProtKB:Q9LJP4};
DE AltName: Full=Cellulose synthase-like protein C5 {ECO:0000303|PubMed:11027699};
DE Short=AtCslC5 {ECO:0000303|PubMed:11027699};
GN Name=CSLC5 {ECO:0000303|PubMed:11027699};
GN OrderedLocusNames=At4g31590 {ECO:0000312|Araport:AT4G31590};
GN ORFNames=F28M20.220 {ECO:0000312|EMBL:CAA19764.1};
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 [MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=24905498; DOI=10.1111/tpj.12577;
RA Lao J., Oikawa A., Bromley J.R., McInerney P., Suttangkakul A.,
RA Smith-Moritz A.M., Plahar H., Chiu T.-Y., Gonzalez Fernandez-Nino S.M.G.,
RA Ebert B., Yang F., Christiansen K.M., Hansen S.F., Stonebloom S.,
RA Adams P.D., Ronald P.C., Hillson N.J., Hadi M.Z., Vega-Sanchez M.E.,
RA Loque D., Scheller H.V., Heazlewood J.L.;
RT "The plant glycosyltransferase clone collection for functional genomics.";
RL Plant J. 79:517-529(2014).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 534-692.
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 (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Root;
RX PubMed=18433157; DOI=10.1021/pr8000173;
RA de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,
RA Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J.,
RA Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H.;
RT "Site-specific phosphorylation profiling of Arabidopsis proteins by mass
RT spectrometry and peptide chip analysis.";
RL J. Proteome Res. 7:2458-2470(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-614, 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 [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: 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD95029.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; KJ138731; AHL38671.1; -; mRNA.
DR EMBL; AL031004; CAA19764.1; -; Genomic_DNA.
DR EMBL; AL161579; CAB79877.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85933.1; -; Genomic_DNA.
DR EMBL; BT003334; AAO29953.1; -; mRNA.
DR EMBL; BT008423; AAP37782.1; -; mRNA.
DR EMBL; AK221113; BAD95029.1; ALT_INIT; mRNA.
DR PIR; T05111; T05111.
DR RefSeq; NP_194887.1; NM_119308.3.
DR AlphaFoldDB; Q9SB75; -.
DR BioGRID; 14572; 3.
DR IntAct; Q9SB75; 3.
DR STRING; 3702.AT4G31590.1; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR iPTMnet; Q9SB75; -.
DR PaxDb; Q9SB75; -.
DR PRIDE; Q9SB75; -.
DR ProteomicsDB; 224425; -.
DR EnsemblPlants; AT4G31590.1; AT4G31590.1; AT4G31590.
DR GeneID; 829286; -.
DR Gramene; AT4G31590.1; AT4G31590.1; AT4G31590.
DR KEGG; ath:AT4G31590; -.
DR Araport; AT4G31590; -.
DR TAIR; locus:2124804; AT4G31590.
DR eggNOG; ENOG502QTBF; Eukaryota.
DR HOGENOM; CLU_012856_1_0_1; -.
DR InParanoid; Q9SB75; -.
DR OMA; HSAYISW; -.
DR OrthoDB; 312652at2759; -.
DR PhylomeDB; Q9SB75; -.
DR BioCyc; ARA:AT4G31590-MON; -.
DR PRO; PR:Q9SB75; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SB75; baseline and differential.
DR Genevisible; Q9SB75; AT.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; Glycoprotein; Glycosyltransferase;
KW Golgi apparatus; Membrane; Phosphoprotein; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..692
FT /note="Probable xyloglucan glycosyltransferase 5"
FT /id="PRO_0000319342"
FT TRANSMEM 106..126
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 180..200
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 497..517
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 522..542
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 646..666
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 667..687
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 266
FT /evidence="ECO:0000255"
FT ACT_SITE 419
FT /evidence="ECO:0000255"
FT BINDING 325
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 327
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT MOD_RES 614
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT CARBOHYD 29
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 394
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 692 AA; 79421 MW; B8F655B91491EA69 CRC64;
MAPRLDFSDW WAKDTRKGTP VVVKMENPNY SVVEIDGPDS AFRPVEKSRG KNAKQVTWVL
LLKAHRAVGC LTWLATVFWS LLGAIKKRLS FTHPLGSEKL GRDRWLFTAI KLFLAVSLVI
LGFEIVAYFR GWHYFQSPSL HIPTSTLEIQ SLFHLVYVGW LTLRADYIAP PIKALSKFCI
VLFLIQSVDR LVLCLGCFWI KYKKIKPRFD EEPFRNDDAE GSGSEYPMVL VQIPMCNERE
VYEQSISAVC QLDWPKDRIL VQVLDDSNDE SIQQLIKAEV AKWSQKGVNI IYRHRLVRTG
YKAGNLKSAM SCDYVEAYEY VAIFDADFQP TPDFLKLTVP HFKDNPELGL VQARWTFVNK
DENLLTRLQN INLCFHFEVE QQVNGVFLNF FGFNGTAGVW RIKALEESGG WLERTTVEDM
DIAVRAHLHG WKFIYLNDVK VLCEVPESYE AYKKQQHRWH SGPMQLFRLC LGSILTSKIA
IWKKANLILL FFLLRKLILP FYSFTLFCII LPLTMFVPEA ELPVWVICYI PVFMSFLNLL
PSPKSFPFIV PYLLFENTMS VTKFNAMVSG LFQLGSSYEW IVTKKAGRSS ESDLLSITEK
ETPTKKSQLL RGVSDSELLE LSQLEEQKQA VSKKPVKKTN KIYHKELALA FLLLTAALRS
LLAAQGVHFY FLLFQGVTFL LVGLDLIGEQ MS
