CSLCC_ARATH
ID CSLCC_ARATH Reviewed; 699 AA.
AC Q9ZQB9;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Probable xyloglucan glycosyltransferase 12 {ECO:0000303|PubMed:11027699};
DE EC=2.4.1.- {ECO:0000250|UniProtKB:Q9LJP4};
DE AltName: Full=Cellulose synthase-like protein C12 {ECO:0000303|PubMed:11027699};
DE Short=AtCslC12 {ECO:0000303|PubMed:11027699};
GN Name=CSLC12 {ECO:0000303|PubMed:11027699};
GN OrderedLocusNames=At4g07960 {ECO:0000312|Araport:AT4G07960};
GN ORFNames=F1K3.3 {ECO:0000312|EMBL:AAD15482.1};
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=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 [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=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
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].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) 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 UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-617 AND LYS-620, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT "Multidimensional protein identification technology (MudPIT) analysis of
RT ubiquitinated proteins in plants.";
RL Mol. Cell. Proteomics 6:601-610(2007).
RN [8]
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:0000305}.
CC -!- TISSUE SPECIFICITY: Mainly expressed in roots, flowers and seeds, and,
CC at very low levels, in seedlings, 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; AC006266; AAD15482.1; -; Genomic_DNA.
DR EMBL; AL161508; CAB77947.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82586.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM66907.1; -; Genomic_DNA.
DR EMBL; AK118480; BAC43084.1; -; mRNA.
DR EMBL; AY087066; AAM64627.1; -; mRNA.
DR EMBL; BT008770; AAP68209.1; -; mRNA.
DR PIR; B85078; B85078.
DR RefSeq; NP_001328773.1; NM_001340568.1.
DR RefSeq; NP_192536.1; NM_116866.3.
DR AlphaFoldDB; Q9ZQB9; -.
DR SMR; Q9ZQB9; -.
DR STRING; 3702.AT4G07960.1; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR iPTMnet; Q9ZQB9; -.
DR PaxDb; Q9ZQB9; -.
DR PRIDE; Q9ZQB9; -.
DR ProteomicsDB; 222663; -.
DR EnsemblPlants; AT4G07960.1; AT4G07960.1; AT4G07960.
DR EnsemblPlants; AT4G07960.2; AT4G07960.2; AT4G07960.
DR GeneID; 826301; -.
DR Gramene; AT4G07960.1; AT4G07960.1; AT4G07960.
DR Gramene; AT4G07960.2; AT4G07960.2; AT4G07960.
DR KEGG; ath:AT4G07960; -.
DR Araport; AT4G07960; -.
DR TAIR; locus:2120532; AT4G07960.
DR eggNOG; ENOG502QTBF; Eukaryota.
DR HOGENOM; CLU_012856_1_0_1; -.
DR InParanoid; Q9ZQB9; -.
DR OMA; YLYSLDF; -.
DR OrthoDB; 404510at2759; -.
DR PhylomeDB; Q9ZQB9; -.
DR BioCyc; ARA:AT4G07960-MON; -.
DR PRO; PR:Q9ZQB9; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9ZQB9; baseline and differential.
DR Genevisible; Q9ZQB9; 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:0009506; C:plasmodesma; 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 Isopeptide bond; Membrane; Phosphoprotein; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix; Ubl conjugation.
FT CHAIN 1..699
FT /note="Probable xyloglucan glycosyltransferase 12"
FT /id="PRO_0000319345"
FT TRANSMEM 126..146
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 194..214
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 511..531
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 536..556
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 649..668
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 674..694
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 616..646
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 616..637
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 280
FT /evidence="ECO:0000255"
FT ACT_SITE 433
FT /evidence="ECO:0000255"
FT BINDING 339
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 341
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT MOD_RES 626
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LJP4"
FT CROSSLNK 617
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:17272265"
FT CROSSLNK 620
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:17272265"
SQ SEQUENCE 699 AA; 80123 MW; F9333F0ACFD5A0FD CRC64;
MAPKFEWWAK GNNNNTRKGT PVVVKMENPN NWSMVELESP SHDDFLVRTH EKSRNKNARQ
LTWVLLLKAH RAAGCLTSLG SALFALGTAV RRRIAAGRTD IEISSSGVGS LQKQNHTKKS
KLFYSCLKVF LWLSLILLGF EIAAYFKGWS FGTSKLQLQF IFNKGFFDWV YTRWVLLRVE
YLAPPLQFLA NGCIVLFLVQ SLDRLILCLG CFWIRFKKIK PVPKPDSISD LESGDNGAFL
PMVLVQIPMC NEKEVYQQSI AAVCNLDWPK GKILIQILDD SDDPITQSLI KEEVHKWQKL
GARIVYRHRV NREGYKAGNL KSAMNCSYVK DYEFVAIFDA DFQPLPDFLK KTIPHFKDNE
EIGLVQARWS FVNKEENLLT RLQNINLAFH FEVEQQVNSV FLNFFGFNGT AGVWRIKALE
DSGGWLERTT VEDMDIAVRA HLHGWKFVFL NDVECQCELP ESYEAYRKQQ HRWHSGPMQL
FRLCLPAVIK SKISIGKKFN LIFLFFLLRK LILPFYSFTL FCIILPMTMF VPEAELPAWV
VCYIPATMSF LNILPAPKSF PFIVPYLLFE NTMSVTKFNA MVSGLFQLGS AYEWVVTKKS
GRSSEGDLAA LVEKDEKTTK HQRGVSAPET EAEKKAEKTK RKKKKHNRIY MKELSLAFLL
LTAATRSLLS AQGIHFYFLL FQGISFLLVG LDLIGEQVE
