CSLC8_ARATH
ID CSLC8_ARATH Reviewed; 690 AA.
AC Q9SJA2; Q0WN05;
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 8 {ECO:0000303|PubMed:11027699};
DE EC=2.4.1.- {ECO:0000250|UniProtKB:Q9LJP4};
DE AltName: Full=Cellulose synthase-like protein C8 {ECO:0000303|PubMed:11027699};
DE Short=AtCslC8 {ECO:0000303|PubMed:11027699};
GN Name=CSLC8 {ECO:0000303|PubMed:11027699};
GN OrderedLocusNames=At2g24630 {ECO:0000312|Araport:AT2G24630};
GN ORFNames=F25P17.7 {ECO:0000312|EMBL:AAD23884.1};
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(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;
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 (JUL-2006) to the EMBL/GenBank/DDBJ databases.
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, 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 flowers and seeds, and, at very
CC low levels, 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; AC006954; AAD23884.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07606.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM62729.1; -; Genomic_DNA.
DR EMBL; AK229651; BAF01495.1; -; mRNA.
DR PIR; A84639; A84639.
DR RefSeq; NP_001318283.1; NM_001335941.1.
DR RefSeq; NP_180039.1; NM_128024.3.
DR AlphaFoldDB; Q9SJA2; -.
DR SMR; Q9SJA2; -.
DR BioGRID; 2351; 14.
DR IntAct; Q9SJA2; 14.
DR STRING; 3702.AT2G24630.1; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR iPTMnet; Q9SJA2; -.
DR PaxDb; Q9SJA2; -.
DR PRIDE; Q9SJA2; -.
DR ProteomicsDB; 224426; -.
DR EnsemblPlants; AT2G24630.1; AT2G24630.1; AT2G24630.
DR EnsemblPlants; AT2G24630.2; AT2G24630.2; AT2G24630.
DR GeneID; 816999; -.
DR Gramene; AT2G24630.1; AT2G24630.1; AT2G24630.
DR Gramene; AT2G24630.2; AT2G24630.2; AT2G24630.
DR KEGG; ath:AT2G24630; -.
DR Araport; AT2G24630; -.
DR TAIR; locus:2046688; AT2G24630.
DR eggNOG; ENOG502QTBF; Eukaryota.
DR HOGENOM; CLU_012856_1_0_1; -.
DR InParanoid; Q9SJA2; -.
DR OMA; WGAMETR; -.
DR OrthoDB; 312652at2759; -.
DR PhylomeDB; Q9SJA2; -.
DR BioCyc; ARA:AT2G24630-MON; -.
DR PRO; PR:Q9SJA2; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SJA2; baseline and differential.
DR Genevisible; Q9SJA2; 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 2: Evidence at transcript level;
KW Cell wall biogenesis/degradation; Glycosyltransferase; Golgi apparatus;
KW Membrane; Phosphoprotein; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..690
FT /note="Probable xyloglucan glycosyltransferase 8"
FT /id="PRO_0000319344"
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 640..660
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 665..685
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:0000250|UniProtKB:Q9LJP4"
FT CONFLICT 24
FT /note="K -> E (in Ref. 3; BAF01495)"
FT /evidence="ECO:0000305"
FT CONFLICT 591
FT /note="E -> G (in Ref. 3; BAF01495)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 690 AA; 79489 MW; 67EBB5A18AC51676 CRC64;
MAPRFDFSDL WAKETRRGTP VVVKMENPNY SIVEVEEPDS AFQPMEKSRG KNAKQVTWVL
LLKAHKAVGC LTWVATVFWS LLGSVKRRLS FTHPLGSERL GRDGWLFSAI KLFLVASLAI
LAFELVAYYR GWHYFKNPNL HIPTSKLEIQ SLLHLFYVGW LSLRADYIAP PIKALSKFCI
VLFLVQSVDR LILCLGCLWI KFKKIKPRID EEHFRNDDFE GSGSEYPMVL VQIPMCNERE
VYEQSISAVC QLDWPKDRLL VQVLDDSDDE SIQELIRDEV TKWSQKGVNI IYRHRLVRTG
YKAGNLKSAM SCDYVEAYEF VAIFDADFQP NSDFLKLTVP HFKEKPELGL VQARWAFVNK
DENLLTRLQN INLCFHFEVE QQVNGVFLNF FGFNGTAGVW RIKALEESGG WLERTTVEDM
DIAVRAHLHG WKFIYLNDVK VLCEVPESYE AYKKQQHRWH SGPMQLFRLC LRSILTSKIA
MWKKANLILL FFLLRKLILP FYSFTLFCVI LPITMFVPEA ELPIWVICYV PIFMSLLNIL
PAPKSFPFIV PYLLFENTMS VTKFNAMVSG LFQLGSSYEW IVTKKAGRSS ESDLLALTDK
ESEKMPNQIL RGVSDSELLE ISQVEEQKKQ PVSVKKTNKI FHKELALAFL LLTAAVRSLL
ASQGVHFYFL LFQGLTFLLV GLDLIGEQMS
