CSLB6_ARATH
ID CSLB6_ARATH Reviewed; 757 AA.
AC O23386; F4JJG5;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 25-MAY-2022, entry version 111.
DE RecName: Full=Cellulose synthase-like protein B6;
DE Short=AtCslB6;
DE EC=2.4.1.-;
GN Name=CSLB6; OrderedLocusNames=At4g15320; ORFNames=dl3705c, FCAALL.268;
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=9461215; DOI=10.1038/35140;
RA Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT thaliana.";
RL Nature 391:485-488(1998).
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 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 TISSUE SPECIFICITY.
RX PubMed=11554468; DOI=10.1023/a:1010627314782;
RA Richmond T.A., Somerville C.R.;
RT "Integrative approaches to determining Csl function.";
RL Plant Mol. Biol. 47:131-143(2001).
CC -!- FUNCTION: Thought to be a Golgi-localized beta-glycan synthase that
CC polymerize the backbones of noncellulosic polysaccharides
CC (hemicelluloses) of plant cell wall.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Multi-
CC pass membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in young seedlings, primarily in the root
CC vascular tissue. {ECO:0000269|PubMed:11554468}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. Plant
CC cellulose synthase-like B subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AEE83584.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB10311.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB78574.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; Z97338; CAB10311.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161541; CAB78574.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE83584.1; ALT_SEQ; Genomic_DNA.
DR PIR; E71417; E71417.
DR RefSeq; NP_193267.1; NM_117620.1.
DR AlphaFoldDB; O23386; -.
DR SMR; O23386; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR PeptideAtlas; O23386; -.
DR GeneID; 827198; -.
DR KEGG; ath:AT4G15320; -.
DR Araport; AT4G15320; -.
DR InParanoid; O23386; -.
DR OrthoDB; 267925at2759; -.
DR PhylomeDB; O23386; -.
DR PRO; PR:O23386; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O23386; baseline and differential.
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:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0016760; F:cellulose synthase (UDP-forming) activity; IEA:InterPro.
DR GO; GO:0051753; F:mannan synthase activity; IBA:GO_Central.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0030244; P:cellulose biosynthetic process; IEA:InterPro.
DR GO; GO:0009833; P:plant-type primary cell wall biogenesis; IBA:GO_Central.
DR Gene3D; 3.90.550.10; -; 2.
DR InterPro; IPR005150; Cellulose_synth.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR Pfam; PF03552; Cellulose_synt; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 2: Evidence at transcript level;
KW Cell wall biogenesis/degradation; Glycosyltransferase; Golgi apparatus;
KW Membrane; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..757
FT /note="Cellulose synthase-like protein B6"
FT /id="PRO_0000319340"
FT TRANSMEM 24..44
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 50..70
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 530..550
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 568..588
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 612..632
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 672..692
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 706..726
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 735..755
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 136
FT /evidence="ECO:0000255"
FT ACT_SITE 460
FT /evidence="ECO:0000255"
SQ SEQUENCE 757 AA; 85579 MW; 5E877E3183424670 CRC64;
MADSSSSLLP LCERISHKSY ILRIVDLTIL VLLFSLLWYR ILHMCENNTI WLVAFLCESC
FSFMWLIITC IKWSPAEDKP YPNRLDERVH DLPSVDMFVP TADPVREPPI IVVNTVLSLL
AVNYPANKLA CYVSDDGCSP LTYFSLKEAS KFVKIWAPFC KKYNVRVRAP FRYFLNPLVA
TDDSVFSKDW KMMKREYVKL CRKVEDATGD SHWLDADDDF EAFSNTKPND HSTIVKVVWE
NKGGVGDEKE VPHLVYISRE KRPNYLHHYK TGAMNFLLRV SGLMTNAPYM LNVDCDMYAN
EPDVVRQAMC VFLQNSKNSN HCAFVQFPQN FYDSYTNELV VLQHYMKRGV AGIQGPIYIG
SGCFHTRRVM YGLSSDDLED DGSLSSVASR EFLSEDSLVR KYGSSKELVK SVVDALQRKS
NPQKSLANLV EAAQEVGHCH YEYQTSWGNL GWLYDSVAED TNTSIGIHLR GWTSSFISPD
PPAFLGSTPS VGPEAIVQHR RWATGSIEVL FNKQSPLIGF RRKIKFRQRL AYFWVLMCIR
SIPELVYCLL PAYCLLNNSA LFPKGPCLGI IVTLVGMHCL YTLWQFMILG FSVKSWYVSQ
SLWRIIATSS WLFSIQDIIL KLLGISKIGF IVAKKNMPET RSGYESKSKP SQGEDDGLKL
ELGKFEFDSS CHFIPGTFIM LVNLAALAGF LVRLQRSSYS HGGGGGSALA ETCGCAMIVM
LFFPFLKGLF EHGKYGIPLS TLSKAAFLTV LFASYHL
