CSLB5_ARATH
ID CSLB5_ARATH Reviewed; 757 AA.
AC Q0WT40; O23383; Q7XA79;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Cellulose synthase-like protein B5;
DE Short=AtCslB5;
DE EC=2.4.1.-;
GN Name=CSLB5; OrderedLocusNames=At4g15290; ORFNames=dl3690c, FCAALL.256;
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 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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 97-757.
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 [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 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
CC vascular tissue. Expressed in the root cap.
CC {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=CAB10308.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB78571.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; Z97338; CAB10308.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161541; CAB78571.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE83581.1; -; Genomic_DNA.
DR EMBL; AK227722; BAE99708.1; -; mRNA.
DR EMBL; BT010152; AAQ22621.1; -; mRNA.
DR PIR; B71417; B71417.
DR RefSeq; NP_193264.3; NM_117617.6.
DR AlphaFoldDB; Q0WT40; -.
DR SMR; Q0WT40; -.
DR STRING; 3702.AT4G15290.1; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR PaxDb; Q0WT40; -.
DR PRIDE; Q0WT40; -.
DR ProteomicsDB; 220362; -.
DR EnsemblPlants; AT4G15290.1; AT4G15290.1; AT4G15290.
DR GeneID; 827195; -.
DR Gramene; AT4G15290.1; AT4G15290.1; AT4G15290.
DR KEGG; ath:AT4G15290; -.
DR Araport; AT4G15290; -.
DR TAIR; locus:2129915; AT4G15290.
DR eggNOG; ENOG502QTT0; Eukaryota.
DR HOGENOM; CLU_001418_3_3_1; -.
DR InParanoid; Q0WT40; -.
DR OMA; NESEFPA; -.
DR OrthoDB; 267925at2759; -.
DR PhylomeDB; Q0WT40; -.
DR BioCyc; ARA:AT4G15290-MON; -.
DR PRO; PR:Q0WT40; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q0WT40; baseline and differential.
DR Genevisible; Q0WT40; AT.
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 GO; GO:0048767; P:root hair elongation; IMP:TAIR.
DR Gene3D; 3.90.550.10; -; 1.
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 B5"
FT /id="PRO_0000319339"
FT TRANSMEM 24..44
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 50..70
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 531..551
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 572..592
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 613..633
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 671..691
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 704..724
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"
FT CONFLICT 256
FT /note="Y -> H (in Ref. 4; BAE99708 and 5; AAQ22621)"
FT /evidence="ECO:0000305"
FT CONFLICT 297
FT /note="M -> T (in Ref. 5; AAQ22621)"
FT /evidence="ECO:0000305"
FT CONFLICT 757
FT /note="K -> E (in Ref. 4; BAE99708)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 757 AA; 85201 MW; 41A0C98755809530 CRC64;
MADSSSSLHP LCERISHKSY VLRAVDLTIL GLLYSLLLYR ILHISENDNV WLLAFFCESC
FSLVWLIFTC LKWSPAEDIP YINTLNERVH DLPSLDMFVP TADTVRESPI ITVNTVLSLL
AVNYPANKLA CYVSDDGCSP LTYFSLKEAS KFVKIWAPFC KKYNVRVRAP FRYFLNPLVA
TDDSVFSKDW KMMKREYVKL CRKVEDATGD SHWLDADDDF EAFSNTKPND HSTIVKVVWE
NKGGVGDEKE VPHLVYISRE KRPNYLHHYK TGAMNFLLRV SGLMTNAPYT LNVDCDMYAN
EPDVVRQAMC VFLQNSKNSN HCAFVQFPQK FYDSYTNELA VLQSILGRGV AGIQGPFYIG
TGCFHTRRVM YGLSSDDLED NGNISQVATR EFLAEDSLVR KYGNSKELVK SVVDALQRKS
NPQKSLANLI EAAQEVGHCH YEYQTSWGNL GWMYDSVAED INTSVGIHLR GWTSSFISPD
PPAFIGSTPT LGLEAIVQQR RWATGAIEVL FNKQSPFMGM FHGKIKFRQR LAYFWALMCL
RSIPELIYCL LPAYCLLHDS ALFPKGPCLC TIVTLVGMHC LYSLWQFMSL GFSVQSWYVV
QSLWRIIATS SWLFSIQDII LKLLGISQIG FVIAKKTIPE TKSVYESKPS QGEDDVPKLN
LGKFEFDSSG LFIPGTFIML VNLAALAGYL VRLQRSSCSH GGGGSGLAEA CGCILVVMLF
LPFLKGLFEH GKYSIPLSTL SKAAFLTVLF VFFCVGK
