CSLA9_ARATH
ID CSLA9_ARATH Reviewed; 533 AA.
AC Q9LZR3; Q0WVY0;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Glucomannan 4-beta-mannosyltransferase 9 {ECO:0000305};
DE EC=2.4.1.32 {ECO:0000269|PubMed:15647349, ECO:0000269|PubMed:17307900};
DE AltName: Full=Cellulose synthase-like protein A9 {ECO:0000303|PubMed:14612582};
DE Short=AtCslA9 {ECO:0000303|PubMed:14612582};
DE AltName: Full=Glucomannan synthase {ECO:0000305};
DE AltName: Full=Mannan synthase 9 {ECO:0000305};
DE AltName: Full=Protein RESISTANT TO AGROBACTERIUM TRANSFORMATION 4 {ECO:0000303|PubMed:14612582};
GN Name=CSLA9 {ECO:0000303|PubMed:14612582};
GN Synonyms=RAT4 {ECO:0000303|PubMed:14612582}; OrderedLocusNames=At5g03760;
GN ORFNames=F17C15.180;
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=9330910; DOI=10.1093/dnares/4.3.215;
RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT features of the 1.6 Mb regions covered by twenty physically assigned P1
RT clones.";
RL DNA Res. 4:215-230(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
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].
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 [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 FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=14612582; DOI=10.1104/pp.103.030726;
RA Zhu Y., Nam J., Carpita N.C., Matthysse A.G., Gelvin S.B.;
RT "Agrobacterium-mediated root transformation is inhibited by mutation of an
RT Arabidopsis cellulose synthase-like gene.";
RL Plant Physiol. 133:1000-1010(2003).
RN [8]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=15647349; DOI=10.1073/pnas.0409179102;
RA Liepman A.H., Wilkerson C.G., Keegstra K.;
RT "Expression of cellulose synthase-like (Csl) genes in insect cells reveals
RT that CslA family members encode mannan synthases.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:2221-2226(2005).
RN [9]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=17307900; DOI=10.1104/pp.106.093989;
RA Liepman A.H., Nairn C.J., Willats W.G.T., Soerensen I., Roberts A.W.,
RA Keegstra K.;
RT "Functional genomic analysis supports conservation of function among
RT cellulose synthase-like a gene family members and suggests diverse roles of
RT mannans in plants.";
RL Plant Physiol. 143:1881-1893(2007).
CC -!- FUNCTION: Possesses glucomannan synthase and mannan synthase activities
CC in vitro. Mannan synthase consists of a 4-beta-mannosyltransferase
CC activity on mannan using GDP-mannose. The beta-1,4-mannan product is
CC the backbone for galactomannan synthesis by galactomannan
CC galactosyltransferase. Galactomannan is a noncellulosic polysaccharides
CC of plant cell wall (PubMed:15647349, PubMed:17307900). Required for
CC lateral root development (PubMed:14612582).
CC {ECO:0000269|PubMed:14612582, ECO:0000269|PubMed:15647349,
CC ECO:0000269|PubMed:17307900}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GDP-mannose + (glucomannan)n = GDP + (glucomannan)n+1.;
CC EC=2.4.1.32; Evidence={ECO:0000269|PubMed:15647349,
CC ECO:0000269|PubMed:17307900};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Multi-
CC pass membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in cotyledons at the base of the
CC hypocotyls, in root elongation zone, lateral root primordia, vascular
CC system of young leaves, abscission zone of the pedicle,.
CC {ECO:0000269|PubMed:14612582}.
CC -!- DISRUPTION PHENOTYPE: Plants develop approximately half the number of
CC lateral roots without affecting significantly aerial parts development,
CC and are resistant to A.tumefaciens transformation.
CC {ECO:0000269|PubMed:14612582}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. Plant
CC cellulose synthase-like A subfamily. {ECO:0000305}.
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DR EMBL; AB005235; BAB08601.1; -; Genomic_DNA.
DR EMBL; AL162506; CAB82941.1; -; Genomic_DNA.
DR EMBL; CP002688; AED90651.1; -; Genomic_DNA.
DR EMBL; AY060563; AAL31192.1; -; mRNA.
DR EMBL; AY149935; AAN31089.1; -; mRNA.
DR EMBL; AK226605; BAE98718.1; -; mRNA.
DR PIR; T48403; T48403.
DR RefSeq; NP_195996.1; NM_120457.4.
DR AlphaFoldDB; Q9LZR3; -.
DR SMR; Q9LZR3; -.
DR BioGRID; 17010; 1.
DR IntAct; Q9LZR3; 1.
DR STRING; 3702.AT5G03760.1; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR PaxDb; Q9LZR3; -.
DR PRIDE; Q9LZR3; -.
DR ProteomicsDB; 220499; -.
DR EnsemblPlants; AT5G03760.1; AT5G03760.1; AT5G03760.
DR GeneID; 831734; -.
DR Gramene; AT5G03760.1; AT5G03760.1; AT5G03760.
DR KEGG; ath:AT5G03760; -.
DR Araport; AT5G03760; -.
DR TAIR; locus:2144638; AT5G03760.
DR eggNOG; ENOG502QR7J; Eukaryota.
DR HOGENOM; CLU_012856_2_0_1; -.
DR InParanoid; Q9LZR3; -.
DR OMA; WIKQRAR; -.
DR OrthoDB; 559375at2759; -.
DR PhylomeDB; Q9LZR3; -.
DR BioCyc; ARA:AT5G03760-MON; -.
DR PRO; PR:Q9LZR3; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LZR3; baseline and differential.
DR Genevisible; Q9LZR3; AT.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
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:0047259; F:glucomannan 4-beta-mannosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016757; F:glycosyltransferase activity; IBA:GO_Central.
DR GO; GO:0051753; F:mannan synthase activity; IDA:TAIR.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009294; P:DNA-mediated transformation; IMP:TAIR.
DR GO; GO:0009617; P:response to bacterium; IMP:TAIR.
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 Membrane; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..533
FT /note="Glucomannan 4-beta-mannosyltransferase 9"
FT /id="PRO_0000319330"
FT TRANSMEM 37..57
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 368..388
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 404..426
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 483..503
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 510..530
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 136
FT /evidence="ECO:0000255"
FT ACT_SITE 289
FT /evidence="ECO:0000255"
FT BINDING 195
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 197
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT CONFLICT 399
FT /note="V -> F (in Ref. 5; BAE98718)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 533 AA; 60919 MW; 57EA25A041791170 CRC64;
MELGDTTSVI PDSFMGYRDD ITMQMSMVLD QIRAPLIVPA LRLGVYICLT MSVMLFVERV
YMGIVISLVK LFGRKPDKRF KYEPIKDDIE LGNSAYPMVL IQIPMFNERE VYQLSIGAAC
GLSWPSDRIV IQVLDDSTDP TIKDLVEMEC SRWASKGVNI KYEIRDNRNG YKAGALKEGM
KKSYVKSCDY VAIFDADFQP EADFLWRTVP YLLHNPKLAL VQARWKFVNS DECLMTRMQE
MSLDYHFTVE QEVGSSTYAF FGFNGTAGIW RISALNEAGG WKDRTTVEDM DLAVRASLKG
WKFLYLGSLK VKNELPSTFK AYRYQQHRWS CGPANLFRKM AFEIMTNKNV TLWKKVHVIY
SFFVVRKLVA HIVTFIFYCV ILPATVLVPE VTVPKWGAVY IPSVITLLNA VGTPRSLHLM
VFWILFENVM SLHRTKATFI GLLEGGRVNE WIVTEKLGDV KAKSATKTSK KVIRFRFGDR
IHVLELGVGM YLLFVGCYDA FFGKNHYYLY LFAQAIAFFI AGFGQIGTIV PNH
