CSLAF_ARATH
ID CSLAF_ARATH Reviewed; 537 AA.
AC Q9T0L2;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Probable glucomannan 4-beta-mannosyltransferase 15 {ECO:0000305};
DE EC=2.4.1.32 {ECO:0000250|UniProtKB:Q9LZR3};
DE AltName: Full=Cellulose synthase-like protein A15 {ECO:0000303|PubMed:11027699};
DE Short=AtCslA15 {ECO:0000303|PubMed:11027699};
DE AltName: Full=Glucomannan synthase {ECO:0000305};
DE AltName: Full=Mannan synthase 15 {ECO:0000305};
GN Name=CSLA15 {ECO:0000303|PubMed:11027699}; OrderedLocusNames=At4g13410;
GN ORFNames=T9E8.150;
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 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).
CC -!- FUNCTION: Probable mannan synthase which consists of a 4-beta-
CC mannosyltransferase activity on mannan using GDP-mannose. The beta-1,4-
CC mannan product is the backbone for galactomannan synthesis by
CC galactomannan galactosyltransferase. Galactomannan is a noncellulosic
CC polysaccharides of plant cell wall. {ECO:0000250|UniProtKB:Q9LZR3}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GDP-mannose + (glucomannan)n = GDP + (glucomannan)n+1.;
CC EC=2.4.1.32; Evidence={ECO:0000250|UniProtKB:Q9LZR3};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Multi-
CC pass membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. Plant
CC cellulose synthase-like A subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB40776.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB78383.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL049608; CAB40776.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161536; CAB78383.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE83276.1; -; Genomic_DNA.
DR PIR; T06298; T06298.
DR RefSeq; NP_193077.2; NM_117415.3.
DR AlphaFoldDB; Q9T0L2; -.
DR STRING; 3702.AT4G13410.1; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR PaxDb; Q9T0L2; -.
DR PRIDE; Q9T0L2; -.
DR EnsemblPlants; AT4G13410.1; AT4G13410.1; AT4G13410.
DR GeneID; 826972; -.
DR Gramene; AT4G13410.1; AT4G13410.1; AT4G13410.
DR KEGG; ath:AT4G13410; -.
DR Araport; AT4G13410; -.
DR TAIR; locus:2142100; AT4G13410.
DR eggNOG; ENOG502QR7J; Eukaryota.
DR HOGENOM; CLU_012856_2_0_1; -.
DR InParanoid; Q9T0L2; -.
DR OMA; FVERIYM; -.
DR OrthoDB; 559375at2759; -.
DR PhylomeDB; Q9T0L2; -.
DR BioCyc; ARA:AT4G13410-MON; -.
DR PRO; PR:Q9T0L2; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9T0L2; baseline and differential.
DR Genevisible; Q9T0L2; 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; IBA:GO_Central.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
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 3: Inferred from homology;
KW Cell wall biogenesis/degradation; Glycosyltransferase; Golgi apparatus;
KW Membrane; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..537
FT /note="Probable glucomannan 4-beta-mannosyltransferase 15"
FT /id="PRO_0000319334"
FT TRANSMEM 50..70
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 382..402
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 418..438
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 494..514
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 515..535
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 150
FT /evidence="ECO:0000255"
FT ACT_SITE 303
FT /evidence="ECO:0000255"
FT BINDING 209
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 211
FT /ligand="substrate"
FT /evidence="ECO:0000255"
SQ SEQUENCE 537 AA; 62374 MW; 2D43AEB7764D5B3C CRC64;
MFLLLKPLLS LHDLSLNLLS VMFHGETLKA SVDGVGINMS TMWRETRNVF IVPLFKCIVV
MCLIISLLVF VESVYMNLVV LYVKLFNRKP EKVYKWEAMQ EDMELGHQNY PMVLVQIPMY
NEREVFELSI GAACRLTWPS DRLIVQVLDD STDPAIMELV SMECTKWASK DININYERRE
NRNGYKAGAL KHGMRHSYVK QCQYLAIFDA DFQPEPDYLQ RAIPFLIHNP EVALVQARWR
FVNANTCLMT RMQEMSLNYH FMAEQQSGST RHAFFGFNGT AGVWRMVAME EAGGWKDRTT
VEDMDLAVRV GLLGWKFIFV NDLEVKSELP SQFKAFRFQQ HRWSCGPANL IRKMTMEIIH
NKRVKIWKKF YVIYSFFFLR KIVVHFFTYF FYCVILPTSV FLPEVNIPNW STIYVPSVIT
LLSAIATPRS FYLVIFWVLF ENVMAMHRTK GTLIGLFEGG RVNEWVVTEK LGDTLNTKLL
PQNGRLPKRV NLKEMMMGIY ILCCACYDFA FGNAFLYLYL FMQATAFLIS GVGFVGT
