CSLAB_ARATH
ID CSLAB_ARATH Reviewed; 443 AA.
AC Q9LF09;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Probable glucomannan 4-beta-mannosyltransferase 11 {ECO:0000305};
DE EC=2.4.1.32 {ECO:0000250|UniProtKB:Q9LZR3};
DE AltName: Full=Cellulose synthase-like protein A11 {ECO:0000303|PubMed:11027699};
DE Short=AtCslA11 {ECO:0000303|PubMed:11027699};
DE AltName: Full=Glucomannan synthase {ECO:0000305};
DE AltName: Full=Mannan synthase 11 {ECO:0000305};
GN Name=CSLA11 {ECO:0000303|PubMed:11027699}; OrderedLocusNames=At5g16190;
GN ORFNames=T21H19.110;
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=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 [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] OF 2-413.
RC STRAIN=cv. Columbia;
RG Center for eukaryotic structural genomics (CESG);
RL Submitted (SEP-2004) 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).
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=CAC01860.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL391148; CAC01860.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED92259.1; -; Genomic_DNA.
DR EMBL; BT011957; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; T51489; T51489.
DR RefSeq; NP_197123.3; NM_121624.4.
DR AlphaFoldDB; Q9LF09; -.
DR STRING; 3702.AT5G16190.1; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR PaxDb; Q9LF09; -.
DR PRIDE; Q9LF09; -.
DR ProteomicsDB; 220356; -.
DR EnsemblPlants; AT5G16190.1; AT5G16190.1; AT5G16190.
DR GeneID; 831477; -.
DR Gramene; AT5G16190.1; AT5G16190.1; AT5G16190.
DR KEGG; ath:AT5G16190; -.
DR Araport; AT5G16190; -.
DR TAIR; locus:2181382; AT5G16190.
DR eggNOG; ENOG502QR7J; Eukaryota.
DR HOGENOM; CLU_012856_2_0_1; -.
DR InParanoid; Q9LF09; -.
DR PhylomeDB; Q9LF09; -.
DR PRO; PR:Q9LF09; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LF09; baseline and differential.
DR Genevisible; Q9LF09; 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 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..443
FT /note="Probable glucomannan 4-beta-mannosyltransferase 11"
FT /id="PRO_0000319332"
FT TRANSMEM 284..304
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 321..341
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 400..420
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 421..441
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 52
FT /evidence="ECO:0000255"
FT ACT_SITE 205
FT /evidence="ECO:0000255"
FT BINDING 111
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 113
FT /ligand="substrate"
FT /evidence="ECO:0000255"
SQ SEQUENCE 443 AA; 51469 MW; 803BCD4723731F18 CRC64;
MQEDLELGNQ NFPMVLVQIP MYNEREVFKL SIGAACRLIW PLDRLIVQVL DDSTDPTIME
MVSTECGKWA TKGINIKCER RDNRNGYKAG ALKQGMRHSY VKTCTYIAIF DADFQPEPDY
LERTVPFLIH NPELALVQAR WKFVNAKKCL MTRMQEMSLN YHFTAEQESG STRHAFFGFN
GTAGVWRLAA MEEAGGWKDR TTVEDMDLAV RVGLHGWKFV FVNDVSVKSE LPSQFKAFRF
QQHRWSCGPA NLFRKMTMEI IRNKRVTIWK KLYVIYSFFF VRKIIVHFFT FFFYCFILPT
SVFFPEVNIP TWSTVYFPFM ITLFNAIATP RSFYLVIFWV LFENVMAMHR TKGTFIGLLE
GGRVNEWVVT EKLGDALETK LLPQVRKPRN GFLERINSKE MMVGIYILCC ASYNLVFGKT
VLYIYLYMQA LAFIIAGIGF IGT
