CSLAE_ARATH
ID CSLAE_ARATH Reviewed; 535 AA.
AC Q84W06; Q9LY45;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 2.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Probable glucomannan 4-beta-mannosyltransferase 14 {ECO:0000305};
DE EC=2.4.1.32 {ECO:0000250|UniProtKB:Q9LZR3};
DE AltName: Full=Cellulose synthase-like protein A14 {ECO:0000303|PubMed:11027699};
DE Short=AtCslA14 {ECO:0000303|PubMed:11027699};
DE AltName: Full=Glucomannan synthase {ECO:0000305};
DE AltName: Full=Mannan synthase 14 {ECO:0000305};
GN Name=CSLA14 {ECO:0000303|PubMed:11027699}; OrderedLocusNames=At3g56000;
GN ORFNames=F27K19.180;
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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].
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 [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 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=CAB87854.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL163832; CAB87854.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE79465.1; -; Genomic_DNA.
DR EMBL; BT004569; AAO42815.1; -; mRNA.
DR EMBL; AK227328; BAE99342.1; -; mRNA.
DR PIR; T49212; T49212.
DR RefSeq; NP_191159.2; NM_115458.5.
DR AlphaFoldDB; Q84W06; -.
DR STRING; 3702.AT3G56000.1; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR PaxDb; Q84W06; -.
DR PRIDE; Q84W06; -.
DR ProteomicsDB; 220500; -.
DR EnsemblPlants; AT3G56000.1; AT3G56000.1; AT3G56000.
DR GeneID; 824766; -.
DR Gramene; AT3G56000.1; AT3G56000.1; AT3G56000.
DR KEGG; ath:AT3G56000; -.
DR Araport; AT3G56000; -.
DR TAIR; locus:2082083; AT3G56000.
DR eggNOG; ENOG502QR7J; Eukaryota.
DR HOGENOM; CLU_012856_2_0_1; -.
DR InParanoid; Q84W06; -.
DR OMA; MAMEIIQ; -.
DR OrthoDB; 559375at2759; -.
DR BioCyc; ARA:AT3G56000-MON; -.
DR PRO; PR:Q84W06; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q84W06; baseline and differential.
DR Genevisible; Q84W06; 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..535
FT /note="Probable glucomannan 4-beta-mannosyltransferase 14"
FT /id="PRO_0000319333"
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 366..386
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 403..423
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 482..502
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 503..523
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 131
FT /evidence="ECO:0000255"
FT ACT_SITE 287
FT /evidence="ECO:0000255"
FT BINDING 193
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 195
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT CONFLICT 110
FT /note="S -> P (in Ref. 3; AAO42815 and 4; BAE99342)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 535 AA; 61483 MW; 1A83F2FCF8C24766 CRC64;
MATLSDGLFD DMSVLGVIGY VLEQTRFIFL VPILKRLVNL CQVVSVLLFV DAAYMAIVVA
IVKLLGRTPQ KVLKWESFKS DDIELAPSSN HPMVLIQIPI FNEKEVCQLS IGAACKLSWP
LDRMIIQVLD DSTEEESQKL VRLECKKWES EGITIKSEVR GGFREGFKAG ALTAGMKHSY
VDEYKCEFVV IFDADFQPEP DFLERTVPFL VHNPEIALVQ AGWKYGNADE CCMTRIQEMS
LNYHFAVEQK SGSSILGFFG FNGTAGVWRI KALNEAEGWK DRTIVEDMDL AVRAYLRGSK
FVYVDDVKVK NELPSSFQAY RFQQHRWSCG PANLFKKIAM EIIKNQNVSL WKKVYLIYNF
FFLRKIVVHI FTFVFYCVIL PATVIFPEIE VPKWTTIYIP ATITILNAIA TPKSFYLILY
WILFENVMAM HRSIGTLIGL LETSRVKEWI VTQKLGESNN LRENLIFPDH YSFPERLRWR
EIMVGMYLFI CGYYDFVFGR TYLYVYLFLQ SIAFFVVGVG YVGMPVPSTP VQTSE
