CSLA7_ARATH
ID CSLA7_ARATH Reviewed; 556 AA.
AC Q9ZQN8; Q8LFW7; Q93YX2;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Glucomannan 4-beta-mannosyltransferase 7 {ECO:0000305};
DE EC=2.4.1.32 {ECO:0000269|PubMed:15647349};
DE AltName: Full=Cellulose synthase-like protein A7 {ECO:0000303|PubMed:11027699};
DE Short=AtCslA7 {ECO:0000303|PubMed:11027699};
DE AltName: Full=Glucomannan synthase {ECO:0000305};
DE AltName: Full=Mannan synthase 7 {ECO:0000305};
GN Name=CSLA7 {ECO:0000303|PubMed:11027699}; OrderedLocusNames=At2g35650;
GN ORFNames=T20F21.16;
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 [MRNA], FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=cv. Columbia; TISSUE=Callus;
RX PubMed=12586879; DOI=10.1104/pp.014555;
RA Goubet F., Misrahi A., Park S.K., Zhang Z., Twell D., Dupree P.;
RT "AtCSLA7, a cellulose synthase-like putative glycosyltransferase, is
RT important for pollen tube growth and embryogenesis in Arabidopsis.";
RL Plant Physiol. 131:547-557(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(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;
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].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) 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, 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).
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 (PubMed:15647349). Required for
CC synthesis of a cell wall polysaccharide essential for pollen tube
CC growth, for cell wall structure, or for signaling during plant embryo
CC development (PubMed:12586879). {ECO:0000269|PubMed:12586879,
CC ECO:0000269|PubMed:15647349}.
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 -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Multi-
CC pass membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:12586879}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethality when homozygous due to
CC defective pollen tube growth and disruption of embryonic development.
CC {ECO:0000269|PubMed:12586879}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. Plant
CC cellulose synthase-like A subfamily. {ECO:0000305}.
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DR EMBL; AJ488284; CAD32548.1; -; mRNA.
DR EMBL; AC006068; AAD15455.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC09136.1; -; Genomic_DNA.
DR EMBL; AY059724; AAL24081.1; -; mRNA.
DR EMBL; AY133807; AAM91741.1; -; mRNA.
DR EMBL; AY084607; AAM61171.1; -; mRNA.
DR PIR; C84771; C84771.
DR RefSeq; NP_565813.1; NM_129120.4.
DR AlphaFoldDB; Q9ZQN8; -.
DR SMR; Q9ZQN8; -.
DR STRING; 3702.AT2G35650.1; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR PaxDb; Q9ZQN8; -.
DR PRIDE; Q9ZQN8; -.
DR ProteomicsDB; 222658; -.
DR EnsemblPlants; AT2G35650.1; AT2G35650.1; AT2G35650.
DR GeneID; 818134; -.
DR Gramene; AT2G35650.1; AT2G35650.1; AT2G35650.
DR KEGG; ath:AT2G35650; -.
DR Araport; AT2G35650; -.
DR TAIR; locus:2058729; AT2G35650.
DR eggNOG; ENOG502QR7J; Eukaryota.
DR HOGENOM; CLU_012856_2_0_1; -.
DR InParanoid; Q9ZQN8; -.
DR OMA; KIYAVSH; -.
DR OrthoDB; 559375at2759; -.
DR PhylomeDB; Q9ZQN8; -.
DR BioCyc; ARA:AT2G35650-MON; -.
DR PRO; PR:Q9ZQN8; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZQN8; baseline and differential.
DR Genevisible; Q9ZQN8; 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:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
DR GO; GO:0009860; P:pollen tube growth; IMP:TAIR.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
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..556
FT /note="Glucomannan 4-beta-mannosyltransferase 7"
FT /id="PRO_0000319329"
FT TRANSMEM 58..78
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 390..410
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 426..448
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 502..522
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 526..546
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 158
FT /evidence="ECO:0000255"
FT ACT_SITE 311
FT /evidence="ECO:0000255"
FT BINDING 217
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 219
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT CONFLICT 68
FT /note="L -> V (in Ref. 5; AAM61171)"
FT /evidence="ECO:0000305"
FT CONFLICT 481
FT /note="D -> H (in Ref. 5; AAM61171)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 556 AA; 63795 MW; 57E930717B2C9819 CRC64;
MSPLPIFHRL PHATFSSFLL SLSQAGSSKT SVAFLNAFKS EDIIARIGLW WQLIRAVVVV
PVFKFLVLLC LVMSVMFFVE VMYMGIVVLY VKLFKRKPEK FYKWEAMEDD VECGSASYPM
VLVQIPMYNE KEVCEQSIAA ACKISWPSNR IIIQVLDDST DPASKELVKK ECDRWSKEGV
NITFEIRDNR NGYKAGALRE GMRHSYVKQC DYVAIFDADF QPDPDFLHRT VPFLIHNPKL
ALVQGRWEFV NAGQCMMTRL QEMSLSYHFT IEQQVGSSTF AFFGFNGTAG VWRISALNES
GGWNDQTTVE DMDLAVRATL RGWKFLYIDD LKVKSELPCS FKALRSQQHR WTCGPANLLR
KMAGQIIRSE NVSLWKKWYM LYSFFFMRKI VAHILTFCFY CVILPATVLF PEVTVPKWAA
FYLPSLITLL IAIGRLRSIH LLAFWVLFEN AMSLLRAKAL VMGLFETGRV QEWVVTEKLG
DTLKTKLIPQ VPNVRFRERV HLLELLVGAY LLFCGIYDIV YGKNTLYVYL LFQSVAFFVV
GFGFVGKYVP ASSYLA
