CSLA2_ARATH
ID CSLA2_ARATH Reviewed; 534 AA.
AC Q9FNI7;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Glucomannan 4-beta-mannosyltransferase 2 {ECO:0000305};
DE EC=2.4.1.32 {ECO:0000269|PubMed:15647349};
DE AltName: Full=Cellulose synthase-like protein A2 {ECO:0000303|PubMed:11027699};
DE Short=AtCslA2 {ECO:0000303|PubMed:11027699};
DE AltName: Full=Glucomannan synthase {ECO:0000305};
DE AltName: Full=Mannan synthase 2 {ECO:0000305};
GN Name=CSLA2 {ECO:0000303|PubMed:11027699}; OrderedLocusNames=At5g22740;
GN ORFNames=MDJ22.16;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9405937; DOI=10.1093/dnares/4.4.291;
RA Kotani H., Nakamura Y., Sato S., Kaneko T., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. II. Sequence
RT features of the regions of 1,044,062 bp covered by thirteen physically
RT assigned P1 clones.";
RL DNA Res. 4:291-300(1997).
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 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 [5]
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: 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. {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 -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. Plant
CC cellulose synthase-like A subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB006699; BAB11680.1; -; Genomic_DNA.
DR EMBL; CP002688; AED93069.1; -; Genomic_DNA.
DR EMBL; AY058158; AAL25573.1; -; mRNA.
DR EMBL; AY059852; AAL24334.1; -; mRNA.
DR EMBL; AY093293; AAM13292.1; -; mRNA.
DR RefSeq; NP_197666.1; NM_122180.3.
DR AlphaFoldDB; Q9FNI7; -.
DR STRING; 3702.AT5G22740.1; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR iPTMnet; Q9FNI7; -.
DR PaxDb; Q9FNI7; -.
DR PRIDE; Q9FNI7; -.
DR ProteomicsDB; 220368; -.
DR EnsemblPlants; AT5G22740.1; AT5G22740.1; AT5G22740.
DR GeneID; 832337; -.
DR Gramene; AT5G22740.1; AT5G22740.1; AT5G22740.
DR KEGG; ath:AT5G22740; -.
DR Araport; AT5G22740; -.
DR TAIR; locus:2162494; AT5G22740.
DR eggNOG; ENOG502QR7J; Eukaryota.
DR HOGENOM; CLU_012856_2_0_1; -.
DR InParanoid; Q9FNI7; -.
DR OMA; DKRYKFE; -.
DR OrthoDB; 559375at2759; -.
DR PhylomeDB; Q9FNI7; -.
DR BioCyc; ARA:AT5G22740-MON; -.
DR PRO; PR:Q9FNI7; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FNI7; baseline and differential.
DR Genevisible; Q9FNI7; AT.
DR GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
DR GO; GO:0005797; C:Golgi medial cisterna; HDA:TAIR.
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; IDA:TAIR.
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:0010192; P:mucilage biosynthetic process; IMP:TAIR.
DR GO; GO:0048359; P:mucilage metabolic process involved in seed coat development; 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..534
FT /note="Glucomannan 4-beta-mannosyltransferase 2"
FT /id="PRO_0000319327"
FT TRANSMEM 36..56
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 509..529
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"
SQ SEQUENCE 534 AA; 61558 MW; EFC37DE018698315 CRC64;
MDGVSPKFVL PETFDGVRME ITGQLGMIWE LVKAPVIVPL LQLAVYICLL MSVMLLCERV
YMGIVIVLVK LFWKKPDKRY KFEPIHDDEE LGSSNFPVVL VQIPMFNERE VYKLSIGAAC
GLSWPSDRLV IQVLDDSTDP TVKQMVEVEC QRWASKGINI RYQIRENRVG YKAGALKEGL
KRSYVKHCEY VVIFDADFQP EPDFLRRSIP FLMHNPNIAL VQARWRFVNS DECLLTRMQE
MSLDYHFTVE QEVGSSTHAF FGFNGTAGIW RIAAINEAGG WKDRTTVEDM DLAVRASLRG
WKFLYLGDLQ VKSELPSTFR AFRFQQHRWS CGPANLFRKM VMEIVRNKKV RFWKKVYVIY
SFFFVRKIIA HWVTFCFYCV VLPLTILVPE VKVPIWGSVY IPSIITILNS VGTPRSIHLL
FYWILFENVM SLHRTKATLI GLFEAGRANE WVVTAKLGSG QSAKGNTKGI KRFPRIFKLP
DRLNTLELGF AAFLFVCGCY DFVHGKNNYF IYLFLQTMSF FISGLGWIGT YVPS
