CSLA3_ARATH
ID CSLA3_ARATH Reviewed; 556 AA.
AC Q9LQC9; Q3ED64; Q9ZUE5;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Probable glucomannan 4-beta-mannosyltransferase 3 {ECO:0000305};
DE EC=2.4.1.32 {ECO:0000250|UniProtKB:Q9LZR3};
DE AltName: Full=Cellulose synthase-like protein A3 {ECO:0000303|PubMed:11027699};
DE Short=AtCslA3 {ECO:0000303|PubMed:11027699};
DE AltName: Full=Glucomannan synthase {ECO:0000305};
DE AltName: Full=Mannan synthase 3 {ECO:0000305};
GN Name=CSLA3 {ECO:0000303|PubMed:11027699}; OrderedLocusNames=At1g23480;
GN ORFNames=F28C11.11, F5O8.4;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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] (ISOFORM 1).
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).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9LQC9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9LQC9-2; Sequence=VSP_031472;
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. Plant
CC cellulose synthase-like A subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC98005.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC005990; AAC98005.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC007945; AAF79586.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30391.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30392.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30393.1; -; Genomic_DNA.
DR EMBL; AY099769; AAM20620.1; -; mRNA.
DR EMBL; BT000203; AAN15522.1; -; mRNA.
DR PIR; D86368; D86368.
DR RefSeq; NP_001031084.1; NM_001036007.2. [Q9LQC9-2]
DR RefSeq; NP_173762.4; NM_102197.5. [Q9LQC9-1]
DR RefSeq; NP_850952.1; NM_180621.3. [Q9LQC9-1]
DR AlphaFoldDB; Q9LQC9; -.
DR STRING; 3702.AT1G23480.2; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR PaxDb; Q9LQC9; -.
DR PRIDE; Q9LQC9; -.
DR ProteomicsDB; 224423; -. [Q9LQC9-1]
DR EnsemblPlants; AT1G23480.1; AT1G23480.1; AT1G23480. [Q9LQC9-1]
DR EnsemblPlants; AT1G23480.2; AT1G23480.2; AT1G23480. [Q9LQC9-1]
DR EnsemblPlants; AT1G23480.3; AT1G23480.3; AT1G23480. [Q9LQC9-2]
DR GeneID; 838956; -.
DR Gramene; AT1G23480.1; AT1G23480.1; AT1G23480. [Q9LQC9-1]
DR Gramene; AT1G23480.2; AT1G23480.2; AT1G23480. [Q9LQC9-1]
DR Gramene; AT1G23480.3; AT1G23480.3; AT1G23480. [Q9LQC9-2]
DR KEGG; ath:AT1G23480; -.
DR Araport; AT1G23480; -.
DR TAIR; locus:2028862; AT1G23480.
DR eggNOG; ENOG502QR7J; Eukaryota.
DR InParanoid; Q9LQC9; -.
DR OMA; QTRIFVF; -.
DR PhylomeDB; Q9LQC9; -.
DR BioCyc; ARA:AT1G23480-MON; -.
DR PRO; PR:Q9LQC9; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LQC9; baseline and differential.
DR Genevisible; Q9LQC9; 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 Alternative splicing; Cell wall biogenesis/degradation;
KW Glycosyltransferase; Golgi apparatus; Membrane; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..556
FT /note="Probable glucomannan 4-beta-mannosyltransferase 3"
FT /id="PRO_0000319328"
FT TRANSMEM 56..76
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 391..411
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 428..448
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 509..529
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 530..550
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 159
FT /evidence="ECO:0000255"
FT ACT_SITE 312
FT /evidence="ECO:0000255"
FT BINDING 218
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 220
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..72
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_031472"
SQ SEQUENCE 556 AA; 64402 MW; A427612B7E849E1F CRC64;
MSPFLKFFLF LYDYLSPSSF FLVQRNTLGA SLDTTDGVVR SGIIGEIIYI WKQTRIFVFI
PILKCLVTIC LVMSLLLFIE RVYMSIVVVF VKLLRRTPEK VHKWEPINDD DLELANTNYP
MVLIQIPMYN EKEVCQLSIG AACRLSWPLD RMIVQVLDDS TDPASKELVN AECDKWARKG
INIMSEIRDN RIGYKAGALK AGMMHNYVKQ CEFVAIFDAD FQPDPDFLER TIPFLIHNHE
ISLVQCRWKF VNANECLMTR MQEMSLNYHF VAEQESGSSI HAFFGFNGTA GVWRIAALNE
AGGWKDRTTV EDMDLAVRAC LHGWKFVYVH DVEVKNELPS TFKAYRFQQH RWSCGPANLW
RKMTMEILQN KKVSAWKKLY LIYNFFFIRK IVVHIFTFVF YCLILPTTVL FPELQVPKWA
TVYFPTTITI LNAIATPRSL HLLVFWILFE NVMSMHRTKA TFIGLLEAGR VNEWVVTEKL
GDTLKSKLIG KATTKLYTRF GQRLNWRELV VGLYIFFCGC YDFAYGGSYF YVYLFLQSCA
FFVAGVGYIG TFVPTV