CSLAA_ARATH
ID CSLAA_ARATH Reviewed; 552 AA.
AC Q9LR87; Q8GWQ3;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Probable glucomannan 4-beta-mannosyltransferase 10 {ECO:0000305};
DE EC=2.4.1.32 {ECO:0000250|UniProtKB:Q9LZR3};
DE AltName: Full=Cellulose synthase-like protein A10 {ECO:0000303|PubMed:11027699};
DE Short=AtCslA10 {ECO:0000303|PubMed:11027699};
DE AltName: Full=Glucomannan synthase {ECO:0000305};
DE AltName: Full=Mannan synthase 10 {ECO:0000305};
GN Name=CSLA10 {ECO:0000303|PubMed:11027699}; OrderedLocusNames=At1g24070;
GN ORFNames=T23E23.23;
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] OF 152-552.
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
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=AAF87149.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAC43295.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC002423; AAF87149.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE30475.1; -; Genomic_DNA.
DR EMBL; AK118701; BAC43295.1; ALT_INIT; mRNA.
DR RefSeq; NP_173818.1; NM_102254.3.
DR AlphaFoldDB; Q9LR87; -.
DR STRING; 3702.AT1G24070.1; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR PaxDb; Q9LR87; -.
DR PRIDE; Q9LR87; -.
DR ProteomicsDB; 220355; -.
DR EnsemblPlants; AT1G24070.1; AT1G24070.1; AT1G24070.
DR GeneID; 839019; -.
DR Gramene; AT1G24070.1; AT1G24070.1; AT1G24070.
DR KEGG; ath:AT1G24070; -.
DR Araport; AT1G24070; -.
DR TAIR; locus:2199917; AT1G24070.
DR eggNOG; ENOG502QR7J; Eukaryota.
DR HOGENOM; CLU_012856_2_0_1; -.
DR InParanoid; Q9LR87; -.
DR OMA; PAWSTFY; -.
DR OrthoDB; 559375at2759; -.
DR PhylomeDB; Q9LR87; -.
DR BioCyc; ARA:AT1G24070-MON; -.
DR PRO; PR:Q9LR87; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LR87; baseline and differential.
DR Genevisible; Q9LR87; 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; IPR029044; Nucleotide-diphossugar_trans.
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..552
FT /note="Probable glucomannan 4-beta-mannosyltransferase 10"
FT /id="PRO_0000319331"
FT TRANSMEM 62..82
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 393..413
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 430..450
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 161
FT /evidence="ECO:0000255"
FT ACT_SITE 314
FT /evidence="ECO:0000255"
FT BINDING 220
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 222
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT CONFLICT 468
FT /note="L -> F (in Ref. 3; BAC43295)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 552 AA; 64155 MW; 19041E9FD411992F CRC64;
MTTFLKSLIF LQDSCLAFLS LMFHRGSSED AAEALKKLET SINGARISFD TTWTREFRSL
FIVPLFKCLV AFCLIISLLV FIEGIYMNLV VLYVKVFERK PEKVYRWEAM QEDIELGHET
YPMVLVQIPM YNEKEVLQLS IGAACRLIWP LDRLIVQVLD DSTDQTIKEL VNTECAKWES
KGVNIKCERR DNRNGYKAGA LKEGMKHNYV KLCNYVVIFD ADFQPEPDYL QHSVPFLVHN
PEVALVQARW RFMNANKCLM TRMQEMSLNY HFMAEQESGS TRHAFFSFNG TAGVWRMAAM
EEAGGWHDRT TVEDMDLAVR AGLLGWKFVF LNDLTVKSEL PSKFKAFRFQ QHRWSCGPAN
LFRKMIMEII RNKRVTIWKK LYLVYSFFFL RKIIVHCFTF IFYCVILPTS VFFPEVNIPA
WSTFYIPSMI TLCIVIATPR SFYLVIFWIL FENVMSMHRT KGTFIGILER QRVNEWVVTE
KLGDALKTKL LPRIGKPSNM FLERVNSKEI MVGIYILCCA CYGLFFGNTL LYLYLFMQAV
AFLISGVGFV GT
