ID W8QNX9_ARATH Unreviewed; 1058 AA.
AC W8QNX9;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=Cellulose synthase {ECO:0000256|RuleBase:RU361116};
DE EC=2.4.1.12 {ECO:0000256|RuleBase:RU361116};
DE Flags: Fragment;
GN Name=CESA10 {ECO:0000313|EMBL:AEC07714.2, ECO:0000313|TAIR:AT2G25540};
GN Synonyms=cellulose synthase 10 {ECO:0000313|EMBL:AEC07714.2};
GN OrderedLocusNames=At2g25540 {ECO:0000313|EMBL:AEC07714.2};
GN ORFNames=AT2G25540 {ECO:0000313|EMBL:AHL38838.1}, F13B15.20
GN {ECO:0000313|EMBL:AEC07714.2}, F13B15_20
GN {ECO:0000313|EMBL:AEC07714.2};
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 {ECO:0000313|EMBL:AHL38838.1};
RN [1] {ECO:0000313|EMBL:AEC07714.2, ECO:0000313|Proteomes:UP000006548}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548};
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S., Shea T.P., Benito M.I., Town C.D.,
RA Fujii C.Y., Mason T., Bowman C.L., Barnstead M., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee 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 [2] {ECO:0000313|EMBL:AEC07714.2}
RP NUCLEOTIDE SEQUENCE.
RG TAIR;
RA Swarbreck D., Lamesch P., Wilks C., Huala E.;
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:AHL38838.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=24905498;
RA Lao J., Oikawa A., Bromley J.R., McInerney P., Suttangkakul A.,
RA Smith-Moritz A.M., Plahar H., Chiu T.Y., Gonzalez Fernandez-Nino S.M.,
RA Ebert B., Yang F., Christiansen K.M., Hansen S.F., Stonebloom S.,
RA Adams P.D., Ronald P.C., Hillson N.J., Hadi M.Z., Vega-Sanchez M.E.,
RA Loque D., Scheller H.V., Heazlewood J.L.;
RT "The plant glycosyltransferase clone collection for functional genomics.";
RL Plant J. 79:517-529(2014).
RN [4] {ECO:0000313|EMBL:AEC07714.2}
RP NUCLEOTIDE SEQUENCE.
RA Krishnakumar V., Cheng C.-Y., Chan A.P., Schobel S., Kim M., Ferlanti E.S.,
RA Belyaeva I., Rosen B.D., Micklem G., Miller J.R., Vaughn M., Town C.D.;
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|Proteomes:UP000006548}
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548};
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).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(1->4)-beta-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->4)-
CC beta-D-glucosyl](n+1) + H(+) + UDP; Xref=Rhea:RHEA:19929, Rhea:RHEA-
CC COMP:10033, Rhea:RHEA-COMP:10034, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:18246, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.12;
CC Evidence={ECO:0000256|ARBA:ARBA00000122,
CC ECO:0000256|RuleBase:RU361116};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU361116};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000256|RuleBase:RU361116};
CC -!- PATHWAY: Glycan metabolism; plant cellulose biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004768, ECO:0000256|RuleBase:RU361116}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651,
CC ECO:0000256|RuleBase:RU361116}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU361116}.
CC Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. Plant
CC cellulose synthase subfamily. {ECO:0000256|ARBA:ARBA00007548,
CC ECO:0000256|RuleBase:RU361116}.
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DR EMBL; CP002685; AEC07714.2; -; Genomic_DNA.
DR EMBL; KJ138898; AHL38838.1; -; mRNA.
DR RefSeq; NP_001318288.1; NM_001336002.1.
DR AlphaFoldDB; W8QNX9; -.
DR SMR; W8QNX9; -.
DR ProteomicsDB; 185666; -.
DR EnsemblPlants; AT2G25540.1; AT2G25540.1; AT2G25540.
DR GeneID; 817092; -.
DR Gramene; AT2G25540.1; AT2G25540.1; AT2G25540.
DR KEGG; ath:AT2G25540; -.
DR TAIR; AT2G25540; CESA10.
DR OMA; GPQWQLQ; -.
DR OrthoDB; 660034at2759; -.
DR UniPathway; UPA00695; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; W8QNX9; baseline and differential.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016760; F:cellulose synthase (UDP-forming) activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0030244; P:cellulose biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd16617; mRING-HC-C4C4_CesA; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR005150; Cellulose_synth.
DR InterPro; IPR027934; CES_Znf_RING.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR13301:SF33; CELLULOSE SYNTHASE A CATALYTIC SUBUNIT 1 [UDP-FORMING]-RELATED; 1.
DR PANTHER; PTHR13301; X-BOX TRANSCRIPTION FACTOR-RELATED; 1.
DR Pfam; PF03552; Cellulose_synt; 1.
DR Pfam; PF14569; zf-UDP; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW ECO:0000256|RuleBase:RU361116};
KW Cell wall biogenesis/degradation {ECO:0000256|RuleBase:RU361116};
KW Cellulose biosynthesis {ECO:0000256|ARBA:ARBA00022916,
KW ECO:0000256|RuleBase:RU361116};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000256|RuleBase:RU361116}; Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU361116};
KW Metal-binding {ECO:0000256|RuleBase:RU361116};
KW Proteomics identification {ECO:0007829|PeptideAtlas:W8QNX9,
KW ECO:0007829|ProteomicsDB:W8QNX9};
KW Reference proteome {ECO:0000313|Proteomes:UP000006548};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361116};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU361116};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU361116};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361116};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT TRANSMEM 252..269
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361116"
FT TRANSMEM 281..300
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361116"
FT TRANSMEM 837..858
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361116"
FT TRANSMEM 870..886
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361116"
FT TRANSMEM 906..924
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361116"
FT TRANSMEM 958..981
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361116"
FT TRANSMEM 987..1009
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361116"
FT TRANSMEM 1021..1041
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361116"
FT DOMAIN 33..79
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT NON_TER 1058
FT /evidence="ECO:0000313|EMBL:AHL38838.1"
SQ SEQUENCE 1058 AA; 119802 MW; F9C7AA89401107C9 CRC64;
MVAGSYRRYE FVRNRDDSDD GLKPLKDLNG QICQICGDDV GLTKTGNVFV ACNECGFPLC
QSCYEYERKD GSQCCPQCKA RFRRHNGSPR VEVDEKEDDV NDIENEFDYT QGNNKARLPH
RAEEFSSSSR HEESLPVSLL THGHPVSGEI PTPDRNATLS PCIDPQLPVP VRILDPSKDL
NSYGLVNVDW KKRIQGWKLK QDKNMIHMTG KYHEGKGGEF EGTGSNGDEL QMVDDARLPM
SRVVHFPSAR MTPYRIVIVL RLIILGVFLH YRTTHPVKDA YALWLTSVIC EIWFAFSWLL
DQFPKWYPIN RETFLDRLAL RYDRDGEPSQ LAPVDVFVST VDPMKEPPLV TANTVLSILA
VDYPVDKVAC YVSDDGSAML TFEALSETAE FSKKWVPFCK KFNIEPRAPE FYFSQKIDYL
KDKIQPSFVK ERRAMKREYE EFKVRINILV AKAQKIPEDG WTMEDGTSWP GNNPRDHPGM
IQVFLGHSGG LDTDGNELPR LIYVSREKRP GFQHHKKAGA MNALIRVSAV LTNGAYLLNV
DCDHYFNNSK AIKEAMCFMM DPAIGKKCCY VQFPQRFDGI DLHDRYANRN TVFFDINLKG
LDGIQGPVYV GTGCCFNRQA LYGYDPVLTE EDLEPNIIVK SCFGSRKKGK SRKIPNYEDN
RSIKRSDSNV PLFNMEDIDE DVEGYEDEMS LLVSQKRLEK RFGQSPVFIA ATFMEQGGLP
STTNPLTLLK EAIHVISCGY EAKTDWGKEI GWIYGSVTED ILTGFKMHAR GWISIYCVPS
RPAFKGSAPI NLSDRLNQVL RWALGSIEIL LSRHCPIWYG YNGRLKLLER IAYINTIVYP
ITSIPLLAYC MLPAFCLITN TFIIPEISNL ASLCFMLLFA SIYASAILEL KWSDVALEDW
WRNEQFWVIG GTSAHLFAVF QGLLKVFAGI DTNFTVTSKA SDEDGDFAEL YVFKWTSLLI
PPTTILLVNL VGIVAGVSYA INSGYQSWGP LMGKLLFAFW VVAHLYPFLK GLLGRQNRTP
TIVIVWSALL ASIFSLLWVR INPFVSTTGV MSNSFMGE
//
