ID A0A6A6KKF6_HEVBR Unreviewed; 1413 AA. AC A0A6A6KKF6; DT 17-JUN-2020, integrated into UniProtKB/TrEMBL. DT 17-JUN-2020, sequence version 1. DT 22-FEB-2023, entry version 10. DE RecName: Full=Cellulose synthase {ECO:0000256|RuleBase:RU361116}; DE EC=2.4.1.12 {ECO:0000256|RuleBase:RU361116}; DE EC=3.2.1.- {ECO:0000256|RuleBase:RU361169}; GN ORFNames=GH714_036018 {ECO:0000313|EMBL:KAF2289412.1}; OS Hevea brasiliensis (Para rubber tree) (Siphonia brasiliensis). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; fabids; Malpighiales; Euphorbiaceae; Crotonoideae; Micrandreae; OC Hevea. OX NCBI_TaxID=3981 {ECO:0000313|EMBL:KAF2289412.1, ECO:0000313|Proteomes:UP000467840}; RN [1] {ECO:0000313|EMBL:KAF2289412.1, ECO:0000313|Proteomes:UP000467840} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. GT1 {ECO:0000313|Proteomes:UP000467840}; RC TISSUE=Leaf {ECO:0000313|EMBL:KAF2289412.1}; RX PubMed=31838037; DOI=10.1016/j.molp.2019.10.017; RA Liu J., Shi C., Shi C.C., Li W., Zhang Q.J., Zhang Y., Li K., Lu H.F., RA Shi C., Zhu S.T., Xiao Z.Y., Nan H., Yue Y., Zhu X.G., Wu Y., Hong X.N., RA Fan G.Y., Tong Y., Zhang D., Mao C.L., Liu Y.L., Hao S.J., Liu W.Q., RA Lv M.Q., Zhang H.B., Liu Y., Hu-Tang G.R., Wang J.P., Wang J.H., Sun Y.H., RA Ni S.B., Chen W.B., Zhang X.C., Jiao Y.N., Eichler E.E., Li G.H., Liu X., RA Gao L.Z.; RT "The Chromosome-Based Rubber Tree Genome Provides New Insights into Spurge RT Genome Evolution and Rubber Biosynthesis."; RL Mol. Plant 13:336-350(2020). 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|RuleBase:RU361116}; 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|RuleBase:RU361116}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU361116}; CC Multi-pass membrane protein {ECO:0000256|RuleBase:RU361116}. Membrane CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004141}. Secreted, cell wall CC {ECO:0000256|ARBA:ARBA00004191}. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 28 family. CC {ECO:0000256|ARBA:ARBA00008834, ECO:0000256|RuleBase:RU361169}. CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. Plant CC cellulose synthase subfamily. {ECO:0000256|RuleBase:RU361116}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|RuleBase:RU361116}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:KAF2289412.1}. 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; JAAGAX010000016; KAF2289412.1; -; Genomic_DNA. DR UniPathway; UPA00695; -. DR Proteomes; UP000467840; Chromosome 8. 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:0004650; F:polygalacturonase activity; IEA:InterPro. 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_plant; 1. DR Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 1. DR InterPro; IPR005150; Cellulose_synth. DR InterPro; IPR027934; CES_Znf_RING. DR InterPro; IPR000743; Glyco_hydro_28. DR InterPro; IPR029044; Nucleotide-diphossugar_trans. DR InterPro; IPR006626; PbH1. DR InterPro; IPR012334; Pectin_lyas_fold. DR InterPro; IPR011050; Pectin_lyase_fold/virulence. DR PANTHER; PTHR13301:SF249; CELLULOSE SYNTHASE; 1. DR PANTHER; PTHR13301; X-BOX TRANSCRIPTION FACTOR-RELATED; 1. DR Pfam; PF03552; Cellulose_synt; 1. DR Pfam; PF00295; Glyco_hydro_28; 1. DR Pfam; PF14569; zf-UDP; 1. DR SMART; SM00710; PbH1; 4. DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1. DR SUPFAM; SSF51126; Pectin lyase-like; 1. DR SUPFAM; SSF57850; RING/U-box; 1. DR PROSITE; PS00502; POLYGALACTURONASE; 1. PE 3: Inferred from homology; KW Cell membrane {ECO:0000256|RuleBase:RU361116}; KW Cell wall {ECO:0000256|ARBA:ARBA00022512}; KW Cell wall biogenesis/degradation {ECO:0000256|RuleBase:RU361116}; KW Cellulose biosynthesis {ECO:0000256|RuleBase:RU361116}; KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361169}; KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676, KW ECO:0000256|RuleBase:RU361116}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361169}; KW Membrane {ECO:0000256|RuleBase:RU361116}; KW Metal-binding {ECO:0000256|RuleBase:RU361116}; KW Reference proteome {ECO:0000313|Proteomes:UP000467840}; KW Secreted {ECO:0000256|ARBA:ARBA00022512}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361116}; KW Transmembrane {ECO:0000256|RuleBase:RU361116}; KW Transmembrane helix {ECO:0000256|RuleBase:RU361116}; KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361116}; KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|RuleBase:RU361116}. FT TRANSMEM 7..26 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361116" FT TRANSMEM 604..622 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361116" FT TRANSMEM 634..651 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361116" FT TRANSMEM 1199..1217 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361116" FT TRANSMEM 1224..1246 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361116" FT TRANSMEM 1258..1277 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361116" FT TRANSMEM 1311..1334 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361116" FT TRANSMEM 1340..1362 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361116" FT TRANSMEM 1374..1394 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361116" FT DOMAIN 396..461 FT /note="Cellulose synthase RING-type zinc finger" FT /evidence="ECO:0000259|Pfam:PF14569" FT REGION 547..570 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 997..1017 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 316 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10052" SQ SEQUENCE 1413 AA; 157761 MW; CBF0EAF82726523E CRC64; MIMALQGLHL YPFFIILLLL SIIIIIPCYD CLQGDTLNHY LEEEEEGGEA FGYDSQAYPS YFSPIEDGQF KDFIKLRSTN VLNLKIFDKV GSISTSVKTV SVDDFRANSN DIDDTEAFQK AWEEACSSKG AVLVVPKNRY LVKPVRFSGP CKSNLTVRIY GTIKASDDRS DYEKDDRRHW LVFDQVQNLL VEGGGTIDGN GKIWWKNSCK VDEDLPCKDA PTALTFHKCQ NLVVDNLKIQ NAQQMHLSFQ SSKDVQVSNL IVTSPKDSPN TDGIHVTHTQ NIQITNSVIA TGDDCISIAS GSQNVQAMDI TCGPGHGISI GSLGSGNSRA YVSGVTIDGA KLSGTSNGVR IKTWQGGSGI ASNIKFQNIE MQNVSNPIII DQYYCDHHKS CKEQTKNVKQ TANRVCQICS GDIGMTVDGE RFVACHVCAF PVCRPCYEYE RKDGNRSCPQ CKTKYKRHKG IQEEKNKIER MLGWDASSGR KDYVAPTNYD KEVSGDLSAA SPERFSMASL ESGSRVNIRV GDPARESGLS GFGNVAWKER IDGWKMKPEK SPAPMSVSNA PSEGRGGGDF DASTDVLMDD SLLNDETRQP LSRKVSIPSS RINPYRMVIV LRLIILCIFL HYRITNPVRD AYSLWLISVI CEIWFAISWI LDQFPKWLPV NRETYLDRLA LRYEKEGEPS QLAAVDIFVS TVDPLKEPPL VTANTVLSIL AVDYPVDKVS CYVSDDGAAM LTFESLSETS EFARKWVPFC KKYSIEPRAP EWYFAQKIDY LKDKVHPSFV KDRRSMKREY EEFKVRINGL VAKAQKVPDE GWVMQDGTPW PGNNTRDHPG MIQVFLGHSG GFDSEGNELP RLVYVSREKR PGFQHHKKAG AMNALVRVSA VLTNGPFLLN LDCDHYINNS RALREAMCFL MDPNLGRSVC YVQFPQRFDG IDKNDRYANR NTVFFDINLR GLDGIQGPVY VGTGCVFNRT ALYGYEPPLK PKHKKPGVLS SCFGGSWKKT SSSGKKNSSK KKSSKHIDPT VPVFSLEDIE EGVEGAGFDD EKSLLMSQMT LEKRFGQSAV FVASTLMENG GVPESATPES LLKEAIHVIS CGYEDKADWG SEIGWIYGSV TEDILTGFKM HARGWRSIYC VPQLAAFKGS APINLSDRLN QVLRWALGSV EILLSRHCPI WYGYGGRLKW LERFAYVNTT IYPVTSIPLL AYCTLPAVCL LTGKFIIPQI SNIASIWFIS LFLSIFATGI LEMRWSGVGI DEWWRNEQFW VIGGVSAHLF AVFQGLLKVL AGIDTNFTVT SKASDEDGDF AELYLFKWTT LLIPPTTLLI INLVGVVAGI SYAINSGYQS WGPLFGKLFF AFWVIIHLYP FLKGLMGRQN RTPTIVVVWS ILLASIFSLL WVRIDPFTTQ VTGPDVEQCG INC //