ID A0A1J7FVN2_LUPAN Unreviewed; 1047 AA. AC A0A1J7FVN2; DT 15-FEB-2017, integrated into UniProtKB/TrEMBL. DT 15-FEB-2017, sequence version 1. DT 11-DEC-2019, entry version 21. DE RecName: Full=Cellulose synthase {ECO:0000256|RuleBase:RU361116}; DE EC=2.4.1.12 {ECO:0000256|RuleBase:RU361116}; GN ORFNames=TanjilG_15037 {ECO:0000313|EMBL:OIV92046.1}; OS Lupinus angustifolius (Narrow-leaved blue lupine). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade; OC genistoids sensu lato; core genistoids; Genisteae; Lupinus. OX NCBI_TaxID=3871 {ECO:0000313|EMBL:OIV92046.1, ECO:0000313|Proteomes:UP000188354}; RN [1] {ECO:0000313|EMBL:OIV92046.1, ECO:0000313|Proteomes:UP000188354} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Tanjil {ECO:0000313|Proteomes:UP000188354}; RC TISSUE=Whole plant {ECO:0000313|EMBL:OIV92046.1}; RX PubMed=27557478; DOI=10.1111/pbi.12615; RA Hane J.K., Ming Y., Kamphuis L.G., Nelson M.N., Garg G., Atkins C.A., RA Bayer P.E., Bravo A., Bringans S., Cannon S., Edwards D., Foley R., RA Gao L.L., Harrison M.J., Huang W., Hurgobin B., Li S., Liu C.W., RA McGrath A., Morahan G., Murray J., Weller J., Jian J., Singh K.B.; RT "A comprehensive draft genome sequence for lupin (Lupinus angustifolius), RT an emerging health food: insights into plant-microbe interactions and RT legume evolution."; RL Plant Biotechnol. J. 15:318-330(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|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}. CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. Plant CC cellulose synthase subfamily. {ECO:0000256|RuleBase:RU361116}. 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; KV862133; OIV92046.1; -; Genomic_DNA. DR RefSeq; XP_019425619.1; XM_019570074.1. DR EnsemblPlants; OIV92046; OIV92046; TanjilG_15037. DR GeneID; 109334350; -. DR Gramene; OIV92046; OIV92046; TanjilG_15037. DR KEGG; lang:109334350; -. DR KO; K10999; -. DR OMA; WIISVIC; -. DR OrthoDB; 679241at2759; -. DR UniPathway; UPA00695; -. DR Proteomes; UP000188354; Chromosome LG19. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. 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 Gene3D; 3.30.40.10; -; 1. DR Gene3D; 3.90.550.10; -; 1. DR InterPro; IPR005150; Cellulose_synth. DR InterPro; IPR027934; CES_Znf_RING. DR InterPro; IPR029044; Nucleotide-diphossugar_trans. DR InterPro; IPR013083; Znf_RING/FYVE/PHD. DR Pfam; PF03552; Cellulose_synt; 1. DR Pfam; PF14569; zf-UDP; 1. DR SUPFAM; SSF53448; SSF53448; 1. PE 3: Inferred from homology; KW Cell membrane {ECO:0000256|RuleBase:RU361116}; KW Cell wall biogenesis/degradation {ECO:0000256|RuleBase:RU361116, KW ECO:0000256|SAAS:SAAS01220012}; KW Cellulose biosynthesis {ECO:0000256|RuleBase:RU361116}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Glycosyltransferase {ECO:0000256|RuleBase:RU361116, KW ECO:0000256|SAAS:SAAS01220026}; KW Membrane {ECO:0000256|RuleBase:RU361116, ECO:0000256|SAAS:SAAS01220013}; KW Metal-binding {ECO:0000256|RuleBase:RU361116}; KW Reference proteome {ECO:0000313|Proteomes:UP000188354}; KW Transferase {ECO:0000256|RuleBase:RU361116, ECO:0000256|SAAS:SAAS01220005}; KW Transmembrane {ECO:0000256|RuleBase:RU361116, KW ECO:0000256|SAAS:SAAS01220035}; KW Transmembrane helix {ECO:0000256|RuleBase:RU361116, KW ECO:0000256|SAAS:SAAS01219998}; Zinc {ECO:0000256|RuleBase:RU361116}; KW Zinc-finger {ECO:0000256|RuleBase:RU361116}. FT TRANSMEM 222..239 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361116" FT TRANSMEM 251..270 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361116" FT TRANSMEM 825..846 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361116" FT TRANSMEM 858..881 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361116" FT TRANSMEM 893..912 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361116" FT TRANSMEM 945..968 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361116" FT TRANSMEM 974..996 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361116" FT TRANSMEM 1008..1028 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361116" FT DOMAIN 32..101 FT /note="zf-UDP" FT /evidence="ECO:0000259|Pfam:PF14569" FT REGION 1..32 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 402..422 FT /evidence="ECO:0000256|SAM:Coils" FT COMPBIAS 1..15 FT /note="Polar" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 1047 AA; 118999 MW; B585335861B283E7 CRC64; MASNSMAGFI TGSHSHISHD SDEHQPPTLQ PSSKECRVCG DEIGYKEDGV LFVACHVCAF PVCKPCYEYE RSEGNQLCPQ CNTRYKRQKG CPRVAGDEEE NFDDDDFEDE FQIKNHHDDD VDREHDVNHV ENGDYNQQKL HTGLAFSSAG SVAGKDLEGD RDFYSNAEWE ERVEKWKVRQ EKRGLLNKED GKEDQGEDDD YLLAEARQPL WRKVPIASSL INPYRIVIIM RLVILAFFFR FRILTPAYDA YPLWLISVIC EIWFALSWIL DQFPKWLPIT RETYLDRLSI RFEREGEPNQ LSPVDVFVSS VDPLKEPPII TANTVLSILS LDYPVEKVCC YVSDDGASML LFDSLAETAE FARRWVPFTK KYNIEPRAPE YYFSQKIDYL KDKVQPTFVK ERRAMKREYE EFKVKINALV AKALKKPEEG WVMQDGTPWP GNNTRDHPGM IQVYLGNAGA LDVEGKELPR LVYISREKRP GYPHHKKAGA MNALVRVSAV LTNAPFMLNL DCDHYINNSK AIREAMCFLM DPQLGKKLCY VQFPQRFDGI DRHDRYANRN TVFFDINMKG LDGIQGPVYV GTGTVFNRQA LYGYDPPVSE KRPKMTCDCW PTWCCFCCGG SRKSKAKKKS GKRGIFGALY SKKKKMMGKD YVRKGSGAMF DLEEIEEGLE GYEDLEKSSL MSQKNFEKRF GQSPVFIAST LVENGGLPEG TNTQSLVKEA IHVISCGYEE KTEWGKEIGW IYGSVTEDIL TGFKMHCRGW KSVYCMPKRP AFKGSAPINL SDRLHQVLRW ALGSVEIFLS RHCPLWYGYG GKLKYLERLA YTNTIVYPFT SIPLIAYCTI PAVCLLTGKF IIPTLTNLAS VWFMALFISI ILTGVLELRW SGVTIEDWWR NEQFWVIGGV SAHLFAVFQG LLKVLAGVDT NFTVTAKAAD DAEFGELYLF KWTTLLIPPT TLIILNIVGV VAGVSGAINN GSGSWGPLFG KLFFAFWVIV HLYPFLKGLM GKQNRTPTIV VLWSILLASI FSLIWVRIDP FLPKQTGPIL KQCGVEC //