ID A0A397XRW4_BRACM Unreviewed; 1019 AA. AC A0A397XRW4; DT 05-DEC-2018, integrated into UniProtKB/TrEMBL. DT 05-DEC-2018, sequence version 1. DT 28-JUN-2023, entry version 20. DE RecName: Full=Cellulose synthase {ECO:0000256|RuleBase:RU361116}; DE EC=2.4.1.12 {ECO:0000256|RuleBase:RU361116}; GN ORFNames=BRARA_I00796 {ECO:0000313|EMBL:RID43965.1}; OS Brassica campestris (Field mustard). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica. OX NCBI_TaxID=3711 {ECO:0000313|EMBL:RID43965.1, ECO:0000313|Proteomes:UP000264353}; RN [1] {ECO:0000313|EMBL:RID43965.1, ECO:0000313|Proteomes:UP000264353} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. B-3 {ECO:0000313|Proteomes:UP000264353}; RA Bowman J., Kohchi T., Yamato K., Jenkins J., Shu S., Ishizaki K., RA Yamaoka S., Nishihama R., Nakamura Y., Berger F., Adam C., Aki S., RA Althoff F., Araki T., Arteaga-Vazquez M., Balasubrmanian S., Bauer D., RA Boehm C., Briginshaw L., Caballero-Perez J., Catarino B., Chen F., RA Chiyoda S., Chovatia M., Davies K., Delmans M., Demura T., Dierschke T., RA Dolan L., Dorantes-Acosta A., Eklund D., Florent S., Flores-Sandoval E., RA Fujiyama A., Fukuzawa H., Galik B., Grimanelli D., Grimwood J., RA Grossniklaus U., Hamada T., Haseloff J., Hetherington A., Higo A., RA Hirakawa Y., Hundley H., Ikeda Y., Inoue K., Inoue S., Ishida S., Jia Q., RA Kakita M., Kanazawa T., Kawai Y., Kawashima T., Kennedy M., Kinose K., RA Kinoshita T., Kohara Y., Koide E., Komatsu K., Kopischke S., Kubo M., RA Kyozuka J., Lagercrantz U., Lin S., Lindquist E., Lipzen A., Lu C., RA Luna E., Martienssen R., Minamino N., Mizutani M., Mizutani M., RA Mochizuki N., Monte I., Mosher R., Nagasaki H., Nakagami H., Naramoto S., RA Nishitani K., Ohtani M., Okamoto T., Okumura M., Phillips J., Pollak B., RA Reinders A., Roevekamp M., Sano R., Sawa S., Schmid M., Shirakawa M., RA Solano R., Spunde A., Suetsugu N., Sugano S., Sugiyama A., Sun R., RA Suzuki Y., Takenaka M., Takezawa D., Tomogane H., Tsuzuki M., Ueda T., RA Umeda M., Ward J., Watanabe Y., Yazaki K., Yokoyama R., Yoshitake Y., RA Yotsui I., Zachgo S., Schmutz J.; RT "WGS assembly of Brassica rapa FPsc."; RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases. 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}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {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; CM010636; RID43965.1; -; Genomic_DNA. DR AlphaFoldDB; A0A397XRW4; -. DR STRING; 3711.Bra037793.1-P; -. DR UniPathway; UPA00695; -. DR Proteomes; UP000264353; Chromosome a9. 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:SF159; CELLULOSE SYNTHASE A CATALYTIC SUBUNIT 6 [UDP-FORMING]; 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 3: Inferred from homology; 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}; Coiled coil {ECO:0000256|SAM:Coils}; KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676, KW ECO:0000256|RuleBase:RU361116}; Manganese {ECO:0000256|ARBA:ARBA00023211}; KW Membrane {ECO:0000256|RuleBase:RU361116}; KW Metal-binding {ECO:0000256|RuleBase:RU361116}; 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|PROSITE- KW ProRule:PRU00175}. FT TRANSMEM 274..294 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361116" FT TRANSMEM 301..320 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361116" FT TRANSMEM 863..883 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361116" FT TRANSMEM 895..913 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361116" FT TRANSMEM 950..968 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361116" FT TRANSMEM 980..998 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361116" FT DOMAIN 39..85 FT /note="RING-type" FT /evidence="ECO:0000259|PROSITE:PS50089" FT REGION 130..150 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 673..700 FT /evidence="ECO:0000256|SAM:Coils" FT COMPBIAS 130..148 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 1019 AA; 115699 MW; EEE8F4ED65BA68CA CRC64; MNTGGRLIAG SHNRNEFVLI NADESARIRS VQELRGQTCE ICRDEVELTV DGEPFVACNE CAFPVCRPCY EYERREGNQA CPQCKTRYKR LKGSPRVEND EEEDDIDDID NEFDYMNNGG IGFDQVSEGM SVSRRHSGFP QSDLDSAPPG SQIPLLTYGD EDIEISSDRH ALIVPPSLSG HSHRGHPASL SDPTIAAHPR PMVPQKDLAV YGYGSVAWKD RMEEWKRKQN EKLQVVKHEG DPDFEDGDDI PMMDEGRQPL SRKIPIKSSK INPYRMLIVL RLVILGLFFH YRILHPVKDA YALWLISVIC EIWFAVSWVL DQFPKWYPIE RETYLDRLSL RYEKEGKPSE LSAVDVFVST VDPLKEPPLI TANTVLSILA VDYPVDRVAC YVSDDGAAML TFEALSETAE FARKWVPFCK KYCIEPRAPE WYFCHKMDYL KNKVHPAFVR ERRAMKRDYE EFKVKINALV ATAQKVPEEG WTMQDGTPWP GNSTRDHPGM IQVFLGSDGV RDVENNELPR LVYVSREKRP GFDHHKKAGA MNSLIRVSGV LSNAPYLLNV DCDHYINNSK ALREAMCFMM DPQSGKKICY VQFPQRFDGI DRHDRYSNRN VVFFDINMKG LDGLQGPIYV GTGCVFRRQA LYGFDAPKKK KAPRKTCNCW PKWCFLCCGS RKNRKAKTAA ADKKKKNREA SKQIHALENI EEGRVTTKGS NVELSTEAMQ LKLEKKFGQS PVFVASARME NGGMARNASP ACLLKEAIQV ISCGYEDKTE WGKEIGWIYG SVTEDILTGF KMHSHGWRSV YCTPKLPAFK GSAPINLSDR LHQVLRWALG SVEIFLSRHC PIWYGYGGGL KWLERLSYIN SVVYPWTSLP LIVYCSLPAI CLLTGKFIVP EISNYASILF MALFSSIAVT GVLEMQWGKV GIDDWWRNEQ FWVIGGVSAH LNGYDSWGPL FGRLFFALWV VIHLYPFLKG LLGKQDRMPT IIVVWSILLA SILTLLWVRV NPFVAKGGPI LEICGLDCL //