ID Q2IB38_EUCGR Unreviewed; 1097 AA.
AC Q2IB38;
DT 07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 07-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE RecName: Full=Cellulose synthase {ECO:0000256|RuleBase:RU361116};
DE EC=2.4.1.12 {ECO:0000256|RuleBase:RU361116};
GN Name=CesA6 {ECO:0000313|EMBL:AAY60848.1};
OS Eucalyptus grandis (Flooded gum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Myrtales; Myrtaceae; Myrtoideae; Eucalypteae; Eucalyptus.
OX NCBI_TaxID=71139 {ECO:0000313|EMBL:AAY60848.1};
RN [1] {ECO:0000313|EMBL:AAY60848.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=16452068;
RA Ranik M., Myburg A.A.;
RT "Six new cellulose synthase genes from Eucalyptus are associated with
RT primary and secondary cell wall biosynthesis.";
RL Tree Physiol. 26:545-556(2006).
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 ---------------------------------------------------------------------------
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; DQ014510; AAY60848.1; -; mRNA.
DR RefSeq; NP_001289648.1; NM_001302719.1.
DR AlphaFoldDB; Q2IB38; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR GeneID; 104450372; -.
DR KEGG; egr:104450372; -.
DR OrthoDB; 1210919at2759; -.
DR UniPathway; UPA00695; -.
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; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR13301:SF222; CELLULOSE SYNTHASE A CATALYTIC SUBUNIT 3 [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.
PE 2: Evidence at transcript 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 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|RuleBase:RU361116}.
FT TRANSMEM 286..306
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361116"
FT TRANSMEM 313..332
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361116"
FT TRANSMEM 875..895
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361116"
FT TRANSMEM 907..925
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361116"
FT TRANSMEM 945..965
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361116"
FT TRANSMEM 986..1007
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361116"
FT TRANSMEM 1027..1045
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361116"
FT TRANSMEM 1057..1077
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361116"
FT DOMAIN 29..105
FT /note="Cellulose synthase RING-type zinc finger"
FT /evidence="ECO:0000259|Pfam:PF14569"
FT REGION 241..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..258
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1097 AA; 123474 MW; 758C24F9A204247D CRC64;
MEVSSGLVAG SHNRNELVVI RRENELGQKP LQKLSGQICQ ICGDDVGLTV DGELFVACNE
CAFPICRTCY EYERREGSQI CPQCKTRFKR LRGCARVDGD EEEDGVDDLE NEFNFDGRHR
QEMDRQGYGA EAMLHGHMSY GRGSDLDLPH VHPLPQVPLL ANGQMVDDVP PEHHALVPAY
MGAGGGGGGG GKRIHPLPFT DSGLPVQPRS MDPSKDLAAY GYGSVAWKER MESWKQKQEK
LQTMKNEKGG KEWDDDGDNP DLPLMDEARQ PLSRRLPISS SQINPYRMII VIRLVVLGFF
FHYRVVHPVN DAYALWLISV ICEIWFGLSW ILDQFPKWLP IDRETYLDRL SLRYEKEGQP
SQLAPVDIFV STVDPLKEPP LVTANTVLSI LAVDYPVDKV SCYVSDDGAA MLTFEALSET
SEFARKWAPF CKKFNIEPRA PEFYFAQKID YLKDKVEASF VKERRAMKRE YEEFKVRINA
LVAKAQKVPE EGWTMQDGTP WPGNNVRDHP GMIQVFLGQS GGHDSDGNEL PRLVYVSREK
RPGYNHHKKA GAMNALVRVS AVLTNAPYLL NLDCDHYFNN SKAIREAMCF MVDPLIGKRV
CYVQFPQRFD GIDRHDRYAN RNTVFFDINM KGLDGIQGPI YVGTGCVFRR LALYGYDAPK
AKKPPTRTCN CLPKWCCCGC CCSGKKKKKK TTKPKTELKK RFFKKKDAGT PPPLEGIEEG
IEVIESENPT PQHKLEKKFG QSSVFVASTL LEDGGTLKGT SPASLLKEAI HVISCGYEDK
TEWGKEVGWI YGSVTEDILT GFKMHCHGWR SIYCIPARPA FKGSAPINLS DRLHQVLRWA
LGSIEIFLSR HCPLWYGYGG GLKWLERLSY INATVYPWTS IPLLAYCTLP AVCLLTGKFI
TPELSNVASL WFLSLFICIF ATSILEMRWS GVGIEEWWRN EQFWVIGGVS AHLFAVFQGL
LKVLAGVDTN FTVTSKGGDD KEFSELYAFK WTTLLIPPTT LLIINLIGVV AGVSNAINNG
HESWGPLFGK LFFAFWVIVH LYPFLKGLLG RQNRTPTIII VWSILLASIF SLLWVRIDPF
LAKSDGPLLE ECGLDCN
//
