ID D8L1W4_BRANA Unreviewed; 1066 AA.
AC D8L1W4;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=Cellulose synthase {ECO:0000256|RuleBase:RU361116};
DE EC=2.4.1.12 {ECO:0000256|RuleBase:RU361116};
GN Name=CesA3.1 {ECO:0000313|EMBL:ACS68192.1};
OS Brassica napus (Rape).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=3708 {ECO:0000313|EMBL:ACS68192.1};
RN [1] {ECO:0000313|EMBL:ACS68192.1}
RP NUCLEOTIDE SEQUENCE.
RA Jiang Y., Deyholos M.K.;
RT "Functional analysis of cellulose synthase (CesA) gene family in canola
RT (Brassica napus).";
RL Submitted (DEC-2008) 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}.
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DR EMBL; FJ529172; ACS68192.1; -; mRNA.
DR RefSeq; NP_001303106.1; NM_001316177.1.
DR RefSeq; XP_013718960.1; XM_013863506.1.
DR AlphaFoldDB; D8L1W4; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR GeneID; 106422729; -.
DR KEGG; bna:106422729; -.
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; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR13301:SF206; CELLULOSE SYNTHASE A CATALYTIC SUBUNIT 3 [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 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|PROSITE-
KW ProRule:PRU00175}.
FT TRANSMEM 259..278
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361116"
FT TRANSMEM 285..305
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361116"
FT TRANSMEM 844..864
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361116"
FT TRANSMEM 876..894
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361116"
FT TRANSMEM 914..936
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361116"
FT TRANSMEM 957..985
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361116"
FT TRANSMEM 997..1015
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361116"
FT TRANSMEM 1027..1047
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361116"
FT DOMAIN 20..66
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 119..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 203..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 644..673
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..135
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..180
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 653..670
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1066 AA; 119794 MW; CA006C93E4DDDAFC CRC64;
MESDGETAGK PMTSVGGQIC QICSDNVGKT VDGDRFVACD ICGFPVCRPC YEYERKHGNQ
SCPQCKTTYK RHKGSPAIPG DKDEDVFADE ATVELNYPQK EKISERMLGW HLTRGKSEEM
GQPEYDKEVS HNHLPRLTSR QDTSGEFSAA SPERLSVSST IAGGKRLPYS SDINQSPNRR
ISDPVGLGNV AWKERVDGWK MKQEKNTGGP VSTQAASERG GGDIDASTDI LADEALLNDE
ARQPLSRKVS IPSSRINPYR MVIMLRLVIL CLFLHYRITN PVPNAFTLWL ISVICEIWFA
FSWILDQFPK WFPVNRETYL DRLALRYDRE GEPSQLAAVD IFVSTVDPLK EPPLVTANTV
LSILAVDYPV DKVSCYVSDD GAAMLSFEAL AETSEFARKW VPFCKKYSIE PRAPEWYFAA
KIDYLKDKVQ TSFVKDRRAM KREYEEFKIR INALVSKALK CPEEGWVMQD GTPWPGNNTR
DHPGMIQVFL GQNGGLDAEG NELPRLVYVS REKRPGFQHH KKAGAMNALV RVSAVLTNGP
FILNLDCDHY INNSKALREA MCFLMDPNLG KQVCYVQFPQ RFDGIDKNDR YANRNTVFFD
INLRGLDGIQ GPVYVGTGCV FNRTALYGYE PPIKVKHKKP SLLSKLCGGS RKKNSKSKKD
SDKKKSGRHT DSTVPVFNLD DIEEGVEGAG FDDEKALLMS QMSLEKRFGQ SAVFVASTLM
ENGGVPPTET PENLLKEAIH VISCGYEDKS DWGMEIGWIY GSVTEDILTG FKMHARGWRS
IYCMPKLPAF KGSAPINLSD RLNQVLRWAL GSVEILFSRH CPIWYGYSGR LKFLERFAYV
NTTIYPLTSV PLLFYCTLPA VCLFTNQFII PQISNIASIW FLSLFLSIFA TGILEMRWSG
VGIDEWWRNE QFWVIGGVSA HLFAVFQGLL KVLAGIDTNF TVTSKASDED GDFAELYLFK
WTTLLIPPTT LLIVNLVGVV AGFSYAINSG YQSWGPLFGK LFFAFWVIVH LYPFLKGLMG
RQNRTPTIVV VWSVLLASIF SLLWVRIDPF TKRVTGPDIL ECGINC
//
