ID O81368_POPTM Unreviewed; 978 AA.
AC O81368;
DT 01-NOV-1998, integrated into UniProtKB/TrEMBL.
DT 01-JAN-1999, sequence version 2.
DT 24-JAN-2024, entry version 97.
DE RecName: Full=Cellulose synthase {ECO:0000256|RuleBase:RU361116};
DE EC=2.4.1.12 {ECO:0000256|RuleBase:RU361116};
GN Name=celA {ECO:0000313|EMBL:AAD03417.1};
OS Populus tremuloides (Quaking aspen).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Salicaceae; Saliceae; Populus.
OX NCBI_TaxID=3693 {ECO:0000313|EMBL:AAD03417.1};
RN [1] {ECO:0000313|EMBL:AAD03417.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Secondary xylem {ECO:0000313|EMBL:AAD03417.1};
RX PubMed=10886769; DOI=10.1046/j.1365-313x.2000.00758.x;
RA Wu L., Joshi C.P., Chiang V.L.;
RT "A xylem-specific cellulose synthase gene from aspen (Populus tremuloides)
RT is responsive to mechanical stress.";
RL Plant J. 22:495-502(2000).
RN [2] {ECO:0000313|EMBL:AAD03417.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Secondary xylem {ECO:0000313|EMBL:AAD03417.1};
RA Wu L., Joshi C.P., Chiang V.L.;
RL Submitted (MAY-2019) 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}.
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DR EMBL; AF072131; AAD03417.1; -; mRNA.
DR AlphaFoldDB; O81368; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
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 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:SF31; CELLULOSE SYNTHASE A CATALYTIC SUBUNIT 8 [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.
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 755..782
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361116"
FT TRANSMEM 788..812
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361116"
FT TRANSMEM 824..842
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361116"
FT TRANSMEM 907..925
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361116"
FT TRANSMEM 937..957
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361116"
FT DOMAIN 6..59
FT /note="Cellulose synthase RING-type zinc finger"
FT /evidence="ECO:0000259|Pfam:PF14569"
FT REGION 120..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 379..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 978 AA; 110280 MW; C351B0E4975C6B8A CRC64;
MMESGAPICH TCGEQVGHDA NGELFVACHE CSYPMCKSCF EFEINEGRKV CLRCGSPYDE
NLLDDVEKKG SGNQSTMASH LNDSQDVGIH ARHISSVSTV DSEMNDEYGN PIWKNRVKSC
KDKENKKKKR SPKAETEPAQ VPTEQQMEEK PSAEASEPLS IVYPIPRNKL TPYRAVIIMR
LVILGLFFHF RITNPVDSAF GLWLTSVICE IWFAFSWVLD QFPKWNPVNR ETYIERLSAR
YEREGEPSQL AGVDFFVSTV DPLKEPPLIT ANTVLSILAV DYPVDKVSCY VSDDGAAMLS
FESLVETAEF ARKWVPFCKK FSIEPRAPEF YFSQKIDYLK DKVQPSFVKE RRAMKRDYEE
YKVRVNALVA KAQKTPEEGW TMQDGTPWPG NNTRDHPGHD SGLPWEILGA RDIEGNELPR
LVYVSREKRP GYQHHKKAGA ENALVRVSAV LTNAPYILNV DCDHYVNNSK AVREAMCILM
DPQVGRDVCY VQFPQRFDGI DKSDRYANRN VVFFDVNMKG LDGIQGPVYV GTGCVFNRQA
LYGYGPPSMP SLRKRKDSSS CFSCCCPSKK KPAQDPAEVY RDAKREDLNA AIFNLTEIDN
YDEHERSMLI SQLSFEKTFG LSSVFIESTL MENGGVPESA NSPPFIKEAI QVIGCGYEEK
TEWGKQIGWI YGSVTEDILS GFKMHCRGWR SIYCMPVRPA FKGSAPINLS DRLHQVLRWA
LGSVEIFFSR HCPLWYGFGG GRLKWLQRLA YINTIVYPFT SLPLIAYCTI PAVCLLTGKF
IIPTLSNLAS MLFLGLFISI IVTAVLELRW SGVSIEDLWR NEQFWVIGGV SAHLFAVFQG
FLKMLAGIDT NFTVTAKAAE DAEFGELYMV KWTTLLIPPT TLLIINMSGC AGFSDALNKG
YEAWGPLFGK VFFAFWVILH LYPFLKGLMG RQNLTPTIVV LWSVLLASVF SLVWVKINPF
VNKVDNTLVA ETCISIDC
//
