ID K4CB55_SOLLC Unreviewed; 1041 AA.
AC K4CB55;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 72.
DE RecName: Full=Cellulose synthase {ECO:0000256|RuleBase:RU361116};
DE EC=2.4.1.12 {ECO:0000256|RuleBase:RU361116};
GN Name=101248888 {ECO:0000313|EnsemblPlants:Solyc07g005840.2.1};
OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=4081 {ECO:0000313|EnsemblPlants:Solyc07g005840.2.1};
RN [1] {ECO:0000313|EnsemblPlants:Solyc07g005840.2.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Heinz 1706 {ECO:0000313|EnsemblPlants:Solyc07g005840.2.1};
RX PubMed=22660326; DOI=10.1038/nature11119;
RG Tomato Genome Consortium;
RT "The tomato genome sequence provides insights into fleshy fruit
RT evolution.";
RL Nature 485:635-641(2012).
RN [2] {ECO:0000313|EnsemblPlants:Solyc07g005840.2.1}
RP IDENTIFICATION.
RC STRAIN=cv. Heinz 1706 {ECO:0000313|EnsemblPlants:Solyc07g005840.2.1};
RG EnsemblPlants;
RL Submitted (JUN-2015) to UniProtKB.
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 RefSeq; XP_004242614.1; XM_004242566.3.
DR AlphaFoldDB; K4CB55; -.
DR STRING; 4081.K4CB55; -.
DR PaxDb; 4081-Solyc07g005840-2-1; -.
DR EnsemblPlants; Solyc07g005840.2.1; Solyc07g005840.2.1; Solyc07g005840.2.
DR GeneID; 101248888; -.
DR Gramene; Solyc07g005840.2.1; Solyc07g005840.2.1; Solyc07g005840.2.
DR KEGG; sly:101248888; -.
DR eggNOG; ENOG502QQXZ; Eukaryota.
DR HOGENOM; CLU_001418_0_2_1; -.
DR InParanoid; K4CB55; -.
DR OMA; NGQVCEI; -.
DR OrthoDB; 1210919at2759; -.
DR PhylomeDB; K4CB55; -.
DR UniPathway; UPA00695; -.
DR Proteomes; UP000004994; Chromosome 7.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0016760; F:cellulose synthase (UDP-forming) activity; IEA:UniProtKB-EC.
DR GO; GO:0016759; F:cellulose synthase activity; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0009833; P:plant-type primary cell wall biogenesis; IBA:GO_Central.
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:SF28; CELLULOSE SYNTHASE A CATALYTIC SUBUNIT 7 [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};
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 Reference proteome {ECO:0000313|Proteomes:UP000004994};
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 250..268
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361116"
FT TRANSMEM 280..299
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361116"
FT TRANSMEM 820..840
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361116"
FT TRANSMEM 852..870
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361116"
FT TRANSMEM 890..910
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361116"
FT TRANSMEM 931..952
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361116"
FT TRANSMEM 972..990
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361116"
FT TRANSMEM 1002..1022
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361116"
FT DOMAIN 37..83
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
SQ SEQUENCE 1041 AA; 117589 MW; 69BF85DFEC82CBE6 CRC64;
MEASAGLVAG SHNRNELVVI HGHEEHKPLK DLSGQVCDIC GDEIGLTVDG DLFVACNECG
FPVCRPCYEY ERREGTQQCP QCKTRYKRLK GSPRVAGDDD EEDIDDIEHE FKVDDDQNKN
RNIVETILHG KMTYGRGPED EDSAQYPPVI AGTRSHPVSG EFPISNHGNG EQMLGSSLHK
RIHPYPASES GSARWDDKKE GGWKERMEDW KFQQGHAGQD YDDSADVDMS MVDEARQPLS
RKVPIASSKI NPYRMVIVAR LVILAVFLRY RILNPVHDAI GLWLTSIICE IWFAFSWILD
QFPKWFPIDR ETYLDRLSLR YEREGEPNML APVDVFVSTV DPMKEPPLVT ANTILSILAM
DYPVDKISCY LSDDGASMCT FEALSETAEF ARKWVPFCKK FAIEPRAPEF YFSLKIDYLK
DKIQPTFVKE RRAMKREYEE FKVRINALVA KATKMPPGGW IMQDGTPWPG NNTRDHPGMI
QVFLGQSGGT DVDGHELPRL VYVSREKRPG FQHHKKAGAM NALVRVSGVL TNAPFMLNLD
CDHYLNNSKA AREAMCFLMD TQMGKKVCFV QFPQRFDGID KHDRYANRNT VFFDINMKGL
DGLQGPVYVG TGCVFRRQAL YGYNPPKRAK RPRMVSCDCC PCFGRKKKLD KYKSEVNADA
ANAQGFDDDN ELLMSQMNFE KKFGQSAIFV TSTLMIEGGV PPSSSPAALL KEAIHVISCG
YEDKTEWGLE LGWIYGSITE DILTGFKMHC RGWRSVYCMP KLAAFKGSAP INLSDRLNQV
LRWALGSVEI FFSHHSPVWY GYKGGNLKWL ERLSYINTTI YPFTSLPLLA YCTLPAVCLL
TGKFIMPEIS TLASLFFIAL FLSIFTTGIL ELRWSGVSIE EWWRNEQFWV IGGVSAHLFA
VVQGLLKILA GIDTNFTVTS KATDDEDFGE LYAFKWTTLL IPPTTILIIN LVGVVAGISD
AINNGYNSWG PLFGKLFFAF WVIVHLYPFL KGLMGRQNRT PTIVVIWSIL LASIFSLLWV
RIDPFVLKTK GPDVKRCGVN C
//
