ID F6I0N5_VITVI Unreviewed; 1094 AA.
AC F6I0N5;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=Cellulose synthase {ECO:0000256|RuleBase:RU361116};
DE EC=2.4.1.12 {ECO:0000256|RuleBase:RU361116};
GN OrderedLocusNames=VIT_03s0038g04250 {ECO:0000313|EMBL:CCB60501.1};
OS Vitis vinifera (Grape).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; Vitales; Vitaceae; Viteae; Vitis.
OX NCBI_TaxID=29760 {ECO:0000313|EMBL:CCB60501.1, ECO:0000313|Proteomes:UP000009183};
RN [1] {ECO:0000313|Proteomes:UP000009183}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Pinot noir / PN40024 {ECO:0000313|Proteomes:UP000009183};
RX PubMed=17721507; DOI=10.1038/nature06148;
RG The French-Italian Public Consortium for Grapevine Genome Characterization.;
RA Jaillon O., Aury J.-M., Noel B., Policriti A., Clepet C., Casagrande A.,
RA Choisne N., Aubourg S., Vitulo N., Jubin C., Vezzi A., Legeai F.,
RA Hugueney P., Dasilva C., Horner D., Mica E., Jublot D., Poulain J.,
RA Bruyere C., Billault A., Segurens B., Gouyvenoux M., Ugarte E.,
RA Cattonaro F., Anthouard V., Vico V., Del Fabbro C., Alaux M.,
RA Di Gaspero G., Dumas V., Felice N., Paillard S., Juman I., Moroldo M.,
RA Scalabrin S., Canaguier A., Le Clainche I., Malacrida G., Durand E.,
RA Pesole G., Laucou V., Chatelet P., Merdinoglu D., Delledonne M.,
RA Pezzotti M., Lecharny A., Scarpelli C., Artiguenave F., Pe M.E., Valle G.,
RA Morgante M., Caboche M., Adam-Blondon A.-F., Weissenbach J., Quetier F.,
RA Wincker P.;
RT "The grapevine genome sequence suggests ancestral hexaploidization in major
RT angiosperm phyla.";
RL Nature 449:463-467(2007).
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; FN596508; CCB60501.1; -; Genomic_DNA.
DR RefSeq; XP_010645442.1; XM_010647140.2.
DR AlphaFoldDB; F6I0N5; -.
DR STRING; 29760.F6I0N5; -.
DR PaxDb; 29760-VIT_03s0038g04250-t01; -.
DR EnsemblPlants; Vitvi03g00274_t001; Vitvi03g00274_P001; Vitvi03g00274.
DR GeneID; 100264115; -.
DR Gramene; Vitvi03g00274_t001; Vitvi03g00274_P001; Vitvi03g00274.
DR KEGG; vvi:100264115; -.
DR eggNOG; ENOG502QQGG; Eukaryota.
DR HOGENOM; CLU_001418_0_0_1; -.
DR InParanoid; F6I0N5; -.
DR OrthoDB; 1210919at2759; -.
DR UniPathway; UPA00695; -.
DR Proteomes; UP000009183; Chromosome 3.
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:SF259; CELLULOSE SYNTHASE; 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:UP000009183};
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 278..296
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361116"
FT TRANSMEM 308..327
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361116"
FT TRANSMEM 872..892
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361116"
FT TRANSMEM 904..922
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361116"
FT TRANSMEM 942..962
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361116"
FT TRANSMEM 983..1004
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361116"
FT TRANSMEM 1024..1042
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361116"
FT TRANSMEM 1054..1074
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361116"
FT DOMAIN 40..86
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
SQ SEQUENCE 1094 AA; 123246 MW; 4C4015E3F5461D6E CRC64;
MEASAGLVAG SHNRNELVVI RREGEAAGRK PLANLSGQTC QICGDDVGLT AEGELFVACN
ECAFPICRTC YEYERSEGNQ VCPQCKTRFK RLKGCARVEG DEEEDDVDDL ENEFNFVGRR
RDTQDMQYIA EGMLQGHMTY GRAGDADMLP QVVNTMPTVP LLTNGQMVDD IPPEHHALVP
SFLGGGGKRI HPLPFSDPAF PVQPRSMDPS KDLAAYGYGS VAWKERMENW KQKQEKLQVM
NENGGKDWDN DGDGPDLPLM DEARQPLSRK LPVPSSQINP YRMIIIIRLV VLGFFFHYRV
MHPVNDAYAL WLVSVICEIW FAISWILDQF PKWLPIDRET YLDRLSLRYD KEGQPSQLSS
VDIFVSTVDP LKEPPLVTAN TVLSILAVDY PVDKVSCYVS DDGAAMLTFE ALSETSEFAR
KWVPFCKKFN IEPRAPEFYF AQKIDYLQDK VLTSFVKDRR AMKREYEEFK VRINALVAKA
QKVPEEGWTM QDGTPWPGNN VRDHPGMIQV FLGQSGGHDT EGNELPRLVY VSREKRPGFN
HHKKAGAMNA LVRVSAVLTN APYLLNLDCD HYFNNSKALK EAMCFMMDPL LGKKVCYVQF
PQRFDGIDRH DRYANRNIVF FDINMKGLDG IQGPIYVGTG CVFRRQAFYG NDAPKTKKPP
TRTCNCWPNW CCCGCCFSGK KKKKTTKSKS EKKQKKFRRL DSGAPVFALE GIEEGIEGIE
SEKSTMLSET KLEKKFGQSP VFVASTLLED GGTLKIASPA SLLKEAIHVI SCGYEDKTDW
GKEVGWIYGS VTEDILTGFK MHCHGWRSIY CIPDRPAFKG SAPINLSDRL HQVLRWALGS
VEIFLSRHCP LWYGYGGGLK WLERLSYINA TVYPWTSIPL VAYCTLPAVC LLTGKFITPE
LSNVASLWFL SLFICIFATS ILEMRWSGVG IDDWWRNEQF WVIGGVSAHL FAVFQGLLKV
LAGIDTDFTV TSKAGDDEDF SELYAFKWTT LLIPPTTLLI INLIGVVAGV SNAINNGYES
WGPLFGKLFF AFWVIVHLYP FLKGLLGRQN RTPTIIIVWS ILLASIFSLL WVRVDPFLAK
SDGPVLEECG LDCH
//
