ID I1Q9H4_ORYGL Unreviewed; 1092 AA.
AC I1Q9H4;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=Cellulose synthase {ECO:0000256|RuleBase:RU361116};
DE EC=2.4.1.12 {ECO:0000256|RuleBase:RU361116};
OS Oryza glaberrima (African rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4538 {ECO:0000313|EnsemblPlants:ORGLA07G0076600.1, ECO:0000313|Proteomes:UP000007306};
RN [1] {ECO:0000313|Proteomes:UP000007306}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IRGC 96717 {ECO:0000313|Proteomes:UP000007306};
RA Wing R.A., Yu Y., Rounsley S., Reddy-Marri P., Goicoechea J.L.,
RA Sisneros N., Lee S., Song X., Angelova A., Kudrna D.P., de Baynast K.,
RA Zuccolo A.;
RT "The complete genome of Oryza glaberrima.";
RL Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:ORGLA07G0076600.1}
RP IDENTIFICATION.
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 AlphaFoldDB; I1Q9H4; -.
DR SMR; I1Q9H4; -.
DR STRING; 4538.I1Q9H4; -.
DR EnsemblPlants; ORGLA07G0076600.1; ORGLA07G0076600.1; ORGLA07G0076600.
DR Gramene; ORGLA07G0076600.1; ORGLA07G0076600.1; ORGLA07G0076600.
DR eggNOG; ENOG502QQGG; Eukaryota.
DR HOGENOM; CLU_001418_0_1_1; -.
DR OMA; ISWVEND; -.
DR UniPathway; UPA00695; -.
DR Proteomes; UP000007306; Unassembled WGS sequence.
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 GO; GO:0071669; P:plant-type cell wall organization or biogenesis; IEA:UniProt.
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:SF255; CELLULOSE SYNTHASE A CATALYTIC SUBUNIT 6 [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.
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 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 275..293
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361116"
FT TRANSMEM 305..324
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361116"
FT TRANSMEM 870..890
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361116"
FT TRANSMEM 902..920
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361116"
FT TRANSMEM 940..960
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361116"
FT TRANSMEM 981..1002
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361116"
FT TRANSMEM 1022..1040
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361116"
FT TRANSMEM 1052..1072
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361116"
FT DOMAIN 42..88
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 100..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..118
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1092 AA; 122410 MW; C6739B6FCB6A91D5 CRC64;
MEASAGLVAG SHNRNELVVI RRDGGGGGGV GGRRAAEAKA ACQICGDDVG EGPDGEPFVA
CNECAFPVCR NCYDYERREG SQACPQCKTR FKRLKGCPRV AGDEEEDGVD DLEGEFGLDG
REDDPQYIAE SMLRANMSYG RGGDLQPFQP IPNVPLLTNG QMVDDIPPEQ HALVPSYMGG
GGGGGKRIHP LPFADPSVPV QPRSMDPSKD LAAYGYGSVA WKERMEGWKQ KQERMQQLRS
EGGGDWDGDG DADLPLMDEA RQPLSRKVPI SSSRINPYRM IIIIRLVVLG FFFHYRVMHP
VNDAFALWLI SVICEIWFAM SWILDQFPKW LPIERETYLD RLSLRFDKEG QPSQLAPVDF
FVSTVDPSKE PPLVTANTVL SILSVDYPVE KVSCYVSDDG AAMLTFEALS ETSEFAKKWV
PFCKKFNIEP RAPEWYFQQK IDYLKDKVAA SFVRERRAMK RDYEEFKVRI NALVAKAQKV
PEEGWTMQDG SPWPGNNVRD HPGMIQVFLG QSGGRDVEGN ELPRLVYVSR EKRPGYNHHK
KAGAMNALVR VSAVLSNAPY LLNLDCDHYI NNSKAIREAM CFMMDPLVGK KVCYVQFPQR
FDGIDRHDRY ANRNVVFFDI NMKGLDGIQG PIYVGTGCVF RRQALYGYDA PKTKKPPSRT
CNCWPKWCCC CCCGNRHTKK KTTKPKPEKK KRLFFKKAEN QSPAYALGEI EEGAPGAETD
KAGIVNQQKL EKKFGQSSVF VASTLLENGG TLKSASPASL LKEAIHVISC GYEDKTDWGK
EIGWIYGSIT EDILTGFKMH CHGWRSIYCI PKRPAFKGSA PLNLSDRLHQ VLRWALGSVE
IFFSKHCPLW YGYGGGLKFL ERFSYINSIV YPWTSIPLLA YCTLPAICLL TGKFITPELT
NVASLWFMSL FICIFVTGIL EMRWSGVAID DWWRNEQFWV IGGVSSHLFA VFQGLLKVLA
GVDTSFTVTS KAGDDEEFSE LYTFKWTTLL IPPTTLLLLN FIGVVAGVSN AINNGYESWG
PLFGKLFFAF WVIVHLYPFL KGLVGRQNRT PTIVIVWSIL LASIFSLLWV RIDPFLAKNN
GPLLEECGLD CN
//
