ID V7CR98_PHAVU Unreviewed; 976 AA.
AC V7CR98;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE RecName: Full=Cellulose synthase {ECO:0000256|RuleBase:RU361116};
DE EC=2.4.1.12 {ECO:0000256|RuleBase:RU361116};
GN ORFNames=PHAVU_002G240200g {ECO:0000313|EMBL:ESW31466.1};
OS Phaseolus vulgaris (Kidney bean) (French bean).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Phaseolus.
OX NCBI_TaxID=3885 {ECO:0000313|EMBL:ESW31466.1, ECO:0000313|Proteomes:UP000000226};
RN [1] {ECO:0000313|Proteomes:UP000000226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. G19833 {ECO:0000313|Proteomes:UP000000226};
RX PubMed=24908249; DOI=10.1038/ng.3008;
RA Schmutz J., McClean P.E., Mamidi S., Wu G.A., Cannon S.B., Grimwood J.,
RA Jenkins J., Shu S., Song Q., Chavarro C., Torres-Torres M., Geffroy V.,
RA Moghaddam S.M., Gao D., Abernathy B., Barry K., Blair M., Brick M.A.,
RA Chovatia M., Gepts P., Goodstein D.M., Gonzales M., Hellsten U.,
RA Hyten D.L., Jia G., Kelly J.D., Kudrna D., Lee R., Richard M.M.,
RA Miklas P.N., Osorno J.M., Rodrigues J., Thareau V., Urrea C.A., Wang M.,
RA Yu Y., Zhang M., Wing R.A., Cregan P.B., Rokhsar D.S., Jackson S.A.;
RT "A reference genome for common bean and genome-wide analysis of dual
RT domestications.";
RL Nat. Genet. 46:707-713(2014).
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; CM002289; ESW31466.1; -; Genomic_DNA.
DR RefSeq; XP_007159472.1; XM_007159410.1.
DR AlphaFoldDB; V7CR98; -.
DR STRING; 3885.V7CR98; -.
DR EnsemblPlants; ESW31466; ESW31466; PHAVU_002G240200g.
DR GeneID; 18638944; -.
DR Gramene; ESW31466; ESW31466; PHAVU_002G240200g.
DR KEGG; pvu:PHAVU_002G240200g; -.
DR eggNOG; ENOG502QTVZ; Eukaryota.
DR OMA; EHELNED; -.
DR OrthoDB; 1210919at2759; -.
DR UniPathway; UPA00695; -.
DR Proteomes; UP000000226; Chromosome 2.
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 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:UP000000226};
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 752..773
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361116"
FT TRANSMEM 785..803
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361116"
FT TRANSMEM 823..843
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361116"
FT TRANSMEM 864..885
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361116"
FT TRANSMEM 905..923
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361116"
FT TRANSMEM 935..955
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361116"
FT DOMAIN 7..61
FT /note="Cellulose synthase RING-type zinc finger"
FT /evidence="ECO:0000259|Pfam:PF14569"
FT REGION 75..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 128..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..103
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 976 AA; 110236 MW; 05706E104C17195F CRC64;
MVQSGVPLCN TCGEQVGLDD NGEVFVACHE CNFPICKDCF EHELNEDHRV CMKCGTPYEE
RTKKEEEEDF HEIEVHENQS TMASEISNSQ DVGLHARHAS SVSTVDSEVH EESGKSFWKN
RVESWKGKDK KNKKKKAAPK VENEASVPPE QQMEEKRPTE AAAAPLSVTI PMSKSKIAPY
RTVIIMRLII LGLFFHYRVT NPVHSAFPLW LTSIICEIWF AFSWVLDQFP KWFPVNRQTF
IDNLSARFER EGETNELAAV DFFVSTVDPL KEPPLITANT VLSILAVDYP VDKVSCYVSD
DGAAMLTFES LVETADFARK WVPFCKKFSI EPRAPEYYFS QKIDYLKDKV QPSFVKERRA
MKRDYDEYKV RVNAMVAKAQ KTPEEGWTMK DGTPWPGNNS RDHPGMIQVF LGHTGARDIE
GNELPRLVYV SREKRPGYQH HKKAGAENAL VRGSAVLTNA PFILNLDCDH YVNNSKAVRE
AMCFLMDPEV GRDVCYVQFP QRFDGIDRSD RYANRNTVFF DVNMKGLDGI QGPVYVGTGC
VFNRQALYGY SPPSMPSLPR SSCCCCPSKK STTDGVYRNA KREELEAAVY NLKEIDNYDD
NERSMLISQM SFEKTFGLST VFIESTLMEN GGVPESADPS MLIKEAIHVI SCGYEEKTDW
GKEIGWIYGS VTEDILTGFK MQCRGWKSIY CMPLRPAFKG SAPINLSDRL HQVLRWALGS
VEIFLSRHCP LWYGFAGGRL KLLQRMAYIN TIVYPFTSLP LIAYCCLPAI CLLTGKFIIP
TLSNVASLLF LGLFLSIIIT SVLELRWSGV SIEDLWRNEQ FWVIGGVSAH LFAVFQGFLK
MLAGVDTNFT VTAKAAEDSE FGELYLVKWT TLLIPPTTLI IVNLVGVVAG FSDALNGGYE
SWGPLFGKVF FAFWVIFHLY PFLKGLMGRQ NRTPTIVILW SVLMASVFSL IWVKINPFVN
KVDSETLSET CIAIDC
//