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Database: UniProt
Entry: V7CR98_PHAVU
LinkDB: V7CR98_PHAVU
Original site: V7CR98_PHAVU 
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
//
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