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Database: UniProt
Entry: M1A914_SOLTU
LinkDB: M1A914_SOLTU
Original site: M1A914_SOLTU 
ID   M1A914_SOLTU            Unreviewed;       764 AA.
AC   M1A914;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   24-JAN-2024, entry version 54.
DE   RecName: Full=Cellulose synthase {ECO:0000256|RuleBase:RU361116};
DE            EC=2.4.1.12 {ECO:0000256|RuleBase:RU361116};
OS   Solanum tuberosum (Potato).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX   NCBI_TaxID=4113 {ECO:0000313|EnsemblPlants:PGSC0003DMT400017531, ECO:0000313|Proteomes:UP000011115};
RN   [1] {ECO:0000313|Proteomes:UP000011115}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. DM1-3 516 R44 {ECO:0000313|Proteomes:UP000011115};
RX   PubMed=21743474; DOI=10.1038/nature10158;
RG   The Potato Genome Sequencing Consortium;
RT   "Genome sequence and analysis of the tuber crop potato.";
RL   Nature 475:189-195(2011).
RN   [2] {ECO:0000313|EnsemblPlants:PGSC0003DMT400017531}
RP   IDENTIFICATION.
RC   STRAIN=DM1-3 516 R44 {ECO:0000313|EnsemblPlants:PGSC0003DMT400017531};
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; M1A914; -.
DR   EnsemblPlants; PGSC0003DMT400017531; PGSC0003DMT400017531; PGSC0003DMG400006799.
DR   Gramene; PGSC0003DMT400017531; PGSC0003DMT400017531; PGSC0003DMG400006799.
DR   UniPathway; UPA00695; -.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   ExpressionAtlas; M1A914; baseline and differential.
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   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; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR13301:SF206; CELLULOSE SYNTHASE A CATALYTIC SUBUNIT 8 [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.
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};
KW   Metal-binding {ECO:0000256|RuleBase:RU361116};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011115};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361116};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361116};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|RuleBase:RU361116}.
FT   DOMAIN          10..86
FT                   /note="Cellulose synthase RING-type zinc finger"
FT                   /evidence="ECO:0000259|Pfam:PF14569"
FT   REGION          70..103
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          665..686
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   764 AA;  85002 MW;  DF1DC245EAD102BB CRC64;
     MDPEGDVKGK SLKTLGGQVC QICGDGVGTT VNGEPFVACD VCAFPVCRPC YEYERKDGNQ
     SCPQCKTRYK RHKGSPAISG ESVEDGDADD GASELNYSSE NLNEKQKVAD RVLSWHATYG
     RGEETGAPKY DKEVSHNHIP LLTNGTDVSG ELSAASPERY SMASPGPAGG AKHIHPLTYS
     TDANQSPNIR VVDPVREFGS PGLGNVAWKE RVDGWKMKQD KNVVPMTTSH PPSERGVGDI
     DASTDILGDD SLLNDEARQP LSRKVSIPSS RINPYRMVIV LRLVILCIFL HYRIMNPVPN
     AIPLWLLSVI CEIWFAVSWI LDQFPKWLPI NRETYLDRLA LRYDREGEPS QLAAVDIFVS
     TVDPLKEPPL VTANTVLSIL AVDYPVDKVS CYVSDDGAAM LTFEALSETA EFARKWVPFS
     KKYSIEPRAP EWYFSQKVDY LKDKVQTSFV KDRRAMKREY EEFKIRINAL VAKAQKVPEE
     GWIMQDGTPW PGNNTRDHPG MIQVFLGQSG GLDSDGNELP RLVYVSREKR PGFQHHKKAG
     AMNALVRVSA VLTNGPFMLN LDCDHYINNS KALREAMCFL MDPNLGKYVC YVQFPQRFDG
     IDRNDRYANR NTVFFDINLR GLDGIQGPVY VGTGCVFNRT ALYGYEPPIK PKHKKAGFLS
     SCFGGSRKKG SKSSKKGSDK KKSSKNVDPT VPIFNLEDIE EGVEGIVQIT KSFHFMLSLS
     KYFTNPRMIT LMLYTTPYSA TPFSKLIGKA VASSAKKKGK IASC
//
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