ID M1CRI1_SOLTU Unreviewed; 998 AA.
AC M1CRI1;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 24-JAN-2024, entry version 65.
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:PGSC0003DMT400073084, 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:PGSC0003DMT400073084}
RP IDENTIFICATION.
RC STRAIN=DM1-3 516 R44 {ECO:0000313|EnsemblPlants:PGSC0003DMT400073084};
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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU361116}.
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DR AlphaFoldDB; M1CRI1; -.
DR SMR; M1CRI1; -.
DR STRING; 4113.M1CRI1; -.
DR PaxDb; 4113-PGSC0003DMT400073084; -.
DR EnsemblPlants; PGSC0003DMT400073084; PGSC0003DMT400073084; PGSC0003DMG400028426.
DR Gramene; PGSC0003DMT400073084; PGSC0003DMT400073084; PGSC0003DMG400028426.
DR eggNOG; ENOG502QTVZ; Eukaryota.
DR HOGENOM; CLU_001418_0_0_1; -.
DR InParanoid; M1CRI1; -.
DR OMA; CATPYDE; -.
DR UniPathway; UPA00695; -.
DR Proteomes; UP000011115; Unassembled WGS sequence.
DR ExpressionAtlas; M1CRI1; baseline and differential.
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 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; 2.
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:UP000011115};
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 775..795
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361116"
FT TRANSMEM 807..825
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361116"
FT TRANSMEM 845..865
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361116"
FT TRANSMEM 886..911
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361116"
FT TRANSMEM 923..945
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361116"
FT TRANSMEM 957..977
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 117..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 998 AA; 113370 MW; 48329E0B59440C5F CRC64;
MESGVPICNI CGEQVGLANN NGEVFVACHE CNYPVCKTCI DYEIKEGRNT CLRCATPYDE
NEQESTNHAI VASHPDTAQD AGVHARTVSF VSTVDSEYHD DTGNPIWKNR VESWKEKKNK
KKKNQSKAVV QEAAEVPPEQ QMEEKPQLAD AAEPLSRIIP VPKSQITPYR IVIIVRLIVL
CFFFHYRVTH PVESAYPLWF TSVFCEIWFA FSWVLDQFPK WSPINRETYL DRLSARYERE
GEPCQLAPVD FFVSTVDPMK EPPLITANTV LSILAVDYPV EKVSCYVSDD GGSMLTFESL
AETSEFARKW VPFCKKFSIE PRAPEFYFTQ KFDYLKDKVQ PSFVKERRAM KREYEEYKVR
VNALVAKAQK TPEDGWTMAD GTPWPGNNPR DHPGMIQVFL GHSGVHDIEG NELPRLVYVS
REKRPGYQHH KKAGAENALI RVSAVLTNAP YILNLDCDHY VNNSKAIREA MCFLMDPQVG
RDVCYVQFPQ RFDGIDKSDR YANRNIVFFD VNMKGLDGIQ GPVYVGTGTV FNRQALYGYS
PSNLPTIHKS SSSFSCCCRR KKPAKEKDLT EVYREAKRED LNSAIFNLRE IENYDDHERS
LLISQMSFEK TFGMSSVFIE STLMENGGVP DSANPSTLIR EAIHVIGCGY EEKTAWGKEV
KIESLFWFHI WKEGANTFLF VCPFQIGWIY GSVTEDILTG FKMQCRGWRS IYCMPLRPAF
KGSAPINLSD RLHQVLRWAL GSVEIFLSRH CPLWYGFGGG RLKWLQRLAY TNTIVYPFTS
LPLIAYCILP AVCLLTGKFI IPTLSNVASI LFLGLFLSII VTSVLELRWS GIGIEDWWRN
EQFWVIGGVS AHLFAVFQGF LKMLAGIDTN FTVTTKAADD GEFADLYLFK WTTVLIPPTT
ILIVNLVGVV AGFSDALNKG YEAWGPLFGK VFFSFWVILH LYPFLKGLMG RQNRTPTIVV
LWSVLLASVF SLVWVKINPF VSKDDPSAMV QNCIDMDC
//
