ID A0A087GIZ8_ARAAL Unreviewed; 1081 AA.
AC A0A087GIZ8;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Cellulose synthase {ECO:0000256|RuleBase:RU361116};
DE EC=2.4.1.12 {ECO:0000256|RuleBase:RU361116};
GN OrderedLocusNames=AALP_Aa7g186800 {ECO:0000313|EMBL:KFK29850.1};
OS Arabis alpina (Alpine rock-cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Arabideae; Arabis.
OX NCBI_TaxID=50452 {ECO:0000313|EMBL:KFK29850.1, ECO:0000313|Proteomes:UP000029120};
RN [1] {ECO:0000313|Proteomes:UP000029120}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Pajares {ECO:0000313|Proteomes:UP000029120};
RX PubMed=27246759; DOI=10.1038/nplants.2014.23;
RA Willing E.M., Rawat V., Mandakova T., Maumus F., James G.V.,
RA Nordstroem K.J., Becker C., Warthmann N., Chica C., Szarzynska B.,
RA Zytnicki M., Albani M.C., Kiefer C., Bergonzi S., Castaings L.,
RA Mateos J.L., Berns M.C., Bujdoso N., Piofczyk T., de Lorenzo L.,
RA Barrero-Sicilia C., Mateos I., Piednoel M., Hagmann J., Chen-Min-Tao R.,
RA Iglesias-Fernandez R., Schuster S.C., Alonso-Blanco C., Roudier F.,
RA Carbonero P., Paz-Ares J., Davis S.J., Pecinka A., Quesneville H.,
RA Colot V., Lysak M.A., Weigel D., Coupland G., Schneeberger K.;
RT "Genome expansion of Arabis alpina linked with retrotransposition and
RT reduced symmetric DNA methylation.";
RL Nat. Plants 1:14023-14023(2015).
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; CM002875; KFK29850.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A087GIZ8; -.
DR EnsemblPlants; KFK29850; KFK29850; AALP_AA7G186800.
DR Gramene; KFK29850; KFK29850; AALP_AA7G186800.
DR eggNOG; ENOG502QQJD; Eukaryota.
DR OMA; HESDGGT; -.
DR OrthoDB; 1210919at2759; -.
DR UniPathway; UPA00695; -.
DR Proteomes; UP000029120; Chromosome 7.
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:0042538; P:hyperosmotic salinity response; IEA:EnsemblPlants.
DR GO; GO:0009833; P:plant-type primary cell wall biogenesis; IEA:EnsemblPlants.
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:SF33; CELLULOSE SYNTHASE A CATALYTIC SUBUNIT 1 [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, ECO:0000256|RuleBase:RU361116};
KW Metal-binding {ECO:0000256|RuleBase:RU361116};
KW Reference proteome {ECO:0000313|Proteomes:UP000029120};
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 857..878
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361116"
FT TRANSMEM 890..908
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361116"
FT TRANSMEM 928..950
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361116"
FT TRANSMEM 971..999
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361116"
FT TRANSMEM 1011..1029
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361116"
FT TRANSMEM 1041..1061
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361116"
FT DOMAIN 31..105
FT /note="Cellulose synthase RING-type zinc finger"
FT /evidence="ECO:0000259|Pfam:PF14569"
FT REGION 115..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..172
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1081 AA; 122275 MW; 151395DFBF4DBB5B CRC64;
MEPSAGLVAG SYRRNELVRI RHESDGGPKA TKVNGQICQI CGDDVGHAET SDVFVACNEC
AFPVCRPCYE YERKDGTQCC PQCKTRYRRH RGCPRVEGDE DEDDVDDIEN EFNYAQGANK
ARLQRRGEEF SSSSRHESQP IPLLTHGHAV SGEIRTPDTQ SVRTTSGPLG PPDRNAISSP
YIDPRQPVPV RIVDPSKDLN SYGLGNVDWK ERVEGWKLKQ EKNMLQMTGK YHEGKGGEIE
GTGSNGEELQ MADDTRLPMS RIVPIPPSRL TPYRVVIILR LIILAFFLQY RTTHPVKNAY
PLWLTSVICE IWFAFSWLLD QFPKWYPINR ETYLDRLAIR FDRDGEPSQL TPVDVFVSTV
DPLKEPPLVT ANTVLSILAV DYPVDKVACY VSDDGSAMLT FESLSETAEF AKKWVPFCKK
FNIEPRAPEF YFAQKIDYLK DKIQPSFVKE RRAMKREYEE FKVRINALVF KAQKIPEEGW
TMQDGTPWPG NNTRDHPGMI QVFLGHSGGL DTDGNELPRL IYVSREKRPG FQHHKKAGAM
NALIRVSAVL TNGAYLLNVD CDHYFNNSKA IKEAMCFMMD PAYGKKCCYV QFPQRFDGID
LHDRYANRNI VFFDINLKGL DGIQGPVYVG TGCCFNRQAL YGYDPVLTEE DLEPNIIVKS
CCGSRKKSKN SKKYNYDQKR RGITRSDSNA PLFNMEDIDE GFEGYDDERS ILMSQKSVEK
RFGQSPVFIA ATFMEQGGIP PTTNPATLLK EAIHVISCGY EDKTEWGKEI GWIYGSVTED
ILTGFKMHAR GWMSIYCNPP RPAFKGSAPI NLSDRLNQVL RWALGSIEIL LSRHCPIWYG
YTGRLKLLER IAYINTIVYP ITAIPLIAYC ILPAFCLITD RFIIPEISNY ASIWFILLFI
SIAVTGILEL RWSGVSIEDW WRNEQFWVIG GTSAHLFAVF QGLLKVLAGI DTNFTVTSKA
SDEDGDFAEL YIFKWTALLI PPTTVLLVNL IGIVAGVSYA VNSGYQSWGP LFGKLFFALW
VIAHLYPFLK GLLGRQNRTP TIVIVWSVLL ASIFSLLWVR INPFVDANPN ANNFNGQGGN
F
//
