CSLF1_ORYSJ
ID CSLF1_ORYSJ Reviewed; 860 AA.
AC Q6ZF89; Q944E2;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Putative mixed-linked glucan synthase 1;
DE EC=2.4.1.-;
DE AltName: Full=1,3/1,4-beta D-glucan synthase 1;
DE AltName: Full=Cellulose synthase-like protein F1;
DE AltName: Full=OsCslF1;
GN Name=CSFL1; OrderedLocusNames=Os07g0553000, LOC_Os07g36700;
GN ORFNames=P0013G11.6;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11842136; DOI=10.1104/pp.010875;
RA Hazen S.P., Scott-Craig J.S., Walton J.D.;
RT "Cellulose synthase-like genes of rice.";
RL Plant Physiol. 128:336-340(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
CC -!- FUNCTION: May catalyze both beta-1,3 and beta-1,4 glycosidic linkage on
CC beta-D-glucan. Essential for (1,3;1,4)-beta-D-glucans synthesis in
CC grasses and cereals (Poaceae). The mixed-linked glucans (which are not
CC present in walls of dicotyledons or most other monocotyledonous plants)
CC are particularly important constituents of the walls of the starchy
CC endosperm and aleurone cells of cereal grains such as oats, wheat, rice
CC and barley. They can account for up to 70% by weight of the wall (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Multi-
CC pass membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. Plant
CC cellulose synthase-like F subfamily. {ECO:0000305}.
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DR EMBL; AF432502; AAL25131.1; -; Genomic_DNA.
DR EMBL; AP004261; BAC83318.1; -; Genomic_DNA.
DR EMBL; AP014963; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_015645039.1; XM_015789553.1.
DR AlphaFoldDB; Q6ZF89; -.
DR SMR; Q6ZF89; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR PaxDb; Q6ZF89; -.
DR PRIDE; Q6ZF89; -.
DR GeneID; 107276327; -.
DR KEGG; osa:107276327; -.
DR InParanoid; Q6ZF89; -.
DR OrthoDB; 679241at2759; -.
DR Proteomes; UP000000763; Chromosome 7.
DR Proteomes; UP000059680; Chromosome 7.
DR Genevisible; Q6ZF89; OS.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0016760; F:cellulose synthase (UDP-forming) activity; IEA:InterPro.
DR GO; GO:0051753; F:mannan synthase activity; IBA:GO_Central.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0030244; P:cellulose biosynthetic process; IEA:InterPro.
DR GO; GO:0009833; P:plant-type primary cell wall biogenesis; IBA:GO_Central.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR005150; Cellulose_synth.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR Pfam; PF03552; Cellulose_synt; 2.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 3: Inferred from homology;
KW Cell wall biogenesis/degradation; Coiled coil; Glycosyltransferase;
KW Golgi apparatus; Membrane; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..860
FT /note="Putative mixed-linked glucan synthase 1"
FT /id="PRO_0000319401"
FT TRANSMEM 63..83
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 625..645
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 655..675
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 693..713
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 747..767
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 781..801
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 812..832
FT /note="Helical"
FT /evidence="ECO:0000255"
FT COILED 235..263
FT /evidence="ECO:0000255"
FT ACT_SITE 183
FT /evidence="ECO:0000255"
FT ACT_SITE 549
FT /evidence="ECO:0000255"
FT BINDING 381
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 383
FT /ligand="substrate"
FT /evidence="ECO:0000255"
SQ SEQUENCE 860 AA; 94970 MW; E40807C61CFC2BF8 CRC64;
MSAAAAVTSW TNGCWSPAAT RVNDGGKDDV WVAVDEADVS GARGSDGGGR PPLFQTYKVK
GSILHPYRFL ILARLIAIVA FFAWRIRHKN RDGAWLWTMS MVGDVWFGFS WVLNQLPKQS
PIKRVPDIAA LADRHSGDLP GVDVFVTTVD PVDEPILYTV NTILSILAAD YPVDRYACYL
SDDGGTLVHY EAMVEVAKFA ELWVPFCRKH CVEPRSPENY FAMKTQAYKG GVPGELMSDH
RRVRREYEEF KVRIDSLSST IRQRSDVYNA KHAGENATWM ADGTHWPGTW FEPADNHQRG
KHAGIVQVLL NHPSCKPRLG LAASAENPVD FSGVDVRLPM LVYISREKRP GYNHQKKAGA
MNVMLRVSAL LSNAPFVINF DGDHYVNNSQ AFRAPMCFML DGRGRGGENT AFVQFPQRFD
DVDPTDRYAN HNRVFFDGTM LSLNGLQGPS YLGTGTMFRR VALYGVEPPR WGAAASQIKA
MDIANKFGSS TSFVGTMLDG ANQERSITPL AVLDESVAGD LAALTACAYE DGTSWGRDVG
WVYNIATEDV VTGFRMHRQG WRSVYASVEP AAFRGTAPIN LTERLYQILR WSGGSLEMFF
SHSNALLAGR RLHPLQRVAY LNMSTYPIVT VFIFFYNLFP VMWLISEQYY IQRPFGEYLL
YLVAVIAMIH VIGMFEVKWA GITLLDWCRN EQFYMIGSTG VYPTAVLYMA LKLVTGKGIY
FRLTSKQTAA SSGDKFADLY TVRWVPLLIP TIVIMVVNVA AVGVAVGKAA AWGPLTEPGW
LAVLGMVFNV WILVLLYPFA LGVMGQWGKR PAVLFVAMAM AVAAVAAMYV AFGAPYQAEL
SGVAASLGKV AAASLTGPSG
