CSLF7_ORYSJ
ID CSLF7_ORYSJ Reviewed; 830 AA.
AC Q94GM9; A0A0P0XT19; Q7E0V9; Q7XFJ8;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Probable mixed-linked glucan synthase 7;
DE EC=2.4.1.-;
DE AltName: Full=1,3;1,4-beta-D-glucan synthase 7;
DE AltName: Full=Cellulose synthase-like protein F7;
DE AltName: Full=OsCslF7;
GN Name=CSLF7; OrderedLocusNames=Os10g0343400, LOC_Os10g20260;
GN ORFNames=OSJNBb0052C09.2;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12791992; DOI=10.1126/science.1083523;
RA Yu Y., Rambo T., Currie J., Saski C., Kim H.-R., Collura K., Thompson S.,
RA Simmons J., Yang T.-J., Nah G., Patel A.J., Thurmond S., Henry D.,
RA Oates R., Palmer M., Pries G., Gibson J., Anderson H., Paradkar M.,
RA Crane L., Dale J., Carver M.B., Wood T., Frisch D., Engler F.,
RA Soderlund C., Palmer L.E., Teytelman L., Nascimento L., De la Bastide M.,
RA Spiegel L., Ware D., O'Shaughnessy A., Dike S., Dedhia N., Preston R.,
RA Huang E., Ferraro K., Kuit K., Miller B., Zutavern T., Katzenberger F.,
RA Muller S., Balija V., Martienssen R.A., Stein L., Minx P., Johnson D.,
RA Cordum H., Mardis E., Cheng Z., Jiang J., Wilson R., McCombie W.R.,
RA Wing R.A., Yuan Q., Ouyang S., Liu J., Jones K.M., Gansberger K.,
RA Moffat K., Hill J., Tsitrin T., Overton L., Bera J., Kim M., Jin S.,
RA Tallon L., Ciecko A., Pai G., Van Aken S., Utterback T., Reidmuller S.,
RA Bormann J., Feldblyum T., Hsiao J., Zismann V., Blunt S., de Vazeille A.R.,
RA Shaffer T., Koo H., Suh B., Yang Q., Haas B., Peterson J., Pertea M.,
RA Volfovsky N., Wortman J., White O., Salzberg S.L., Fraser C.M., Buell C.R.,
RA Messing J., Song R., Fuks G., Llaca V., Kovchak S., Young S., Bowers J.E.,
RA Paterson A.H., Johns M.A., Mao L., Pan H., Dean R.A.;
RT "In-depth view of structure, activity, and evolution of rice chromosome
RT 10.";
RL Science 300:1566-1569(2003).
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=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [4]
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).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [6]
RP IDENTIFICATION.
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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Zhonghua 10; TISSUE=Pollen;
RX PubMed=16548068; DOI=10.1002/pmic.200401351;
RA Dai S., Li L., Chen T., Chong K., Xue Y., Wang T.;
RT "Proteomic analyses of Oryza sativa mature pollen reveal novel proteins
RT associated with pollen germination and tube growth.";
RL Proteomics 6:2504-2529(2006).
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 -!- TISSUE SPECIFICITY: Expressed in mature pollen.
CC {ECO:0000269|PubMed:16548068}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. Plant
CC cellulose synthase-like F subfamily. {ECO:0000305}.
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DR EMBL; AC090441; AAK91320.1; -; Genomic_DNA.
DR EMBL; DP000086; AAP53148.1; -; Genomic_DNA.
DR EMBL; AP008216; BAF26304.1; -; Genomic_DNA.
DR EMBL; AP014966; BAT10422.1; -; Genomic_DNA.
DR EMBL; AK110467; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BK000091; DAA01754.1; -; Genomic_DNA.
DR RefSeq; XP_015614348.1; XM_015758862.1.
DR AlphaFoldDB; Q94GM9; -.
DR SMR; Q94GM9; -.
DR STRING; 4530.OS10T0343400-01; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR PaxDb; Q94GM9; -.
DR PRIDE; Q94GM9; -.
DR EnsemblPlants; Os10t0343400-01; Os10t0343400-01; Os10g0343400.
DR GeneID; 4348365; -.
DR Gramene; Os10t0343400-01; Os10t0343400-01; Os10g0343400.
DR KEGG; osa:4348365; -.
DR eggNOG; ENOG502QU14; Eukaryota.
DR HOGENOM; CLU_001418_3_1_1; -.
DR InParanoid; Q94GM9; -.
DR OMA; VVHLYPF; -.
DR OrthoDB; 679241at2759; -.
DR Proteomes; UP000000763; Chromosome 10.
DR Proteomes; UP000059680; Chromosome 10.
DR Genevisible; Q94GM9; 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 1: Evidence at protein level;
KW Cell wall biogenesis/degradation; Coiled coil; Glycosyltransferase;
KW Golgi apparatus; Membrane; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..830
FT /note="Probable mixed-linked glucan synthase 7"
FT /id="PRO_0000319407"
FT TRANSMEM 61..81
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 98..118
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 613..633
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 638..658
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 676..696
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 735..755
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 776..796
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 805..825
FT /note="Helical"
FT /evidence="ECO:0000255"
FT COILED 251..279
FT /evidence="ECO:0000255"
FT ACT_SITE 186
FT /evidence="ECO:0000255"
FT ACT_SITE 529
FT /evidence="ECO:0000255"
FT BINDING 367
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 369
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT CONFLICT 125
FT /note="M -> T (in Ref. 5; AK110467)"
FT /evidence="ECO:0000305"
FT CONFLICT 154
FT /note="P -> L (in Ref. 5; AK110467)"
FT /evidence="ECO:0000305"
FT CONFLICT 775
FT /note="A -> V (in Ref. 5; AK110467)"
FT /evidence="ECO:0000305"
FT CONFLICT 829
FT /note="T -> M (in Ref. 5; AK110467)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 830 AA; 89399 MW; 7148B5F151FFE895 CRC64;
MPPSAGLATE SLPAATCPAK KDAYAAAASP ESETKLAAGD ERAPLVRTTR ISTTTIKLYR
LTIFVRIAIF VLFFKWRITY AARAISSTDA GGIGMSKAAT FWTASIAGEL WFAFMWVLDQ
LPKTMPVRRA VDVTALNDDT LLPAMDVFVT TADPDKEPPL ATANTVLSIL AAGYPAGKVT
CYVSDDAGAE VTRGAVVEAA RFAALWVPFC RKHGVEPRNP EAYFNGGEGG GGGGKARVVA
RGSYKGRAWP ELVRDRRRVR REYEEMRLRI DALQAADARR RRCGAADDHA GVVQVLIDSA
GSAPQLGVAD GSKLIDLASV DVRLPALVYV CREKRRGRAH HRKAGAMNAL LRASAVLSNA
PFILNLDCDH YVNNSQALRA GICFMIERRG GGAEDAGDVA FVQFPQRFDG VDPGDRYANH
NRVFFDCTEL GLDGLQGPIY VGTGCLFRRV ALYGVDPPRW RSPGGGVAAD PAKFGESAPF
LASVRAEQSH SRDDGDAIAE ASALVSCAYE DGTAWGRDVG WVYGTVTEDV ATGFCMHRRG
WRSAYYAAAP DAFRGTAPIN LADRLHQVLR WAAGSLEIFF SRNNALLAGG RRRLHPLQRA
AYLNTTVYPF TSLFLMAYCL FPAIPLIAGG GGWNAAPTPT YVAFLAALMV TLAAVAVLET
RWSGIALGEW WRNEQFWMVS ATSAYLAAVA QVALKVATGK EISFKLTSKH LASSATPVAG
KDRQYAELYA VRWTALMAPT AAALAVNVAS MAAAGGGGRW WWWDAPSAAA AAAAALPVAF
NVWVVVHLYP FALGLMGRRS KAVRPILFLF AVVAYLAVRF LCLLLQFHTA